Title of Invention: Compositions and methods for the threatment of sepsis Abstract: The present invention relates to compositions and methods for the prevention and treatment of blood-borne and toxin mediated diseases, and in particular anti-C5a antibodies for the prevention and treatment of sepsis in humans as well as other animals. The present invention also relates to methods of generating anti-C5a antibodies employing C-terminal truncated C5a peptides. Detailed Description: This invention was made with Government support under the National Institutes of Health (NIH) awarded by contract GM29507 and HL31963. The government has certain rights in this invention. FIELD OF THE INVENTION The present invention relates to compositions and methods for the prevention and treatment of blood-borne and toxin-mediated diseases, and in particular anti-C5a antibodies for the prevention and treatment of sepsis in humans as well as other animals. BACKGROUND OF THE INVENTION Sepsis is a major cause of morbidity and mortality in humans and other animals. It is estimated that 400,000-500,000 episodes of sepsis resulted in 100,000-175,000 human deaths in the U.S. alone in 1991. Sepsis has become the leading cause of death in intensive care units among patients with non-traumatic illnesses. [G. W. Machiedo et al., Surg. Gyn. & Obstet. 152:757-759 (1981).] It is also the leading cause of death in young livestock, affecting 7.5-29% of neonatal calves [D. D. Morris et al., Am. J. Vet. Res. 47:2554-2565 (1986)], and is a common medical problem in neonatal foals. [A. M. Hoffman et al., J. Vet. Int. Med. 6:89-95 (1992).] Despite the major advances of the past several decades in the treatment of serious infections, the incidence and mortality due to sepsis continues to rise. [S. M. Wolff, New Eng. J. Med. 324:486-488 (1991).] Sepsis is a systemic reaction characterized by arterial hypotension, metabolic acidosis, decreased systemic vascular resistance, tachypnea and organ dysfunction. Sepsis can result from septicemia (i.e., organisms, their metabolic end-products or toxins in the blood stream), including bacteremia (i.e., bacteria in the blood), as well as toxemia (i.e., toxins in the blood), including endotoxemia (i.e., endotoxin in the blood). The term “bacteremia” includes occult bacteremia observed in young febrile children with no apparent foci of infection. The term “sepsis” also encompasses fungemia (i.e., fungi in the blood), viremia (i.e., viruses or virus particles in the blood), and parasitemia (i.e., helminthic or protozoan parasites in the blood). Thus, septicemia and septic shock (acute circulatory failure resulting from septicemia often associated with multiple organ failure and a high mortality rate) may be caused by a number of organisms. The systemic invasion of microorganisms presents two distinct problems. First, the growth of the microorganisms can directly damage tissues, organs, and vascular function. Second, toxic components of the microorganisms can lead to rapid systemic inflammatory responses that can quickly damage vital organs and lead to circulatory collapse (i.e., septic shock) and oftentimes, death. There are three major types of sepsis characterized by the type of infecting organism. Gram-negative sepsis is the most common and has a case fatality rate of about 35%. The majority of these infections are caused by Escherichia coli, Klebsiella pneumoniae and Pseudomonas aeruginosa. Gram-positive pathogens such as the Staphylococci and Streptococci are the second major cause of sepsis. The third major group includes fungi, with fungal infections causing a relatively small percentage of sepsis cases, but with a high mortality rate. Many of these infections are acquired in a hospital setting and can result from certain types of surgery (e.g., abdominal procedures), immune suppression due to cancer or transplantation therapy, immune deficiency diseases, and exposure through intravenous catheters. Sepsis is also commonly caused by trauma, difficult newborn deliveries, and intestinal torsion (especially in dogs and horses). Many patients with septicemia or suspected septicemia exhibit a rapid decline over a 24-48 hour period. Thus, rapid methods of diagnosis and treatment delivery are essential for effective patient care. Unfortunately, a confirmed diagnosis as to the type of infection traditionally requires microbiological analysis involving inoculation of blood cultures, incubation for 18-24 hours, plating the causative organism on solid media, another incubation period, and final identification 1-2 days later. Therefore, therapy must be initiated without any knowledge of the type and species of the pathogen, and with no means of knowing the extent of the infection. It is widely believed that anti-endotoxin antibody treatment administered after sepsis is established may yield little benefit because these antibodies cannot reverse the inflammatory cascade initiated by endotoxin. In addition, the high cost of each antibody could limit physicians' use of a product where no clear benefit has been demonstrated. [K. A. Schulman et al., JAMA 266:3466-3471 (1991).] Furthermore, these endotoxin antibodies only target gram-negative sepsis, and no equivalent antibodies exist for the array of gram-positive organisms and fungi. Clearly, there is a great need for agents capable of preventing and treating sepsis. It would be desirable if such agents could be administered in a cost-effective fashion. Furthermore, approaches are needed to combat all forms of sepsis. SUMMARY OF THE INVENTION The present invention relates to compositions and methods for the prevention and treatment of blood-borne and toxin mediated diseases, and in particular anti-C5a antibodies for the prevention and treatment of sepsis in humans as well as other animals. The present invention provides a composition comprising antibody specific for complement component C5a peptide. In another embodiment, the