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3 THE DIVINITY OF JESUS CHRIST A study in the history of Christian doctrine since Kant Hulsean Lectures, igj6 by JOHN MARTIN CREED, D.D. Ely Professor of Divinity in the University of Cambridge, Fellow of St John's College CAMBRIDGE AT THE UNIVERSITY PRESS 1938
4 cambridge university press Cambridge, New York, Melbourne, Madrid, Cape Town, Singapore, São Paulo, Delhi, Tokyo, Mexico City Cambridge University Press The Edinburgh Building, Cambridge cb2 8ru, UK Published in the United States of America by Cambridge University Press, New York Information on this title: / Cambridge University Press 1938 This publication is in copyright. Subject to statutory exception and to the provisions of relevant collective licensing agreements, no reproduction of any part may take place without the written permission of Cambridge University Press. First published 1938 First paperback edition 2011 A catalogue record for this publication is available from the British Library isbn Paperback Cambridge University Press has no responsibility for the persistence or accuracy of URLs for external or third-party internet websites referred to in this publication, and does not guarantee that any content on such websites is, or will remain, accurate or appropriate.
5 To MY WIFE
7 CONTENTS CONTENTS Preface page ix I. Introductory i II. The Christology of Romanticism 19 III. Process and Incarnation 4i IV. Greeds, Confessions and the new Learning 62 V. The fact of Christ 83 VI. The problem of Revelation 103 VII. The Divinity of Jesus Christ 119 Index of names 145
9 PREFACE This book includes the substance of the six lectures which I delivered in Cambridge as Hulsean Lecturer in the Lent Term Except for some few modifications and expansions I have reproduced the first five lectures in the form in which I delivered them. The sixth lecture I have entirely recast, using the material in the sixth and seventh sections of this book. I frequently discussed the subject-matter of these lectures with my friend and colleague, the Rev. J. S. Boys Smith, both at the time when I was preparing them for delivery, and again later when I was revising them for publication. I am much indebted to those conversations, though of course I am alone responsible for the opinions which I express. Mr Boys Smith has further enhanced my obligations to him by suggesting a number of amendments at the proof stage. I wish also to acknowledge help in reading the proofs which I have received from my father-in-law Canon A. L. Lilley, and from my wife. I have followed the usage of the English Bible in the printing of pronouns and relatives which refer to God and to Jesus Christ, except that in quoting from other writers I have reproduced their own usage. My subject is of course a very large one and the treatment of it has of necessity been selective. I am well aware that there are gaps and that some not inconsiderable theologians who have dealt with the doctrine
10 x Preface of the Person of Christ in the course of the last century and a half are not even mentioned. But I believe that I have discussed representatives of all the main tendencies in Christological doctrine within the period. J. M. GREED THE COLLEGE ELY March 1938
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An atmosphere (atm) was a unit of measurement for pressure, defined by the force exerted by the weight of air molecules in an atmosphere.
Comparative units of pressure
When Jonathan Archer chose to interrogate the Osaarian pirate Orgoth for information about the Xindi in 2153, he place the Osaarian into an airlock and began to decompression it at a rate of 0.5 atmospheres per minute until his captive would start talking. He warned Orgoth that he better start soon or "in about forty seconds you won't be able to." (ENT: "Anomaly")
The Federation typically measured the atmospheric pressure of planets they encountered by relating to "Earth normal". (TAS: "The Eye of the Beholder") The atmospheric pressure of the habitats aboard the Nyrian biosphere vessel, encountered by USS Voyager in 2373, were kept at an Earth-normal atmosphere or 1 atm. (VOY: "Displaced")
When Mira Romaine became possessed by the Zetarians in 2269, she was placed in the pressure chamber where she was subjected to increased pressure. James T. Kirk ordered it pressure chamber to start at 2 atmospheres, then had it increase 1 atmosphere per second until it reached roughly 3.5 atmospheres, when they were finally forced from her body. (TOS: "The Lights of Zetar")

subset: commoncrawl


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Bury St Edmunds clinics join forces for Macmillan Coffee Morning
Bury Physio Clinic
Two Bury St Edmunds businesses are joining forces for a Macmillan coffee morning.
Bury Physio and Working Towards Wellbeing will be hosting an event on Friday, September 28 for the cancer charity's World's Biggest Coffee Morning fundraising campaign.
The event will run from 10.30am to 12pm at the premises the companies share in Maynewater Lane.
Anna Clayton, lead physio at the clinic, said: "Health and wellbeing are close to our heart. Raising money for such a worthy cause is a great way to get involved with the local community and support the fantastic work of the Macmillan nurses."
Working Towards Wellbeing partner Dr Julie Denning said: "We are continually using the Macmillan expertise and resources to help and support our patients, and so it is lovely to be able to give something back to the charity – and what better way than through cake and a chat."
If you value what this story gives you, please consider supporting the Eastern Daily Press. Click the link in the orange box above for details.


text:
Got tagged again from leng lui Huei. It is about what is inside your bag. Huei, since i don't carry a bag like all 'si lai' do, all i can show you is my 'kung si pau' wokeh?
Things inside my bag which includes:-
1). My cash sales book - While on the road, if got sales i use this cash book. No time to go back opis to print invoice la.
2). My insurance policy - car and life insurance. This is where kills me. Bulan-bulan bayar and yearly bayar. Pay until leg cramp ledi. Not only this kena bayar others things also ler.
3). Name card - Opis mia name card and Yinsi Yat mia name card. kekeke
4). Thumb drive - 1GB removable thumb drive just in case got porn to download!! kakaka
5). Passport - Must have this with me just in case all the ahlongs come and find me.!! Liddat can 'cheok choh' faster ma lol.
6). BirthCert - I Dunno why i always carry this with me.
7). Cheque book - This cheque book is to con people wan. Take goods issue bounce cheque. Mana mau cari!!!
8). Pens - My magic pen. Mali-mali humm!!
Hahahaha...that all you can find in my bag. Nothing much you can see in my bag ler. Okay, kau tim your tag. sau kung! Not tagging anyone this time round. hehehe.


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And I watch as the last blue rectangle of the wall in front of me disappears.
I have been here for a hundred years and I am going to stay here for another thousand. I am a prisoner. Unlike Kafka's The Trial, I am not here for a crime I have not committed but I was born here. This has been my home and haven ever since. I have seen more than any people, more than a blind. I know more about this room than the hands and heads that constructed it. I know the place better than the insects and souls that inhabit this room. I know this world; as it has been before me and as it is now. But alas, I am a prisoner.
I have no visitors, never. And I like it. I have seen the death of the person who shared this room with me. I have seen the body rot, decay. I have seen the flesh invite guests to the feast, and I have seen the greedy ones licking the bones until the bones starts to eat them up. The bones lie in a heap round the corner. They take up an unusually huge space of this small room and at times I have such a dislike for the dirt that I want to throw it off the window, but the bones are my only connection to the world outside. I am locked and I have the only room to walk around, but I do not complain, I don't have the habit. Wait, I do have visitors or a visitor, I know, although I have never seen anyone get in or stand outside my wooden bars, but they do come, I know. Whenever I fall asleep (and I have tried a million times not to fall asleep for reasons obvious), someone comes, I know because when I wake up I find a book lying on the floor of my room. But you don't believe what you've not seen, hence I have no visitors. The books now cover the wall in front of me and my room is getting smaller, not that I care about it. The only thing that I care about is my Life; the ambiguity of it. I am not afraid to die, but death comes slow to people like me, and that is the only sane reason I don't wait for it, neither do I run away from the claws of Death. I have seen Death and have felt it knock on the walls of my heart. I think Death is my only true friend, every time I think about Life Death puts a hand on my burning head and lulls me to sleep, whispers in my ear that Life isn't something I should think about, Life is leaving me each day, it isn't faithful. I believe what Death says because Death is the only one who stays with me. It talks to me, gives me company and promises to stay. Death has no end.
The window in my room is high up almost touching the ceiling that holds the lone light bulb. It is not a ventilator, it is a window. I haven't been to other houses and rooms but I know what a window is. The only thing the window sees is the small piece of the vast blue sky and black night. The only thing the window does is glare, sometimes at me and mostly at things that it is not. I think the window is the only head that has eyes on either side of it. It looks out at the open world outside and at the closed room where I stay, at the same time. The window brings in the freshness of the nature (sometimes it is very difficult to control the obstreperous wind that comes from outside) and takes away the staleness of the inside. The window is an essential part of the room, it is the way to dispose of the things I no longer want in the room; it's a gargoyle in the shape of a window. I wish I could write someday and throw the pages from the window for the world to read, but I cannot, I don't know how to write and therefore I think and send my thoughts flying out of the window, I don't know if anyone has caught them and read. But I know it has passed by everyone, poking them. They don't care about it, because empiricism doesn't hold true with me, I have no observations and experiences, I am confined to this room that has no existence, that has no address. Well, I don't need an address. But you will, if you want to visit me.
I don't want a name. I don't have a name. But you will want me to have a name if you want to call me.
The above page still hangs by loose threads in the diary, Kashiv's diary, Delirium.
Image courtesy : http://www.google.com


text:
The ability of a serotype M1 strain of Streptococcus pyogenes to efficiently invade A549 human lung epithelial cells was previously shown to be dependent on bacterial exposure to human or bovine serum proteins or synthetic peptides containing the sequence RGD. In this study, stimulation by invasion agonists was determined to be dependent on expression of the streptococcal cell surface protein, M1. Fetal bovine serum (FBS), fibronectin (Fn), the extracellular matrix protein laminin (Lm), and RGD-containing peptides were tested for their abilities to promote epithelial cell invasion and adherence by isogenic M1+ and M1− strains of S. pyogenes. In the absence of an agonist, invasion and adherence were comparable for the two bacterial strains. FBS, Fn, and Lm stimulated invasion of the M1+ strain as much as 70-fold but failed to significantly affect invasion by the M1−mutant. Adherence of the wild-type strain was stimulated by these same agonists. Epithelial cell adherence by the M1− strain, however, was unaffected by the presence of Fn or Lm. Several RGD-containing peptides were found to promote invasion independently of M1 expression. Binding of 125I-Fn was reduced 88% by the M1− mutation and Fn was found to bind purified M1 protein, suggesting that Fn mediates invasion by direct binding to M1. To determine if host integrins might be involved in internalization of streptococci, several anti-integrin monoclonal antibodies (MAbs) were tested for their abilities to inhibit invasion. Antibody directed against integrin β1 inhibited FBS-, Fn-, and Lm-mediated invasion but did not abrogate RGD-peptide-stimulated invasion. MAb directed against the epithelial cell Fn receptor, integrin α5β1, inhibited Fn and FBS-mediated invasion but did not specifically inhibit Lm-mediated invasion. These results indicate that S. pyogenes has evolved multiple mechanisms for invasion of eukaryotic cells, at least two of which involve interactions between M1 protein, host integrins, and integrin ligands.
Previous studies have demonstrated that the gram-positive human pathogen Streptococcus pyogenesis capable of invading and persisting within cultured human cells (18, 24, 30, 31, 37). Moreover, intracellular streptococci have been observed in tonsils removed from children with a history of recurrent pharyngitis (36). The capacity of S. pyogenes to invade host cells may provide a mechanism whereby the organism can gain access to deep tissues and blood. Intracellular streptococci may also be afforded at least partial protection from host defenses and antibiotics. The latter may contribute to the frequent recovery of S. pyogenes from throats of patients following a full 10-day course of penicillin treatment (16).
A number of bacterial pathogens (e.g., Listeria monocytogenes, Yersinia pseudotuberculosis [12, 13], Staphylococcus aureus [3],Neisseria gonorrhoeae [11, 17], andMycobacterium spp. [26, 43]) are proficient at invading cultured cells. Although pathogens have evolved a number of strategies for intracellular invasion, some common themes have emerged (12, 13). For example, with the exception of S. aureus, invasion by the aforementioned bacteria has been shown to depend on expression of specific, bacterial cell surface proteins. In the case of S. pyogenes, multiple cell surface-exposed proteins have been implicated in the invasion process. In separate studies, the closely related fibronectin (Fn)-binding proteins Sfbl (31) and protein F (24) were found, at least in part, to mediate streptococcal invasion of HEp2 cells.
M protein is an important virulence factor expressed on the surface ofS. pyogenes cells. Although there are more than 80 known serotypes of M protein, all are alpha-helical coiled-coil molecules capable of binding numerous plasma proteins (14). Two recent reports have demonstrated that at least two M proteins, serotypes 1 and 6, play roles in intracellular invasion by S. pyogenes(10a, 24). Recently, our laboratory found that intracellular invasion by a highly invasive M1 strain (strain 90-226) is heavily dependent on expression of M1 (10a). Invasion by this same strain was also shown to be equally dependent on bacterial exposure to mammalian serum proteins or small synthetic peptides containing the tripeptide sequence RGD (10).
Intracellular invasion by several bacterial pathogens is stimulated by microbial binding of mammalian serum/extracellular matrix (ECM) proteins such as vitronectin (11, 17), laminin (Lm) (43), or Fn (26, 47). Eukaryotic cells bind to ECM proteins via integrins, a family of heterodimeric transmembrane receptors (22). Integrins are utilized by enteropathogenicYersinia species for entry into mammalian cells.Yersinia internalization is mediated by invasin, a bacterial cell surface protein with a high affinity for β1 integrins. Invasion binding to integrins results in activation of host cell signal transduction pathways, which leads to actin-mediated "zipper phagocytosis" of adherent bacteria (13, 23, 51). It seems likely that ECM protein-dependent intracellular invasion by pathogens occurs via a similar mechanism. In the latter case, however, engagement of eukaryotic receptors appears dependent on binding of ECM proteins to the surface of bacteria. The bound protein, in turn, binds to its cognate receptor on the surface of a host cell.
S. pyogenes 90-226 is a representative of a widely disseminated subclone of the M1 serotype (8, 32). This highly virulent subclone was demonstrated to invade epithelial cells at an unusually high frequency relative to other serotype M1 isolates (7, 30). Since strain 90-226 lacks the genes coding for protein F and Sfbl (33), the mechanism whereby it invades epithelial cells clearly must differ from that described for less virulent S. pyogenes isolates. Experiments described here demonstrate that both Fn and Lm promote high-frequency invasion by strain 90-226, apparently by fostering bacterial interaction with distinct epithelial cell integrins. Moreover, the ability of either agonist to facilitate invasion is dependent on bacterial expression of M1 protein. In contrast, invasion stimulated by RGD-containing peptides was found to be M1 independent. This study demonstrates that strain 90-226 has evolved at least three distinct pathways for invasion of human epithelial cells.
Bacterial strains, plasmids, and culture media. S. pyogenes 90-226, a serotype M1 strain cultured from the blood of a patient with sepsis (10, 30), was obtained from the WHO Center for Reference and Research on Streptococci at the University of Minnesota. Strain 90-226 emm1::Km was constructed by insertional inactivation of emm1 with theaphA-3 (kanamycin resistance) gene (10a).S. pyogenes JRS4, which produces a type 6 M protein, and SAM1, an isogenic protein F− derivative of JRS4, were provided by M. Caparon (20). S. pyogenes AP1, which expresses a serotype M1 protein, was provided by L. Björck (15). Escherichia coli DH11S (Life Technologies Inc., Gaithersburg, Md.) served as the host for cloning experiments and plasmid maintenance. The protease-deficient E. coli strain BL21 (Novagen Inc., Madison, Wis.) was used for expression of the M42-382 fragment of M1 protein encoded by plasmid pM42-382.
Streptococci were grown in Todd-Hewitt broth supplemented with 2% neopeptone (Difco Laboratories, Detroit, Mich.). Solid media for streptococci were Todd-Hewitt broth or sheep blood agar. E. coli was grown in Luria-Bertani broth (LB) (45). Solid media contained 1.5% agar. The plasmid vectors pSport1 and pCYB4 were obtained from Life Technologies and New England Biolabs (Beverly, Mass.), respectively. Plasmid pMYB129, encoding an E. colimaltose-binding–intein fusion protein, was from New England Biolabs. Construction of plasmids pemm1 and pM42-382 is described below.