composition comprises antibody which is specific for complement component C5a peptide, wherein the C5a peptide has a C-terminal region and an N-terminal region, and the antibody is not reactive with the C-terminal region. In further embodiments, the antibody is specific for the N-terminal region of complement component C5a peptide. In an additional embodiment, the antibody is also not reactive with complement component C5 protein. It is not intended that the present invention be limited to antibodies specific for C5a peptides from certain animals. In certain embodiments, the antibody is specific for rat C5a peptide. In other embodiments, the antibody is specific for bovine C5a peptide. In still other embodiments, the antibody is specific for porcine C5a peptide. In a preferred embodiment, the antibody is specific for human C5a peptide. It is also not intended that the present invention be limited to antibodies generated in a particular animal. A variety of animals are useful for generating the antibodies of the present invention. In one embodiment, the antibody is generated in an animal selected from a mouse, a rat, a horse, a goat, a chicken, and a rabbit. In some embodiments, the antibodies are collected from the blood of the animal. In other embodiments, the animal generating the antibodies is a bird, and the antibodies are collected from egg yolk. It is not intended that the present invention be limited to the nature of the antibodies, as a variety of antibody types are contemplated. In one embodiment, the antibodies are monoclonal. In another embodiment, the antibodies are humanized. In other embodiments, the antibodies are chimaeric. In a preferred embodiment, the antibodies are polyclonal. The present invention also provides a method of producing polyclonal antibody. In one embodiment, the method comprises, providing; an animal and an immunogenic composition, wherein the composition comprises C-terminal truncated C5a peptides; and immunizing the animal with the immunogenic composition in order to generate antibodies. In some embodiments, the immunogenic composition comprises adjuvant. In a further embodiment, antibodies are collected from the animal. It is not intended that the present invention be limited to antibodies specific for C5a peptides from any particular animal. In certain embodiments, the antibody is specific for rat C5a peptide. In other embodiments, the antibody is specific for bovine C5a peptide. In still other embodiments, the antibody is specific for porcine C5a peptide. In a preferred embodiment, the antibody is specific for human C5a peptide. It is not intended that the present invention be limited to particular C-terminal truncated peptides. A variety of C-terminal truncated peptides are contemplated. In one embodiment, the C-terminal truncated peptide corresponds to the entire N-terminal region of C5a peptide. In another embodiment, the C-terminal truncated peptide corresponds to the entire N-terminal region of C5a peptide and a portion of the C-terminal region. In another embodiment, the C-terminal truncated peptide is a fragment or portion of the N-terminal region of C5a peptide. In another embodiment, the C-terminal truncated C5a peptide is between approximately 5 and 50 amino acids in length. In some embodiments, the C-terminal truncated peptide is approximately fifty amino acids in length. In other embodiments, the C-terminal truncated peptide is approximately five amino acids in length. In preferred embodiments, the C-terminal truncated peptides are 20 amino acids in length. In certain embodiments, the C-terminal truncated peptides are selected from SEQ ID NOS:2, 4, 5, 14, 15, and 16. The present invention also provides a method of treating a subject with the antibodies of the present invention. In one embodiment, the method comprises; providing; a subject, and a therapeutic composition comprising an antibody specific for complement component C5a peptide, wherein the C5a peptide has a C-terminal region and an N-terminal region, and wherein the antibody is not reactive with the C-terminal region; and administering the therapeutic composition to the subject. In another embodiment, the antibody is specific for the N-terminal region of complement component C5a peptide. In one embodiment, the present invention provides a method comprising; providing; a subject, and a therapeutic composition comprising an antibody specific for complement component C5a peptide, wherein the C5a peptide has a C-terminal region and an N-terminal region, and wherein the antibody is not reactive with the C-terminal region; and administering the therapeutic composition to the subject. In another embodiment, administering the therapeutic composition reduces the binding of complement component C5a peptide to one or more neutrophils of the subject. In a certain embodiment, administering the therapeutic composition reduces bacteremia in the subject. In yet another embodiment, administering the therapeutic composition increases the H2O2 production of neutrophils of the subject. In a preferred embodiment, administering the therapeutic composition reduces the symptoms of sepsis. It is not intended that the therapeutic method of the present invention be limited to particular subjects. A variety of subjects are contemplated. In one embodiment the subject is selected from a pig, a rat, a cow, a horse, and a human. In one embodiment, the therapeutic composition is administered to a subject suffering from symptoms of sepsis. In another embodiment, the therapeutic composition is administered prophylactically to a subject at risk for sepsis, including new born humans and animals. It is not intended that the therapeutic method of the present invention be limited to certain modes of administration. A variety of modes of administering the therapeutic composition are contemplated. In one embodiment, the therapeutic composition is administered by a mode