Proteins antibodies and peptides.Human fibrinogen (Fg) was obtained from Chromogenix Corp. (Molndal, Sweden). Human plasma Fn was obtained from Sigma Chemical Co. and Life Technologies. Mouse laminin-1 (mouse Lm) and human placental laminin (HLm) were purchased from Life Technologies. Monoclonal antibodies (MAbs) against integrins β1 and α5β1 were purchased from Life Technologies and Chemicon International Inc. (Temecula, Calif.), respectively. Other MAbs recognizing integrin subunits were generously provided by the following University of Minnesota researchers: anti-integrin α2 and α3, P. Southern; anti-integrin α5 and α6, J. McCarthy; anti-integrin β2, Y. Schimizu; and anti-integrin β4, A. Skubitz. Sheep anti-human Fn antibody (Ab) was purchased from ICN Pharmaceuticals, Costa Mesa, Calif. Alkaline phosphatase conjugated to mouse anti-sheep immunoglobulin G (IgG) was from Sigma.
The six-amino-acid peptide GRGDTP was purchased from Sigma. The cyclic (N-acetyl-l-penicillamine-RGDC) RGD and RGDS peptides were purchased from Bachem California Inc. (Torrance, Calif.). Lyophilized peptides were dissolved in RPMI 1640 medium and filter sterilized; aliquots were stored at −80°C.
Cell culture and epithelial cell invasion assay.A549 human lung epithelial cells (ATCC CCL 185) were cultured in RPMI 1640 medium supplemented with 10% fetal bovine serum (FBS; Life Technologies). Cultures of A549 cells were maintained in medium containing penicillin (5 μg/ml) and streptomycin (100 μg/ml) (Sigma).
Assays of bacterial invasion and adherence were performed as previously described (10, 30). Assays were performed in unsupplemented RPMI 1640 medium or medium containing 10% FBS (RPMI-FBS), Fg (25 μg/ml), Fn (10 μg/ml), or mouse Lm (10 μg/ml). In some experiments, RPMI 1640 medium was supplemented with 10 μg of HLm per ml in place of mouse Lm. Monolayers of A549 cells (≅2 × 105 cells/well) were infected with 1 × 105 to 5 × 105 bacterial CFU and incubated for 2 h at 37°C in 5% CO2–95% air. Infected monolayers were then washed three times with 1 ml of Hanks balanced salt solution (HBSS) before RPMI-FBS containing gentamicin (100 μg/ml) and penicillin (5 μg/ml) was added. Following 2 h of incubation at 37°C, the monolayers were washed with HBSS, dispersed by the addition of 0.2 ml of 0.25% trypsin–1 mM EDTA (Life Technologies), and then lysed by dilution into 0.8 ml of sterile distilled H2O. The numbers of bacterial CFU released from the lysed epithelial cells were determined by plating of diluted lysates on Todd-Hewitt agar. Typically, less than 5 × 10−3% of input bacteria survive exposure to antibiotics in the absence of epithelial cells, and survival is unaffected by the presence of invasion agonists or the emm1::Km mutation.
To measure bacterial adherence, culture media were removed from monolayers at the end of the invasion period and discarded. The monolayers were then washed three times with HBSS to remove nonadherent bacteria. Epithelial cells were dispersed and lysed, and bacteria were plated as described above. While the numbers of CFU recovered from these wells is reflective of the number of adherent and internalized CFU, for simplicity we will refer to these bacteria as adherent CFU. The statistical significance of data was determined by Student'st test, using Microsoft Excel 97 software. Pvalues of <0.005 were considered significant.
Poly-l-lysine-coated plates were used in invasion experiments that involved the addition of anti-integrin MAbs. One milliliter of poly-l-lysine (0.1 mg/ml; 30 to 70 kDa; Sigma) was added to each well of 24-well tissue culture plates, and the plates were incubated for 10 min at room temperature. The solution was then aspirated from the wells, and each well was washed three times with 1 ml of sterile distilled water. Plates were dried in a laminar-flow hood prior to inoculation with A549 cells.
DNA techniques.Plasmid DNA was isolated from E. coli strains by the alkaline lysis method (45).S. pyogenes chromosomal DNA was isolated as described previously (21). DNA sequencing was performed with reagents purchased from United States Biochemical. PCRs were performed by standard procedures (45).
The emm1 gene of strain 90-226 was amplified via PCR using primers complementary to the conserved 5′ portion of M genes (GGGGGGGGATCCATAAGGAGCATAAAAATGGCT) (21, 40) and nucleotides 55 to 30 of the sic gene (AAGAAAGGATCCAAGGGATGTAAATAGTAGTGT) (1).BamHI restriction sites were added to the 5′ ends of the primers to facilitate cloning of the fragment. The amplified DNA fragment was digested with BamHI, ligated withBamHI-digested pSportI, and transformed into E. coli. One plasmid isolate, designated pemm1, was chosen for further study. Restriction enzyme mapping and DNA sequencing were performed to verify that the plasmid carried emm1.
For expression of M1 fragments in E. coli, a portion of theemm1 gene was PCR amplified with pemm1 as the template. The oligonucleotide primers used were complementary to nucleotides 154 to 174 (GCGATGTCATGAACGGTGATGGTAATCCTAGG) and 1177 to 1156 (AGTCCCCCGGGAAGTTTTGCTTGTAGTTCAGC) of emm1(21). The amplified fragment encodes the first 341 amino acid residues of the mature M1 protein (residues 42 to 382). The DNA fragment was purified, cut with BspHI and SmaI, and then ligated into NcoI-SmaI-digested pCYB4, to construct plasmid pM42-382. Cloning of the emm1 fragment into pCYB4 resulted in the construction of a hybrid gene wherein the M1 coding region is fused, at its 3′ terminus, to the N-terminal coding region of an intein–chitin-binding protein (34, 52). The fusion protein has a predicted molecular mass of 94.5 kDa. E. coli transformed with pM42-382 can be induced to express the fusion protein, which can then be purified by chromatography of bacterial sonicates on a chitin affinity column (New England Biolabs). The addition of dithiothreitol to the column promotes intein-mediated autocleavage of the fusion protein, releasing the M42-382 fragment from the affinity matrix. The purified M42-382 fragment (39.5 kDa) is predicted to possess an N-terminal formylmethionine and a C-terminal glycine residue not present in native M1.
General protein techniques.Concentrations of protein solutions were determined according to the method of Bradford (4), using bovine serum albumin as the standard. Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) was performed as described by Laemmli (27). For Western blotting, proteins were transferred to nitrocellulose membranes (Schleicher & Schuell, Keene, N.H.), using a Trans-Blot cell apparatus (Bio-Rad). Membranes were blocked with 0.25% gelatin, washed briefly in TBST (20 mM Tris [pH 7.5], 0.5 M NaCl, 0.05% Tween 20), and then incubated with anti-Fn Ab in TBST. Membranes were then incubated with alkaline phosphatase conjugated to mouse anti-sheep IgG, washed, and finally developed by using nitroblue tetrazolium–5-bromo-4-chloro-3-indolylphosphate phosphatase detection reagents (Life Technologies).
Detection of Fn binding to immobilized M42-382 was performed similarly except that membranes were blocked with 5% nonfat dry milk and incubated with Fn (25 μg/ml) prior to incubation with Abs.
Protein purifications.Fn and Fg were purified from commercially available Fg as follows (44). A 250-mg aliquot of lyophilized protein was suspended in 50 ml of HBSS (Life Technologies) containing 1 mM phenylmethylsulfonyl fluoride (PMSF) and filtered through a 0.22-μm-pore-size cellulose acetate filter to remove insoluble material. The protein was loaded onto a 1.5- by 5.7-cm gelatin-Sepharose (Pharmacia) column. Chromotography was performed at room temperature. The effluent, containing Fn-depleted Fg, was collected, and aliquots were stored at −20°C. No Fn was detected in Western blot analysis of the repurified Fg, using anti-Fn Ab. To recover Fn, the column was washed with 50 ml of HBSS-PMSF followed by 0.05 M sodium acetate–1 M sodium bromide. Fractions of 1.5 ml were collected, and protein-containing fractions were pooled and then dialyzed against HBSS. Aliquots of the purified Fn were stored at −20°C.