selected from intravenously, intra-muscularly, subcutaneously, intradermally, intrapenrtoneally, intrapleurally, intrathecally, and topically. It is not intended that the present invention be limited to a particular therapeutic composition. A variety of compositions are contemplated. In one embodiment the therapeutic composition comprises a soluble mixture of anti-C5a antibodies. In another embodiment, the anti-C5a antibodies are provided together with physiologically tolerable liquid, gels, solid carriers, diluents, adjuvants or excipients, and combinations thereof. In other embodiments, the therapeutic composition comprises anti-C5a antibodies and other therapeutic agents (e.g. other immunoglobulins or antibiotics). The present invention also provides a method for screening C-terminal truncated C5a peptides to identify immunogens for the production of anti-C5a antibodies. In one embodiment, the method comprises, providing a C-terminal truncated C5a peptide, modifying the amino acid sequence of said C-terminal truncated C5a peptide, and screening said C-terminal truncated C5a peptide to identify immunogens for the production of anti-C5a antibodies. In one embodiment, the C-terminal truncated C5a peptide which is provided is selected from SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:14, SEQ ID NO:15, and SEQ ID NO:16. In other embodiments, the screening step involves a chemotaxis assay (See e.g. Examples 7, 8 and 11). In a different embodiment, the screening step involves a competitive binding assay (See e.g. Examples 10 and 11). In an additional embodiment, the screening step involves administering the C-terminal truncated peptides to septic animals (See e.g. Example 11). DESCRIPTION OF THE FIGURES FIG. 1 shows survival curves of septic rats with and without the administration of anti-C5a antibodies. FIG. 2 shows a graph demonstrating the ability of anti-C5a antibodies to reduce bacteria blood of septic rats. FIG. 3 shows a graph demonstrating the ability of anti-C5a antibodies to reduce bacteria in the organs of septic rats. FIG. 4 shows a graph demonstrating the ability of anti-C5a antibodies to increase the level of H2O2 production in neutrophils of septic rats. FIG. 5 shows a graph demonstrating the ability of synthetic peptides to reduce human C5a-induced chemotaxis of neutrophils. FIG. 6 shows the chemotactic activity of KLH-linked synthetic peptides of human C5a peptide. FIG. 7 shows polyclonal rabbit anti-human C5a reactivity with regions of human C5a peptide. FIG. 8 shows the amino acid sequence of human C5a peptide and various smaller portions of the human C5a peptide. FIG. 9 shows a graph demonstrating the ability of certain synthetic peptides to inhibit the binding of human C5a peptide to human neutrophils. DEFINITIONS The phrase “symptoms of sepsis” refers to any symptoms characteristic of a subject with sepsis including but not limited to, arterial hypotension, metabolic acidosis, fever, decreased systemic vascular resistance, tachypnea and organ dysfunction. Sepsis can result from septicemia (i.e., organisms, their metabolic end-products or toxins in the blood stream), including bacteremia (i.e., bacteria in the blood), as well as toxemia (i.e., toxins in the blood), including endotoxemia (i.e., endotoxin in the blood). The term “sepsis” also encompasses fungemia (i.e., fungi in the blood), viremia (i.e., viruses or virus particles in the blood), and parasitemia (i.e., helminthic or protozoan parasites in the blood). Thus, phenotypes associated with septicemia and septic shock (acute circulatory failure resulting from septicemia often associated with multiple organ failure and a high mortality rate) are symptoms of sepsis. The phrase “reduces the symptoms of sepsis” refers to a qualitative or quantitative reduction in detectable symptoms, including but not limited to a detectable impact on the rate of recovery from disease. The phrase “at risk for sepsis” in reference to a subject is herein defined as a subject predisposed to the development of sepsis by virtue of the subject's medical status, including but not limited to such factors as infection, trauma (e.g., abdominal perforation, such as by a gun shot wound), surgery (e.g., intestinal surgery), and invasive procedures (e.g., placement of a catheter, etc.) and the like. As used herein, the term “antigen” refers to any agent (e.g., any substance, compound, molecule [including macromolecules], or other moiety), that is recognized by an antibody, while the term “immunogen” refers to any agent (e.g., any substance, compound, molecule [including macromolecules], or other moiety) that can elicit an immunological response in an individual. These terms may be used to refer to an individual macromolecule or to a homogeneous or heterogeneous population of antigenic macromolecules. It-is intended that the term encompasses protein and peptide molecules or at least one portion of a protein or peptide molecule, which contains one or more epitopes. In many cases, antigens are also immunogens, thus the term “antigen” is often used interchangeably with the term “immunogen.” The substance may then be used as an antigen in an assay to detect the presence of appropriate antibodies in the serum of the immunized animal. The term “specific for” when used in reference to the interaction of an antibody and a protein or peptide means that the interaction is dependent upon the presence of a particular structure (i.e., the antigenic determinant or epitope) on the protein; in other words the antibody is recognizing and binding to a specific protein structure rather than to proteins in general (i.e. non-specific or background binding). The term “not reactive with” when used in reference to the potential interaction of an antibody and a protein or peptide means that the antibody does not recognize or bind specifically to that particular protein (i.e. binding is at background levels). The term “operably