For purification of the M42-382 fragment, E. coliBL21/pM42-382 was grown in LB-ampicillin at 37°C to an optical density at 600 nm (OD600) of 0.2 and then at room temperature to an OD600 of 0.5. At that time, isopropyl-β-d-thiogalactopyranoside (IPTG) was added to 1 mM and the culture was incubated at 15°C for 16 to 18 h. Cells were harvested by centrifugation and suspended in 50 ml of column buffer (20 mM Tris [pH 8.0], 0.5 M NaCl, 0.1 M EDTA, 0.1% Triton X-100) containing 1 μg of DNase I per ml and 1 mM PMSF. All subsequent steps were performed at 4°C. Bacterial cells were disrupted by passage through a French press at 8,000 lb/in2. Lysates were then clarified by centrifugation, and the resulting supernatants were loaded onto a 1.5- by 5-cm chitin affinity column (New England Biolabs). The column was washed with 100 ml of column buffer followed by 15 ml of cleavage buffer (20 mM Tris [pH8], 50 mM NaCl, 0.1 mM EDTA) containing 30 mM dithiothreitol. The column was incubated with cleavage buffer for 16 h at 4°C. The M1 fragment was then eluted by the addition of 15 ml of cleavage buffer. The eluted protein was dialyzed against 50 mM ammonium acetate (pH 6.9) and then concentrated by lyophilization. Lyophilized protein was suspended in phosphate-buffered saline (PBS) to 1 μg/ml, aliquoted, and stored at −80°C.
Fn binding assay.Fn suspended in 0.1 M sodium phosphate–0.15 M NaCl (pH 6.5) was labeled with 125I (Amersham), using Iodobeads iodination reagent (Pierce Chemical Co.), to a specific activity of approximately 106 cpm/μg of protein. Iodinated protein was separated from free label by chromatography on cross-linked dextran columns. Fractions were collected, and those containing 125I-Fn were pooled, aliquoted, and stored at −20°C.
Assay of Fn binding to streptococci was performed as described previously (20). Briefly, overnight cultures of streptococci were harvested by centrifugation, washed twice with 1 volume of PBS (pH 7.4), and finally suspended in PBSAT (PBS containing 0.02% sodium azide and 1% Tween 20) to an OD600 of 0.5; 100-μl portions of the cell suspensions were diluted into 800 μl of PBSAT; 1 to 100 μl of 125I-Fn was then added to duplicate tubes of the cell suspension, and the final reaction volumes were adjusted to 1 ml with PBS. Bacteria and labeled protein were then incubated at room temperature, with end-over-end rotation, for 2 h after which 50 μl of E. coli DH11S, suspended at an OD600 of 10 in PBSAT, was added to each tube. Tubes were centrifuged at 14,000 × g for 10 min at room temperature. Bacterial pellets were washed once with 1 volume of PBSAT, and the amount of radioactivity associated with the pellets was determined. Nonspecific binding was determined by adding the same amount of labeled Fn to tubes containing no streptococci. These reaction mixtures were incubated and bound counts were determined as described above. Radioactive counts recovered from the reaction mixtures were subtracted from those obtained from tubes containing streptococci. Regression analyses were performed by the method of least squares.
Effects of invasion agonists on adherence and internalization of M1+ and M1− streptococci.Intracellular invasion of A549 epithelial cells by S. pyogenes 90-226 is highly dependent on the presence of serum, plasma Fn, or the ECM protein Lm (Fig. 1). To determine if expression of M1 protein is required for the stimulation of invasion by these factors, invasion and adherence assays were performed with strains 90-226 (M1+) and 90-226emm1::Km (M1−). Invasion by either strain was very inefficient in the absence of an agonist, with less than 1% internalization of the bacterial inoculum (Fig. 1a). The addition of FBS, Fn, or mouse Lm stimulated internalization of M1+ bacteria 35-, 70-, and 50-fold, respectively. In contrast, invasion by the M1− strain was unaffected by FBS or Fn addition and was stimulated only twofold by Lm.
M1+ and M1− streptococci both adhere well to A549 cells in the absence of an invasion agonist. Typically, 20 to 30% of the wild-type CFU and 25 to 35% of the M1− CFU remain associated with epithelial cells after washing of the infected monolayers (Fig. 1b). FBS, Fn, or Lm stimulates adherence of the M1+ strain approximately twofold. Fn- and Lm-stimulated adherence is apparently M1 dependent, as adherence of the M1− mutant was not increased by these factors. FBS was found to increase adherence of M1− bacteria by approximately 30%. This result and the slightly higher adherence of the M1− mutant in the absence of agonist are not statistically significant, however.
Invasion by the M1+ strain was previously shown to positively respond to small RGD-containing peptides (10). To determine if M1 expression is required for peptide-mediated invasion, the potential of a four-amino-acid (RGDS) peptide to promote invasion by 90-226 emm1::Km was tested. In four independent experiments in which each assay was performed in triplicate (i.e.,n = 12), the RGDS peptide increased internalization of M1− bacteria an average of 4.5 ± 1.1-fold. It should be noted that while the agonistic effect of small peptides is less than those of Fn or Lm, the effect is readily reproducible and statistically significant (P < 0.001). A peptide of the sequence GRGDTP and a cyclic peptide were also found to promote invasion by the M1− strain (Fig. 2). The tripeptide RGD had no measurable impact on bacterial internalization. These results are nearly identical to those obtained from experiments with the M1+ strain. These results demonstrate that strain 90-226 possesses at least two distinct mechanisms for invasion of epithelial cells: one mechanism that is dependent on M1 expression and the presence of either Fn or Lm, and a second, M1-independent mechanism that is stimulated by exposure to small peptides.
Inhibition of invasion by Fn antiserum.We previously reported that human Fg could activate intracellular invasion by strain 90-226, whereas Fn could not (10). We have since determined that the Fg preparation used in earlier experiments contained approximately 1.6% Fn (Fig. 3). The Fn and Fg in this mixture were separated by chromatography on gelatin-Sepharose, and the recovered proteins were tested for invasion stimulation activity. The Fn-depleted Fg (Fig. 3) failed to stimulate invasion, while the Fg-depleted Fn was an active agonist. It is not clear why the Fn preparation used in the previous study failed to promote invasion. A second preparation of Fn, obtained from the same supplier (Sigma), was also inactive. Bovine and human plasma Fn, obtained from a different commercial source (Life Technologies), had activities comparable to that of the Fn purified from the Fg-Fn mixture.
In light of these results, it seemed plausible that our Lm preparations could have contained Fn, or vice versa, and that only one of these proteins facilitated invasion. It was also possible that all of the active protein preparations contained a common contaminant that was the true invasion agonist. Staining of SDS-polyacrylamide gels, however, did not reveal a contaminating factor that was present exclusively in active protein preparations (Fig. 3a). Dialysis of active protein preparations did not result in any appreciable losses in activity; thus, it is unlikely that agonistic activity is due to a low-molecular-weight contaminating factor (data not shown). Moreover, anti-Fn Ab did not react with an active preparation of HLm or with any protein found exclusively in active preparations (Fig. 3b). Anti-Fn Ab was found to inhibit internalization of streptococci when the agonist was FBS, Fn, or Fg-Fn. The same antiserum did not appreciably affect HLm-mediated invasion (Fig. 4), nor did it adversely affect bacterial growth (data not shown). These results are all consistent with Fn and Lm being distinct, bona fide invasion agonists.
Sequencing of emm1.The emm1 gene of strain 90-226 was amplified by PCR using oligonucleotides complementary to the M-protein signal sequence (21, 40) and to a sequence in the 5′ coding region of sic (1). The PCR fragment was cloned into pSport1 and transformed into E. coli. One plasmid isolate, pemm1, was chosen for sequencing of the cloned fragment. The entire 1,724-bp insert of pemm1 was sequenced and found to contain an open reading frame of 1,452 bp, predicted to encode a 484-amino-acid protein (Fig. 5). The 1,452-bp segment was 99.4% homologous to the emm1.0 gene ofS. pyogenes AP1 (2). Of the eight nucleotide substitutions found, only one is predicted to affect the amino acid sequence of M1 protein. Amino acid residue 366 is predicted to be glutamic acid in the AP1 protein and glycine in the strain 90-226 protein. This result is consistent with the report of Musser et al. (32) that the globally disseminated M1 subclone, responsible for the majority of contemporary invasive streptococcal infections, carries the emm1.0 allele. The last 54 bp of the sequenced fragment were 100% homologous to the N-terminal coding region ofsic. A 190-bp sequence was found between the emm1stop codon and the sic start codon. The sph gene, found between emm1 and sic in some M1 strains (2), is apparently absent from this segment of the strain 90-226 chromosome.
Fn binding by M1 protein.A number of S. pyogenesisolates express a cell surface Fn-binding protein, protein F, that mediates bacterial adherence to host cells. Protein F has been shown to foster adherence by binding soluble Fn which, in turn, binds to the ECM of host tissues (35). Fn and Lm could promote intracellular invasion by M1+ streptococci via a similar mechanism, although we know of no studies demonstrating binding of either agonist by M1 protein.
As a partial test of this mechanism, we first compared levels of binding of 125I-Fn to M1+ and M1−bacteria (Fig. 6). As controls, Fn binding by S. pyogenes JRS4, SAM1, and AP1 was also measured. JRS4 constitutively expresses protein F and binds Fn with high affinity. SAM1 is an isogenic protein F− derivative of JRS4 (20). S. pyogenes AP1 is a serotype M1 isolate that lacks the gene encoding protein F. AP1 is capable of binding Fn; however, this trait is at least partially attributable to expression of protein H (15). Fn binding by 90-226 was comparable to that by AP1, although the affinity of the M1 strains for Fn is significantly less than that of JRS4. Consistent with earlier work (20), the protein F− mutant SAM1 exhibited a greatly diminished capacity to bind Fn. Similarly, strain 90-226 was found to consistently bind Fn with a greater affinity than did its M1− derivative. Overall, Fn binding was reduced 88% for the M1− mutant.
While these results were consistent with direct binding of M1 to Fn, other explanations for these results were possible. Therefore, we tested whether purified M1 could bind Fn. To accomplish this, a DNA fragment coding for amino acid residues 42 to 382 of M1 was cloned into the E. coli expression vector pCYB4. The 343-amino-acid peptide encoded by this fragment corresponds to the extracellular portion of M1 plus 2 amino acids encoded by the vector (Fig. 5). The recombinant protein (M42-382) was expressed in E. coli and purified as described in Materials and Methods. Western blot analysis of M42-382 indicated that the purified protein reacted with M1 antiserum and could bind human Fg (data not shown). Thus, the recombinant protein possessed the properties predicted of M1 protein.
To test for Fn binding to M42-382, the protein was electrophoresed on SDS-polyacrylamide gels and then transferred to nitrocellulose membranes (Fig. 7). As a control,E. coli maltose-binding protein, purified from a strain carrying a derivative of pCYB4, and/or ovalbumin was run in separate lanes of the gels. Membranes were incubated successively with Fn, anti-Fn Ab, and labeled secondary Ab. Fn binding by M1 protein was readily detected in this assay (Fig. 7, lane 2). The higher-molecular-weight band visible in lane 2 appears to be a dimer of the M42-382 protein. As a control for binding of Abs directly to M1 protein, duplicate membranes were incubated with the primary and secondary Abs, without prior incubation with Fn (lane 3). Either no signal or a weak signal was obtained from this control. We conclude that M1 protein can directly bind Fn and that this interaction accounts for most of the Fn binding by strain 90-226.
Effects of anti-integrin MAbs on intracellular invasion efficiency.Integrins are the major receptors by which mammalian cells adhere to ECM proteins, such as Fn and Lm (22). Integrins have also been found to mediate intracellular invasion by some microbial pathogens (23). Since invasion by strain 90-226 is dependent on binding of Fn or Lm, the involvement of a host integrin(s) in internalization of streptococci seemed likely. To test this possibility, we assayed several MAbs for inhibition of invasion by M1+ bacteria. These experiments were performed in the presence of added Fn. MAbs directed against the integrin α5 and β1 subunits were found to inhibit Fn-mediated invasion, whereas MAbs directed against integrins α2, α3, α5, α6, β1, β2, and β4 had slight to no inhibitory effects (Fig.8). Control experiments were performed to verify that the inhibitory MAbs did not adversely affect bacterial viability or adherence of A549 cells to the substratum (data not shown). Since the two inhibitory MAbs should both react with the epithelial cell Fn receptor, integrin α5β1, we obtained a MAb that specifically recognizes this receptor (5) and tested it for invasion inhibition. This MAb also inhibited Fn-mediated invasion, suggesting that Fn stimulates internalization of M1+streptococci by facilitating bacterial interaction with integrin α5β1.
The potential of anti-integrin β1 and α5β1 MAbs to inhibit invasion promoted by agonists other than Fn was also evaluated (Fig.9a). Anti-integrin β1 MAb inhibited Fn-, Lm-, and FBS-mediated invasion by 91, 98, and 86%, respectively. Invasion in the presence of the GRGDTP peptide was also inhibited by 23%, but this inhibition appeared not to be specific for the peptide-promoted invasion pathway, since a comparable level of inhibition (21.5%) was observed when no agonist was present (Fig. 9a, None).
The anti-integrin α5β1 MAb inhibited Fn-mediated invasion by 94% and FBS-mediated invasion by 80% (Fig. 9b). Lm-mediated invasion did not seem to be specifically inhibited by this Ab since the level of inhibition (32%) was comparable to that observed in the absence of an agonist (26%). The nonspecific effects of the MAbs could result from blocking bacterial access to other receptors or cross-reactions with other integrins, or perhaps they are the result of physiological effects on the epithelial cells. These results suggest that even though Fn and Lm are both dependent on M1 protein expression to stimulate invasion, the two agonists target bacteria to distinct host cell integrins.
The streptococcal M protein is an important virulence factor known to bind a number of human plasma proteins, including albumin, IgG, Fg, and complement components. M protein is known to play multiple roles in the pathogenesis of S. pyogenes infections, including resistance to phagocytosis, adherence to host tissues, microcolony formation subsequent to adherence, and intracellular invasion (6, 14, 24). Expression of serotype M1 protein by a highly invasiveS. pyogenes isolate, strain 90-226, has been found to be required for adherence to and invasion of HeLa cells (10a). Invasion of A549 human lung epithelial cells by this strain has also been reported to be dependent on bacterial exposure to mammalian serum, human Fg, or RGD-containing peptides (10). The Fg preparation used in earlier experiments, however, contained approximately 1.6% Fn, and as reported here, Fn was the true invasion agonist. The results reported here indicate that Lm is also an effective agonist.
Fn and Lm are high-molecular-weight extracellular glycoproteins present in blood and the ECM of numerous tissues (41, 44, 49). Isogenic M1+ and M1− strains were tested for their responses to FBS, Fn, or Lm addition, with regard to invasion of A549 cells. In the absence of an agonist, invasion by either strain was very inefficient, with less than 1% internalization of the inoculum. FBS, Fn, or Lm stimulated invasion of M1+streptococci up to 70-fold. FBS and Fn failed to promote invasion by the M1− mutant, and Lm stimulated invasion only twofold. Therefore, the ability of either Fn or Lm to stimulate invasion by strain 90-226 is dependent on expression of M1 protein. Abs directed against Fn or integrin α5β1 were both effective at blocking invasion stimulation by Fn; however, neither Ab abrogated Lm-mediated invasion. These results establish that Fn and Lm are distinct, M1-dependent agonists.