linked” refers to an arrangement of elements wherein the components so described are configured so as to perform their usual function. Thus, control sequences operably linked to a coding sequence are capable of effecting the expression of the coding sequence. The control sequences need not be contiguous with the coding sequence, so long as they function to direct the expression As used herein, the phrase “anti-C5a antibody” refers to antibodies which are specific for complement component C5a peptide, or portions thereof. As used herein, the term “adjuvant” is defined as a substance known to increase the immune response to other antigens when administered with other antigens. If adjuvant is used, it is not intended that the present invention be limited to any particular type of adjuvant—or that the same adjuvant, once used, be used all the time. It is contemplated that adjuvants may be used either separately or in combination. The present invention contemplates all types of adjuvant, including but not limited to agar beads, aluminum hydroxide or phosphate (alum), Incomplete Freund's Adjuvant, as well as Quil A adjuvant commercially available from Accurate Chemical and Scientific Corporation, Gerbu adjuvant also commercially available (GmDP; C.C. Biotech Corp.), and bacterin (i.e., killed preparations of bacterial cells). As used herein, the term “N-terminal region of C5a peptide” refers to the N-terminal 50% of the complement component C5a peptide. As used herein, the term “C-terminal region of C5a peptide” refers to the C-terminal 30% of the complement component C5a peptide. As used herein, the term “wherein said antibody is not reactive with the C-terminal of C5a region” refers to antibodies that do not recognize or bind to the C-terminal 30% of the C5a peptide. As used herein, the term “C-terminal truncated C5a peptides” refers to peptides of varying lengths derived from the N-terminal 70% of the C5a peptide, wlhiclh do not include amino acid sequences from the C-terminal 30% of the C5a peptide. Examples of these peptides include, but are not limited to, SEQ ID NO:2 (from Rat C5a peptide), and SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:14, SEQ ID NO:15, and SEQ ID NO:16 (from Human C5a peptide). As used herein, the terms “C5a peptide”, “C5a protein”, and “complement component C5a peptide” all refer to the complement component peptide in animals which is cleaved from the amino terminus of complement component C5 when the complement system is activated. Examples of animals with this protein include, but are not limited to, mice, rats, cows, pigs, and humans. This definition also includes peptides with synthetic sequences which share substantial homology to naturally occurring C5a peptides. An example of this type of sequence, includes, but is not limited to, the sequence disclosed in Mandecki W, et al., Proc Natl Acad Sci USA. June;82(11):3543-7(1985). As used herein, the term “modifying the amino acid sequence” of said C-terminal truncated C5a peptide refers to the addition, deletion, or substitution of one or more amino acids to create a variant or modified C-terminal truncated C5a peptide (See section II.b, below). Examples of such variants or modified sequences are listed in Table 3 below. A “variant” of a C5a peptide (or C-terminal truncated CSapeptide) is defined as an amino acid sequence which differs by one or more amino acids from the C5a peptide (or C-terminal truncated C5a peptide) sequence. The variant may have “conservative” changes, wherein a substituted amino acid has similar structural or chemical properties, e.g. replacement of leucine with isoleucine. More rarely, a variant may have “nonconservative” changes, e.g. replacement of glycine with a tryptophan. Similar minor variations may also include amino acid deletions or insertions (i.e., additions), or both. A variant may be an epitope as short as four amino acids in length, and as long as a modified full-lenth C5a peptide. More preferably, a variant is greater than five amino acids in length, and less than twenty-five amino acids in length. Variants may also contain a fusion protein. In such cases, the variant may have more amino acids than the natural, full-lenght C5a peptide. DESCRIPTION OF THE INTENTION The present invention relates to compositions and methods for the prevention treatment of blood-borne and toxin mediated diseases, and in particular anti-C5a antibodies for the prevention and treatment of sepsis caused by various types of organisms in humans as well as other animals. It is contemplated that the present invention finds use in the treatment of gram-negative and gram-positive sepsis. Although the invention may be used for treatment of sepsis due to an individual organism, it may also be used to treat sepsis caused by multiple organisms (e.g., sepsis and/or bacteremia due to gram-negative and gram-positive organisms). I. The C5a Peptide and Sepsis The complement system is a complex group of proteins present in body fluids that, working together with antibodies or other factors, plays an important role as mediators of immune, allergic, immunochemical and immunopathological reactions. Activation of the complement system can result in a wide range of reactions such as lysis of various kinds of cells, bacteria and protozoa, inactivation of viruses, and the direct mediation of inflammatory processes. Through the hormone-like activity of several of its components, the complement system can recruit and enlist the participation of other humoral and cellular effector systems. These in turn can induce directed migration of leukocytes, trigger histamine release from mast cells, and stimulate the release of lysosomal constituents from phagocytes. The complement system consists of at least twenty distinct plasma proteins capable of interacting with each other, with antibodies, and with cell membranes. Many of these proteins, when activated, combine with still others to