Small synthetic peptides containing the tripeptide sequence RGD can promote epithelial cell invasion by strain 90-226 (10). The same peptides were found to be equally effective at promoting invasion by M1− streptococci; thus, peptide-promoted invasion is independent of M1 expression. Also, anti-integrin β1 MAb did not block peptide-promoted invasion, whereas the same MAb inhibited invasion in the presence of Fn or Lm. As a whole, these results indicate that strain 90-226 possesses at least three distinct mechanisms for invasion of epithelial cells. EnteropathogenicYersinia also encode multiple, independent pathways for entry into cultured cells (12).
Strain 90-226 was previously shown to adhere to A549 cells independently of invasion agonists, but adherence could be stimulated approximately twofold by the addition of 10% FBS (10). Agonist-independent adherence is also M1 independent, as we found that M1+ and M1− bacteria adhered nearly equally well to cultured A549 cells suspended in unsupplemented medium. Adherence by the M1+ strain responded to Fn and Lm, as well as to FBS. In contrast, adherence by the M1− mutant was not appreciably affected by Fn or Lm. Thus, strain 90-226 possesses both factor-dependent and factor-independent adhesins for binding A549 cells. Epithelial cell binding via the latter is apparently insufficient for efficient internalization of bacteria. Adherence mediated by the factor-dependent adhesin, M1 protein, presumably targets bacteria to the appropriate cell receptor for efficient internalization to occur. This is consistent with the fact that invasion agonists have their greatest impact on the efficiency with which adherent bacteria are internalized by epithelial cells. Only 0.1 to 1% of M1+ bacteria that adhere to A549 cells in the absence of an agonist are internalized. This value is increased to approximately 6, 36, or 26% when FBS, Fn, or Lm, respectively, is present. In contrast, adherent M1− bacteria are inefficiently internalized even in the presence of these factors.
The potential of serum or ECM proteins to facilitate adherence to host tissues is a common trait of bacterial pathogens (39). For some microbial pathogens, intracellular invasion is facilitated by binding of host ECM proteins. Vitronectin and Fn can facilitate intracellular invasion by N. gonorrhoeae (11, 17) and Mycobacterium bovis (26), respectively, and invasion by M. leprae can be stimulated by microbial binding of Fn (47) or, as suggested by a recent report, Lm (43).
Two closely related Fn-binding proteins, SfbI and protein F, have been implicated in intracellular invasion by S. pyogenes. Molinari et al. (31) demonstrated that Fn binding by SfbI is apparently sufficient to trigger internalization of streptococci by HEp-2 cells. Jadoun et al. (24) recently reported that a mutation in the gene encoding protein F decreased invasion of HEp-2 cells about sevenfold. The latter study also demonstrated that expression of the cloned protein F gene in a noninvasive strain resulted in a significant increase in invasion efficiency. In both studies, invasion was tested in the presence of FBS, and it was not reported whether exogenous addition of Fn could stimulate internalization of streptococci. This seems likely to be the case, however, since soluble Fn has been shown to promote adherence of protein F+ strains to host cells, apparently by forming a bridge between bacterial cells and host tissues (35). A bridging effect also seems likely to account for Fn- and Lm-mediated invasion by M1+ streptococci. Ab directed against integrin α5β1, known to be expressed by A549 cells (28), specifically abrogates Fn-mediated invasion, suggesting that Fn targets bacterial binding to this integrin. We propose that interaction with this receptor results in ligand-mediated endocytosis of bacteria by A549 cells. Since Fn is the only known α5β1 ligand (22), it was not anticipated that MAb specific for this receptor would block invasion mediated by Lm. Ab directed against the β1 integrin subunit does abrogate Lm-mediated invasion, suggesting that Lm fosters bacterial interaction with one or more β1 integrins (α1β1, α2β1, α3β1, α6β1, or α7β1) for which Lm is a ligand (22, 49). Although MAbs against the integrin α2, α3, and α6 subunits were used in this study, these MAbs have thus far been tested only for inhibition of Fn-mediated invasion. The mechanism underlying M1-dependent entry of streptococci into cultured cells seems to most closely resemble that underlying uptake of Y. pseudotuberculosis. This organism also encodes multiple, independent pathways for entry into mammalian cells. One pathway is mediated by invasin, a 108-kDa outer membrane protein capable of binding at least four different β1 chain integrins, including the α5β1 receptor (23). Interaction of invasin with α5β1 is not dependent on Fn binding by either receptor. Rather, invasin binds directly to α5β1 with high affinity and binding can be inhibited by Fn or RGD-containing peptides (51). This mechanism is clearly distinct from that used by M1+streptococci, which is mediated by integrin ligands. It is not yet clear, however, whether integrin recognition of M1-bound ligands is sufficient to promote bacterial entry. Direct engagement of integrins or possibly other host receptor molecules by M1 may be required for efficient internalization of bacteria.
Among the numerous streptococcal proteins capable of binding Fn that have been described are protein F/SfbI, protein F2, serum opacity factor (SOF), protein H, glyceraldehyde-3-phosphate dehydrogenase (GPD), and Fbp54 (9, 15, 20, 25, 31, 38, 42). The clonal line of which strain 90-226 is representative reportedly lacks the genes encoding protein F/SfbI and SOF (33, 42), and results reported here suggest that the strain may also lack the gene encoding protein H. 90-226 does carry the Fbp54 gene, but anti-Fbp54 serum did not inhibit invasion by this strain (unpublished data). At present, we have no information regarding the presence of genes coding for F2 or GPD in this strain. Regardless of what other Fn-binding proteins may be expressed by 90-226, M1 appears to account for the majority of the strain's Fn-binding activity, since the emm1::Km mutation reduces binding by 88%. Additionally, purified M1 protein is capable of binding Fn. These results are consistent with the proposal that Fn functions as a bridging molecule between M1 and integrin α5β1. Although we are unaware of any previous reports of Fn binding by M1, M3 protein and protein H, an M-like protein, are known to bind Fn (15, 46).
Strains 90-226 and AP1 bind Fn less efficiently than do strains (e.g., JRS4) expressing the high-affinity Fn-binding protein, protein F. As shown here, however, the invasion properties of the former organism can be markedly affected by exposure to Fn. Inclusion of 10 μg of Fn per ml in in vitro assays can increase bacterial internalization by a factor of 70, and Fn can stimulate bacterial uptake when present at much lower concentrations. The concentration of Fn in bodily fluids such as serum (300 μg/ml [44]) or saliva (≤3 μg/ml [29]) seems sufficiently high to accommodate Fn acquisition by organisms possessing only low-affinity Fn receptors.
While M1 expression is necessary for invasion, one question not fully addressed is whether M1 expression is sufficient for high-efficiency invasion. Recent results in our laboratory suggest that this may be the case, since M1-coated polystyrene latex beads can be internalized by human epithelial cells (10a). It is difficult, however, to quantitatively compare these results with those obtained from antibiotic protection assays. Moreover, other studies suggest that M1 expression may not be sufficient for high-level invasion. For example, several recent studies demonstrate that serotype M1 strains vary considerably in their abilities to invade cultured cells (7, 24, 30). These differences could be due to sequence divergence in M1 proteins (32), different levels of emm1expression (7), or expression of novel genes by highly invasive isolates.
Another factor with the potential to influence the efficiency of intracellular invasion by S. pyogenes is the concentration of invasion agonists present in in vitro assays. As reported here, we have found that the ability of Fn to mediate invasion varies considerably, depending on the source of the preparation. This may not be surprising since the activity of Fn in other types of assays can be markedly affected by the procedure used for protein isolation. Even the concentration of Fn in serum can be greatly influenced by the method used for serum preparation (44). It is possible that the concentration or quality of soluble invasion agonists partially accounts for the different invasion efficiencies reported by different laboratories. For example, Jadoun et al. (24) found that AP1 is inefficiently internalized by HEp-2 cells. Recent results in our laboratory indicate that AP1 can be internalized with a reasonable efficiency but that internalization is highly Fn dependent. Obviously, additional work is required to understand what variables account for the different intracellular invasion efficiencies by M1 strains.
Several researchers (18, 37, 48, 50) have reported that there is no observable growth of intracellular streptococci, and infected cell lines are eventually cleared of bacteria. This led Schrager et al. (48) to propose that intracellular invasion by streptococci may not represent a virulence mechanism but rather may actually contribute to host containment of infections. Österlund and Engstrand (37), however, reported that S. pyogenes can remain viable within HEp2 cells for up to 7 days. Also, we have found that M1+ bacteria can be recovered from infected A549 cells after several days of exposure to antibiotics. These results suggest that invasion of host cells may promote bacterial persistence in infected patients who receive antibiotic therapy. This proposal is supported by the finding of Österlund et al. (36) that streptococci can be localized in pharyngeal epithelial cells in 93% of patients with recurrent pharyngotonsillitis. While it is yet undetermined to what extent intracellular invasion affects the severity or frequency of streptococcal disease, it is clear that S. pyogenes has evolved a number of mechanisms for invasion of human cells, suggesting that intracellular invasion is an important aspect of streptococcal pathogenesis.
We thank Tim Leonard, University of Minnesota, for help in figure preparation.
This study was financed by PHS grant AI34503. D.C. was supported by PHS training grant AI07421. P.E.D. was supported by PHS training grant T32-HD-07381.
Editor: P. E. Orndorff
- Received 23 March 1998.
- Returned for modification 18 May 1998.
- Accepted 2 July 1998.
- Copyright © 1998 American Society for Microbiology


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Man who suffered depression found hanged in Norwich tower, inquest hears
PUBLISHED: 17:05 20 March 2018 | UPDATED: 12:25 21 March 2018
Archant Norfolk 2016
A 29-year-old father who suffered depression and "had difficulty expressing his feelings" was found hanged at his flat at the Ashbourne Tower in Heartsease on October 10 last year, an inquest has heard.
Family and friends had not heard from Martin Hartnoll for a number of days and concern was growing. His brother and best friend went to the tenth floor of one of the towers and let themselves in with a key when they found Mr Hartnoll.
Norfolk Coroner's Court heard yesterday how Mr Hartnoll had not had the best start in life and had been through foster care.
His brother Simon Hartnoll had last seen him on September 23, when he "had been fine".
"Three weeks before we found him I heard that he had tried to hang himself," he told the court in a statement. "The next day I spoke to Martin when he indicated he was fine and didn't want to talk about it. I couldn't get him to share anything with me.
"He was fine and his usual self. He was cracking jokes and talking about the future."
Simon went to his brother's flat on October 10 with a friend who had a key, and they discovered him in a bedroom.
They later had to go through his brother's belongings.
"Despite knowing him for 27 years I did not know him at all," said Mr Hartnoll. "I only knew what he wanted me to know.
"The only other time Martin might have harmed himself was when he wrote his Ford Mondeo off. He had driven his car at 80mph over a roundabout when he had been drinking.
"I think he needed professional help. His depression wasn't just linked to one thing. We lost my mum six or seven years ago and a close family friend three months later."
Katrina Duffield, Mr Hartnoll's ex partner, had a son with him in 2012 but the relationship ended soon after.
"We had a close relationship and he would often confide in me," she told the court in a statement. "I believe he had mental health issues but he would not go to the doctor for this as he had difficulty speaking to people. He was having difficulty expressing his feelings.
"He would often stay in his flat due to his difficulties speaking to people."
A statement from Thorpewood Medical Group, where Martin had been a patient prior to January 2017, said there is "no record" of any mental health condition during the period of time he was registered.
Senior coroner for Norfolk Jacqueline Lake ruled out suicide, recording a narrative verdict.
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Canterbury Windsports Association
Sat 30th Oct 10am. Estuary.
Beginners Free Windsurf School/
Come along and find out about the local club.
More info Dan Willemse 03 381 6909
Canterbury Windsports Association Junior Windsurf Coaching Update
We will have Tom Taylor - Winner of the JP Young Gun Freestyle Camp in Spain 3yrs ago- from Wellington down here for the weekend of 27/28 November to do a clinic- The cost for the clinic with Tom will likely be $50.
Will Keep you posted.
CWA Beginners - see http://www.cwa.org.nz for details
What outcomes are being sought?
SPARC is seeking applications that will ultimately lead to increased long-term participation by young people, through:
1. improving organisational capability that leads to more effective service delivery;
2. improving national leadership to better co-ordinate delivery of outdoor recreation;
3. developing skills and knowledge to participate in outdoor recreation, by deliverers of opportunities.
SPARC is not seeking proposals to create more participation opportunities, unless they address at least one of the three outcomes referred to above. Read on ...
The number of dinghy, windsurfing and powerboat instructors in England has risen by almost 1,500 in the last year. The rise comes since the launch of the RYA's Adult Participation Programme, funded through Sport England, which aims to increase and develop the number of adults regularly sailing and windsurfing.
Windsurfing NZ has put in an Expression of Interest (EOI) for funding over the next 3 years to employ someone to promote windsurfing at the youth / yacht club level. This would be backed up with other initiatives to support the development of clubs and promote windsurfing in general. The 2 page submission has been accepted by SPARC but there's a lot of competition so we will now start working on the next phase of the proposal. If you would like to be involved in any way please contact Bruce Spedding. The 2 page submission is included below.
This recent interview with Nevin Sayre demonstrates how lucky NZ has been so far to be as successful as we have been on the International scene, particularly at the Olympics. The interview confirms not only the recent resurgence in windsurfing but also outlines the strategies for getting more kids into windsurfing and more success in competition. Its a powerful affirmation of the approach WNZ is taking to do the same here. Click more to see the full interview.
Windsurfing School registration/certification
Temporary page - to be developed
Starting Thursday 14th Jan through til the end of March. Lessons and rentals available or if you have your own gear just turn up for a social sail and a chat to other sailors. Most weeks there's a BBQ too, though not for the first one tomorrow. Its always weather dependent. So tell your friends and family about it… get them on the water too !
Sue 027 640 8596.
Contacts are Dan 027 785 85 78 and Russell 027 274 76 34
| DeepFried.TV - forums - news | Windsurf.co.nz - webcams - winds | wiNZurf - locations - archive |
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is getting a full-blown Story Mode, the developers at Hinterland Studio have announced. The first part launches in Spring 2016, and the first teaser can be seen in the video above. It's expected to clock in at about 3-4 hours, with subsequent episodes lasting 2-3 hours for a grand season total of 10-12 hours. The current Sandbox Mode is available for $19.99 on Steam and Xbox One, but the price will increase when Story mode launches in the Spring. At launch,all Kickstarter, Early Access, and Game Preview backers will get Story mode at no additional charge.Players in Story Mode will alternate playing as pilot Will Mackenzie and Dr. Astrid Greenwood in their quest to survive in the aftermath of the "First Flare" event. "After keeping our community in the dark about our plans for Story Mode, we're thrilled to finally be able to reveal some details of what we've been working on alongside the over 75 updates we've made to Sandbox Mode over the last year," said Hinterland founder and creative director Raphael van Lierop. "Our success on Early Access proved there's an audience for a more thoughtful survival experience, and the resources we've been able to invest in the game will help us pursue our ambitions around storytelling as we continue to expand this world. We see a bright future for The Long Dark, and are committed to a longterm relationship with our players."
see deal
The Long Dark - PC$34.99on Microsoft Store
According to Hinterland, approximately 25%-30% of Story Mode will take place in entirely new areas. Furthermore, the Sandbox Mode's permadeath will be replaced by a checkpoint save system in Story Mode. Furthermore, the December update for Sandbox adds a new region called Timberwolf Mountain, rope-climbing gameplay, a survival log, a stats screen, and other fixes.Below are concept art looks at Story Mode's two playable heroes, Will and Astrid.