form enzymes that cleave and activate still other proteins in the system. The sequential activation of these proteins follows two main pathways, the classical pathway and the alternative pathway, Both pathways use a common terminal trunk that leads to cell lysis or virus inactivation. The classical pathway can be activated by antigen-antibody complexes, aggregated immunoglobulins and non-immunological substances such as DNA and trypsin-like enzymes. The classical pathway includes activation of C1, C4, C2 and C3. These components can be grouped into two functional units: C1 or recognition unit; and C4, C2 and C3 or activation unit. Five additional components denominated C5, C6, C7, C8, and C9 define the membrane attack unit forming the terminal trunk common to both pathways. C5a peptide, also called anaphylatoxin, is a complement component peptide which is cleaved from the amino terminus of component C5 when the complement system is activated. C5a peptide has been shown to stimulate contraction of smooth muscle, enhance vascular permeability, promote the synthesis and release of other mediators including leukotrienes, prostaglandins, platelet-activating factor, and histamine. In vivo, C5a peptide results in the accumulation of polymorphonuclear leukocytes (PMN) (i.e. neutrophils) and marcrophages at the site of inflammation, one of the hallmark events of an acute inflammatory response. In vitro, C5a peptide is a potent chemotaxin for leukocytes, most notably PMN and macrophages, and it activates PMN causing them to release a variety of hydrolytic enzymes and to generate oxygen radicals. These latter-phenomena are thought to be responsible not only for the killing of microorganisms but for much of the tissue destruction that takes place in inflammatory situations. There is abundant evidence that in sepsis, complement activation, production of cytokines, and unregulated inflammatory responses occurs. It is well established in humans with sepsis that complement activation and complement consumption have occurred, as defined by loss of whole hemolytic activity of serum complement (CH50) and the presence of C5a peptide in serum [Koehl, J., Bitter-Suermann, D., Anaphylatoxins. Complement in health and disease., Edited by Whaley, K., Loos, M., Weiler, J. M., Kluwer Academic publishers, pp 299-324, (1993), and Solomkin, et al., Surgery 90:319-327, (1981)]. It is well established from in vitro studies that interaction of C5a peptide with C5a receptor (C5aR) leads to phosphorylation of serine residues of the receptor, followed by rapid internalization of the receptor-ligand complex, dephosphorylation of the receptor and its recycling back to the surface of the cell. All of this occurs fairly rapidly. Furthermore, the maximal C5a-induced H2O2 response of the neutrophil requires that only a fraction of C5aR be occupied with ligand [Van Epps, et al., J. Immunol. 150:246-252 (1993)]. Neutrophils stimulated with C5a peptide become refractory (“deactivated”) to further stimulation with this peptide; following exposure to high doses of C5a peptide, global deactivation to chemotactic peptides occurs [Ward, P. A. & Becker, E. L., J. Exp. Med. 127:693-709 (1968)]. There is clinical evidence that blood neutrophils from humans with early sepsis lose functional responsiveness to C5a peptide and in the latter phases of sepsis lose responsiveness to structurally different chemotaxins such as the bacterial chemotactic factor [Solomkin, J. S., et al., Surgery 90:319-327 (1981)]. It has also been reported that C5 deficient mice demonstrate somewhat prolonged survival times when sepsis is induced, but ultimately all animals succumbed to the sepsis syndrome [Olson, L. M., et al., Ann. Surg. 202:771-776 (1985)]. It is not necessary to the successful practice the present invention that one understand the precise mechanism by which a therapeutic benefit is achieved, nor is the present invention limited to any particular mechanistic explanation. However, it is believed that sepsis results in excessive production of C5a peptides, which leads to deactivation of neutrophils, compromising the respiratory burst (H2O2 production) of these cells and the closely linked bactericidal function, which is dependent upon H2O2 generation and participation of myeloperoxidase. The anti-C5a antibodies of the present invention, therefore, are believed to prevent the deactivation of neutrophils caused by sepsis, thus preserving the bactercidial function of the neutrophils. In this regard, the present invention contemplates antibodies specific for complement component C5a peptides and methods of using these antibodies to treat sepsis. In some embodiments, these antibodies are specific for complement component C5a peptide, wherein said C5a peptide has a C-terminal region and an N-terminal region, and wherein said antibody is not reactive with said C-terminal region. II. Generating Antibodies to C5a Peptides a. Antibodies The present invention contemplates monoclonal, polyclonal, and humanized antibodies to C5a peptides. In some embodiments, the antibodies are specific for complement component C5a peptide, wherein said C5a peptide has a C-terminal region and an N-terminal region, and said antibody is not reactive with said C-terminal region. Monoclonal antibodies useful in this invention are obtained, for example, by well known hybridoma methods. In one embodiment, an animal is immunized with a preparation containing C-terminal truncated peptides. A fused cell hybrid is then formed between antibody-producing cells from the immunized animal and an immortalizing cell such as a myeloma. In one embodiment, antibodies of the present invention are produced by murine hybridomas formed by fusion of mouse myeloma or hybridoma which does not secrete antibody with murine spleen cells which secrete antibodies obtained from mice immunized against C-terminal truncated C5a peptides. In some embodiments, mice are immunized with a primary injection of C-terminal truncated C5a peptides, followed by a number of boosting injections. During or after the immunization procedure, sera of the mice may be screened to identify mice in which a substantial immune response to the C-terminal truncated C5a peptides has been evoked. From the selected mice, spleen cells are obtained and fusions are performed. Suitable fusion techniques include, but are not limited to, the Sendai virus technique [Kohler, G. and Milstein, C., Nature 256:495 (1975)] or the polyethylene glycol method [Kennet, R. H., “Monoclonal Antibodies, Hybridoma—A New Dimension in Biological Analysis,” Plenum Press, NY (1980)]. The hybridomas are then screened for production of anti-C5a antibodies. Suitable screening techniques include, but are not limited to, solid phase radioimmunoassay. A solid phase immunoadsorbent is prepared by coupling C5a peptides to an insoluble matrix. The immunoadsorbent is brought into contact with culture supernatants of hybridomas. After a period of incubation, the solid phase is separated from the supernatants, then contacted with a labelled antibody against murine immunoglobulin. Label associated with the immunoadsorbent indicates the presence of hybridoma products reactive with C5a peptides. In preferred embodiments the monoclonal anti-C5a antibodies are produced in large quantities by injecting anti-C5a antibody producing hybridoma cells into the peritoneal cavity of mice and, after an appropriate time, harvesting acites fluid from the mice which yield a high titer of homogenous antibody. The monoclonal antibodies are isolated therefrom. Alternatively, the antibodies are produced by culturing anti-C5a antibody producing cells in vitro and isolating secreted monoclonal anti-C5a antibodies from the cell culture medium directly. Another method of forming antibody-producing cells is by viral or oncogenic transformation. For example, a B-lymphocyte which produces anti-C5a specific antibody is infected and transformed with a virus, such as the Epstein-Barr virus, to give an immortal antibody-producing cell [Kozbon and Roder, Immunol. Today 4:72-79 (1983)]. The present invention also contemplates anti-C5a polyclonal antibodies. Polyclonal antibodies can be prepared by immunizing an animal with a crude preparation of C-terminal truncated C5a peptides, or purified C-terminal truncated C5a peptides. The animal is maintained under conditions whereby antibodies reactive with the components of the peptides are produced. [See e.g. Elzaim, et al., Infect. Immun. May;66(5):2170-9 (1998)]. Typically the animal is “boosted” by additional immunizations to increase the antibody titer. In one method, blood is collected from the animal upon reaching a desired titer of antibodies. The serum containing the polyclonal antibodies (antisera) is separated from the other blood components. The polyclonal antibody-containing serum may be further separated into fractions of particular types of antibodies (e.g. IgG or IgM) or monospecific antibodies can be affinity purified from polyclonal antibody containing serum. In another method, the immunized animal is a bird. In this method antibodies (IgY) are collected from egg yolks. The egg yolk is separated from the yolk lipid and non-antibody proteinaceous matter, recovering the IgY anti-C5a antibodies in purified form (see e.g. U.S. Pat. 4,357,272 to Polson and U.S. Pat. No. 5,904,922 to Carroll). The present invention also contemplates humanized antibodies (i.e. substantially non-immunogenic antibodies). Such antibodies are particularly useful in treating human subjects. Chimeric and ‘reshaped’ humanized anti-C5a antibodies may be produced according to techniques known in the art (see e.g. U.S. Pat. No. 5,585,089 to Queen et al., and Kettleborough, et al., Protein Engineering, vol. 4, no. 7, pp 773-783, 1991). In one embodiment, humanized anti-C5a chimeric antiboides are produced using a combinatorial approach (see e.g. U.S. Pat. No. 5,565,332 to Hoogenboom et al. and U.S. Pat. No. 5,658,727 to Barbas et al.). The present invention also contemplates single polypeptide chain binding molecules which have binding specificity and affinity subtantially similar to the binding specificity and affinity of the light and heavy chain aggregate variable region of an anti-C5a antibody (see e.g. U.S. Pat. No. 5,260,203 to Ladner et al.). b. C5a Peptide Immunogens The present invention provides various C5a peptide immunogens. For example, the C5a peptides can be from various animals (e.g. human, rat, pig, and cow). The amino acid sequence of these C5a peptides are described in the literature [see Rothermel et al., Biochim. Biophys. Acta 1351 (1-2), 9-12, (1997){rat}; Babkina, I. N., et al., Bioorg Khim, May;21(5):359-64, (1995){human}; Gerard, C. et al., J. Biol. Chem. 255(10), 4710-4715, (1980){pig}; and Zarbock, J., et al., FEBS Lett. 238(2), 289-294, (1988){cow}]. The C5a immunogen may be the full length C5a peptide, or various peptides derived from the full length C5a peptide. In particular embodiments, the peptides are C-terminal truncated peptides (e.g. SEQ ID NOS:2, 4, 5, 14, 15 and 16). Representative sequences are listed in, Table 1. Representative human and rat DNA sequences which are used to generate various C-terminal truncated C5a peptides are listed in Table 2, along with the full human and full rat C5a DNA sequences. Modifications of these sequences (i.e. longer/shorter sequence, from various regions) are contemplated by the present invention. Generation of these various C-terminal truncated C5a peptide immunogens are described below. Variants of the C-terminal truncated C5a peptides are contemplated as useful immunogens (See e.g. Table 3). For example, it is contemplated that an isolated replacement of a leucine with an isoleucine or valine, an aspartate with a glutamate, a threonine with a serine, or a similar replacement of an amino acid with a structurally related