Ryan McCaffrey is IGN's Executive Editor of Previews and Xbox Guru-in-Chief. Follow him on Twitter at @DMC_Ryan, catch him on Podcast Unlocked, and drop-ship him Taylor Ham sandwiches from New Jersey whenever possible.
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DecemberDecember 16th, 2014
Dr. Mary Courage invited us to submit a paper for a Special Issue of Developmental Review on the topic of multitasking. For many months Mary Rothbart and I have been working to apply the study of attention networks to the multiple issues involved in multitasking. We reviewed an extensive literature ranging from studies of how hierarchies of goals were implemented by the brain to studies of training by the use of video games and the issue of internet addiction. We believe we have found and reported in the attached paper some important observations on the multiple issued involved in multitasking. For example, I edited paper for PNAS which showed that multitaskers were poor in switching attention. This seems like a paradox because practice we thought was important for developing the executive attention network important for switching. We now recognize the possibility that Stanford undergraduates who choose multitasking (e.g. listening or watching programs while studying) may be high in sensation seeking and relatively low in other features of attention. In the attached accepted, but not yet published, paper we discuss the literature that seems to provide insight into many issues of multitasking.
For other projects currently underway check the July, August and October posts


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"Have nothing in your houses that you do not know to be useful or believe to be beautiful." ~ William Morris
Sunday, December 23, 2012
Christmas Program
Kate bounced back from her illness quick, so we all enjoyed our Christmas Sacrament Meeting Program together. The youth were in charge of putting together the program and they did a great job! Zoe started it off by reading scripture verses about Samuel the Lamanite ( A Book of Mormon prophet who prophesied of Christ's birth). Then the primary sang "Samuel the Lamanite". I love watching our kids sing because they work hard to learn the words, which allows them to sing with confidence and smiles. Zoe, Emily, Eleanor & I sang in the choir. We sang "The Lamb of God". Thanks to Mallory, we have a choir again. Yay! It has been a long time. Zoe (flute) & Morgan (clarinet) played "Do you hear what I hear". It was beautiful! Emily & Eleanor played in the children's bell choir. They were fun to watch! We have had these bells sitting in our Primary closet for years and years and they were finally used thanks to Cheryl! It was a great addition to our program today. :-)
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Ilala Weavers
Braided basket with a lid "ukhamba", S
Item number HWT0022-02-14
Braided basket with a lid "ukhamba", S
This braided Zulu basket is not only a great decoration item but also a real artwork.
Real art handcraft from South Africa: the braided lid basket in Zulu style
Made of plaited Ilala palms artfully this traditional basketwork with a lid stands out through its great patterns and the exact workmanship. The container in question is unique and was made in extensive handcraft by South African artists. The ground was levelled a little bit so you can put the Africa basket uprightly.
A container for Zulu beer
Traditionally "ukhambas" were used at the Zulu tribe to store self made beer. Round here the artful basketwork from Kwazulu-Natal is perfectly suited as decoration object on a table or sideboard. With this stunning Zulu basket you get a great piece of traditional South Africa as decoration to your home.
Every basketwork is unique - so you get exactly this exemplar
Every basketwork is pure handcraft from South Africa and absolute unique. That means you get exactly the container you can see on the pictures.
For exact dimensions please refer to the tab "Additional information".


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CEM Systems releases new software version
Source: CEM Systems
Date: 2013/05/14
CEM Systems, part of Tyco Security Products, today announced the release of version 6.7 of AC2000 SE (Standard Edition) and AC2000 AE (Airport Edition) integrated access control and security management software. The latest release offers a host of new features that increase the performance and improve the functionality of the CEM AC2000 access control system.
"CEM AC2000 is a powerful access control system that is designed with the customer in mind" said Andrew Fulton, Senior Director of Global Sales, CEM Systems. "The enhanced features and functionality in this new release are based on valuable customer feedback and will ensure that AC2000 continues to provide a flexible access control solution that helps increase security, improve business efficiency and operational effectiveness for CEM sites around the world."
New in version 6.7 are updates and enhancements to AC2000 WEB, CEM's powerful suite of browser based applications for AC2000. The AC2000 WEB menu has an improved and more intuitive look and feel to enhance user experience. In addition to the current suite of WEB applications, AC2000 now provides a unique WEB Zonal Control application for anti-tailgating. This new web based tool discourages tail-gating or passing back of cards to facilitate strict policy control of cardholder movements for operational efficiency. The AC2000 WEB Visitors application has also been updated with a 'Batch Visitor Request Import' tool and new powerful WEB Reports. All these features continue to provide the power of the AC2000 system but through a web browser.
In addition, AC2000 v6.7 software includes enhanced support for emerald?, CEM's revolutionary touch screen intelligent access terminal. emerald features a reader & controller in one, integrated VoIP (Voice over IP) intercom functionality and a range of remote applications that enable elements of AC2000 software to be accessed directly at the door. This latest v6.7 software release offers customers even more enhanced functionality including 'Live video pop-up on intercom request', display of company advertising messages while emerald is idle and six new remote applications. When integrated with a CCTV system, operators can now see who they are talking to when a user initiates an emerald intercom request.
In addition, at v6.7, emerald supports the display of company advertisements which can be uploaded to AC2000 in JPG format as well as offering six new remote applications including Suppress/Enable Alarms for filtering alarms during maintenance periods and One Shot which enables security to remotely open doors from an emerald terminal for a short period of time. Other new applications include Open/Close to enable or disable PIR's or lights with a simple swipe and Online Status which allows users to view the status of all readers directly from an emerald terminal.
Another new feature in v6.7 is alarm escalation, allowing unacknowledged alarms from multiple sites to be forwarded to a supervisory operator workstation after a set time scale. New 'Soft Anti-Passback' functionality also sends a silent alarm to the operator workstation to notify of access cards passed back in breach of policy. This new functionality can be applied on a reader by reader basis or per cardholder for full flexibility.
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Former BYU big man Eric Mika returned to the Heat lineup for the quarter-finals of the Las Vegas summer league, and had his most productive
Tag: Miami Heat
The Eric Mika tracker, game 4
It wasn't a great outing for former BYU basketball star Eric Mika or the Miami Heat in game 4 of the Orlando summer league. Not
The Eric Mika tracker, game 3: Mika has perfect shooting performance
Former BYU big man Eric Mika had a strong showing in his return to action on Monday afternoon in an 86-83 loss to the Indiana
The Eric Mika tracker, game 1: A look at how Mika performed in his first summer league action
Eric Mika's first foray into NBA summer league basketball provided mixed results. His Miami Heat dropped a 74-67 decision to the Charlotte Hornets and he
The Cougar NBA tracker, Jimmer Fredette: Preseason, game 2
The San Antonio Spurs struggled down the stretch as they fell to the Miami Heat 97-94 on Monday night in AmericanAirlines Arena. The Spurs scored
The Cougar NBA tracker, Jimmer Fredette: Preseason, game 1
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Jackson County's Phase 2.5 Recovery Plan which provides guidelines for reopening is now in effect. Stay up to date on Phase 2.5 guidelines and local information at cityofLS.net/coronavirus.
Jackson County personal property, business and real estate tax bills can be paid at Treasury located in the lobby of City Hall. The City benefits by receiving 1 percent of the tax dollars collected for acting as an agent for Jackson County. Taxpayers benefit by receiving tax receipts immediately upon payment.
Payments received at Treasury can be in the form of cash, check, Visa, Mastercard, Discover or American Express. A non-refundable 2.5 percent service fee is charged if using a credit or debit card. There is no fee for cash or check. Checks should be made payable to Jackson County Collector. There will be extended hours to pay at the end of December from 7 a.m. - 6 p.m.
Taxpayers can also place tax bill payments in the City's night drop box, available 24 hours, conveniently located outside the north entrance to City Hall. Checks must be attached to the tax bill with a contact phone number. Tax receipts for payments received via the night drop box will be mailed to payees.
Treasury can also assist taxpayers with an incorrect tax statement. To avoid long lines bring incorrect statements to Treasury for correction prior to the last week of December. Please note, titles, registrations or proof of sale documents are required for billing corrections.
Jackson County Tax Levy Charts
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