amino acid (i.e., conservative mutations) will not have a major effect on the biological activity of the resulting molecule. Conservative replacements are those that take place within a family of amino acids that are related in their side chains. Genetically encoded amino acids can be divided into four families: (1) acidic (aspartate, glutamate); (2) basic (lysine, arginine, histidine); (3) nonpolar (alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan); and (4) uncharged polar (glycine, asparagine, glutamine, cysteine, serine, threonine, tyrosine). Phenylalanine, tryptophan, and tyrosine are sometimes classified jointly as aromatic amino acids. In similar fashion, the amino acid repertoire can be grouped as (1) acidic (aspartate, glutamate); (2) basic (lysine, arginine histidine), (3) aliphatic (glycine, alanine, valine, leucine, isoleucine, serine, threonine), with serine and threonine optionally be grouped separately as aliphatic-hydroxyl; (4) aromatic (phenylalanine, tyrosine, tryptophan); (5) amide (asparagine, glutamine); and (6) sulfur -containing (cysteine and methionine) (See e.g., Stryer ed., Biochemistry, 2nd ed, WH Freeman and Co.[1981]). Thus, in certain embodiments, modifications of the C-terminal truncated C5a peptides are contemplated by the present invention. Similar minor variations may also include amino acid deletions or insertions (i.e. additions), or both. Guidance in determining which and how many amino acid residues may be substituted, inserted or deleted without abolishing biological or immunological activity may be found using computer programs well known in the art, for example, DNAStar software or GCG (Univ. of Wisconsin). Whether a change in the amino acid sequence of a C-terminal truncated C5a peptide results in a useful immunogen for producing the anti-C5a antibodies of the present invention can be readily determined. One method involves screening the C-terminal truncated C5a peptides for the ability to inhibit the chemotaxis of neutrophils. Useful immunogens are identified by the ability to induce cheimotaxis (See e.g. Examples 7, 8 and 11). Another indication of a useful immunogen is the ability of the C-terminal truncated C5a peptide to inhibit chemotaxis when combined with C5a peptide (See e.g. Examples 7, 8, and 11). Another method involves screening the C-terminal truncated C5a peptides for the ability to antagonize the binding of labelled C5a peptides to neutrophils in a competitive assay (See e.g. Examples 10 and 11). Yet another method involves administering the C-terminal truncated C5a peptides to CLP sepsis induced rats, and monitoring their response over a given time period. Useful immunogens are identified by the ability to reduce the symptoms of sepsis, and/or increase survival times of the rats (See e.g. Example 11). The C-terminal truncated C5a peptides employed in the present invention may also comprise a fusion partner. Examples of fusion partners include Protein A, ABP, GST, poly histidine, HA, KLH, and MBP. Other fusion partners /are well known in the art. (See Nilsson et al., Prot. Expr. Purif., 11(1):1-16 [(1997]). The fusion partner may serve various functions, including, but not limited to, enhancement of the solubility of the C-terminal truncated C5a peptides, as well as providing an “affinity tag” to allow the purification of the recombinant fusion C-terminal truncated C5a peptide from the host cell or culture supernatant, or both. If desired, the exogenous protein fragment may be removed from the peptide of interest prior to immunization by a variety of enzymatic or chemical means known in the art. In some embodiments, nucleic acid sequences corresponding to these various C-terminal truncated C5a peptides (e.g., SEQ ID NOS:10, 11, 13, 17, 18, and 19) are used to generate recombinant DNA molecules that direct the expression of the C-terminal truncated C5a peptides in appropriate host cells, which are then purified and used as immunogens to generate the antibodies of the present invention. These DNA sequences may be included in any one of a variety of expression vectors for expressing C-terminal truncated C5a peptides in various hosts. Examples of vectors include, but are not limited to, chromosomal, nonchromosomal and synthetic DNA sequences, e.g., derivatives of SV40; bacterial plasmids; phage DNA; baculovirus; yeast plasmids; vectors derived from combinations of plasmids and phage DNA, viral DNA such as vaccinia, adenovirus, fowl pox virus, and pseudorabies, and the like. Any vector may be used as long as it is replicable and viable in the host. Large numbers of suitable vectors are known to those of skill in the art, and are commercially available. Such vectors include, but are not limited to, the following: 1) Bacterial—pQE70, pQE60, pQE-9 (Qiagen), pBS, pD10, phagescript, psiX174, pbluescript SK, pBSKS, pNH8A, pNH16a, pNH18A, pNH46A (Stratagene); ptrc99a, pKK223-3, pKK233-3, pDR540, pRIT5 (Pharmacia); and 2) Eukaryotic—pWLNEO, pSV2CAT, pOG44, PXT1, pSG (Stratagene) pSVK3, pBPV, pMSG, pSVL (Pharmacia). In general, mammalian expression vectors comprise an origin of replication, a suitable promoter and enhancer, and also any necessary ribosome binding sites, polyadenylation site, splice donor and acceptor sites, transcriptional termination sequences, and 5′ flanking nontranscribed sequences. DNA sequences derived from the SV40 splice, and polyadenylation sites may be used to provide the required nontranscribed genetic elements. The DNA sequence in the expression vector may be operably linked to an appropriate expression control sequence(s) (promoter) to direct mRNA synthesis. Promoters useful in the present invention include, but are not limited to, the LTR or SV40 promoter, the E. coli. lac or trp, the phage lambda PL and PR, T3 and T7 promoters, and the CMV immediate early, HSV thymidine kinase, and mouse metallothionein-I promoters and other promoters known to control expression of peptides in prokaryotic or eukaryotic cells or their viruses. Recombinant expression vectors generally include origins of replication and selectable markers permitting transformation of the host cell (e.g., dihydrofolate reductase or neomycin resistance for eukaryotic cell culture, or such as tetracycline or ampicillin resistance in E. coli). Transcription of the DNA encoding the C-terminal truncated C5a peptides of the present invention is increased by inserting an enhancer sequence into the vector. Enhancers are cis-acting elements of DNA, usually about from 10 to 300 bp that act on a promoter to increase its transcription. Enhancers useful in the present invention include, but are not limited to, the SV40 enhancer on the late side of the replication origin bp 100 to 270, a cytomegalovirus early promoter enhancer, the polyoma enhancer on the late side of the replication origin, and adenovirus enhancers. The expression vector may also contain a ribosome binding site for translation initiation and a transcription terminator. Various host cells may be employed to recombinantly express the C-terminal truncated C5a peptides. Suitable host cells are higher eukaryotic cells (e.g., a mammalian or insect cell), lower eukaryotic cells (e.g., a yeast cell), and prokaryotic cells (e.g., a bacterial cell). Specific examples of host cells include, but are not limited to, Escherichia coli, Salmonella typhimurium, Bacillus subtilis, and various species within the genera Pseudomonas, Streptomyces, and Staphylococcus, as well as, Saccharomycees cerivisiae, Schizosaccharomycees pombe, Drosophila S2 cells, Spodoptera Sf9 cells, Chinese Hamster Ovary (CHO) cells, COS-7 lines of monkey kidney fibroblasts, (Gluzman, Cell, 23:175 [1981]), C127, 3T3, HeLa and BHK cell lines. The constructs in host cells can be used in a conventional manner to produce the C-terminal truncated C5a peptides encoded by the recombinant sequences. In some embodiments, introduction of the construct into the host cell is effected by calcium phosphate transfection, DEAE-Dextran mediated transfection, or electroporation [Davis et al., Basic Methods in Molecular Biology, (1986)]. Following transformation of a suitable host strain and growth of the host strain to an appropriate cell density, the selected promoter is induced by appropriate means (e.g., temperature shift or chemical induction) and cells are cultured for an additional period. Cells are typically harvested by centrifugation, disrupted by physical or chemical means, and the resulting crude extract retained for further purification. Methods for recovering and purifying C-terminal truncated C5a peptides from recombinant cell culture include, but are not limited to, ammonium sulfate or ethanol precipitation, acid extraction, anion or cation exchange chromatography, phosphocellulose chromatography, hydrophobic interaction chromatography, affinity chromatography, hydroxylapatite chromatography and lectin chromatography. High performance liquid chromatography (HPLC) can also be employed for final purification steps. DNA sequences having coding sequences (e.g., SEQ ID NOS:10, 11, 13, 17, 18, and 19) fused in frame to a marker sequence allow for purification of the C-terminal truncated C5a peptide. One example is a histidine tag which may be supplied by a vector (e.g., a pQE-9 vector) which provides for purification of the polypeptide fused to the marker in the case of a bacterial host, or, for example, the marker sequence may be a hemagglutinin (HA) tag when a mammalian host (e.g., COS-7 cells) is used. The HA tag corresponds to an epitope derived from the influenza hemagglutinin protein (Wilson, et al., Cell, 37:767 [1984]). The coding sequences for the C-terminal truncated C5a peptides can also be incorporated as a part of a fusion gene including a nucleotide sequence encoding a different polypeptide. One example employs the VP6 capsid protein of rotavirus used as an immunologic carrier protein for the C-terminal truncated C~a peptides, either in the monomeric form or in the form of a viral particle. The nucleic acid sequences corresponding to the various C5a peptides to which antibodies are to be raised can be incorporated into a fusion gene construct which includes coding sequences for a late vaccinia virus structural protein to produce a set of recombinant viruses expressing fusion proteins comprising C-terminal truncated C5a peptides as part of the virion. It has been demonstrated with the use of immunogenic fusion proteins utilizing the Hepatitis B surface antigen fusion proteins that recombinant Hepatitis B virions can be utilized in this role as well. Similarly chimeric constructs coding for fusion proteins containing C-terminal truncated C5a peptides and the poliovirus capsid protein are created to enhance immunogenicity of the set of polypeptide antigens [see e.g., EP Publication No. 025949; and Evans et al., Nature 339:385 (1989); Huang et al., J. Virol. 62:3855 (1988); and Schlienger et al., J. Virol. 66:2 (1992)]. The Multiple Antigen Peptide system for peptide-based immunization can also be utilized, wherein a desired C-terminal truncated C5a peptide sequence is obtained directly from organo-chemical synthesis of the peptide onto an oligomeric branching lysine core [see e.g., Posnett et al., JBC 263:1719 (1988) and Nardelli et al., J. Immunol. 148:914 (1992)]. C-terminal truncated C5a peptides can also be expressed and presented by bacterial cells in order to generate the antibodies of the present invention. In addition to utilizing fusion proteins to enhance immunogenicity, fusion proteins can also facilitate the purification of proteins. Accordingly, the C5a peptides can be generated as a glutathione-S-transferase (GST) fusion protein. Such GST fusion proteins enable easy purification of the C5a peptides, such as by the use of glutathione-derivatized matrices [see e.g, Current Protocols in Molecular Biology, Eds. Ausabel et al., N.Y.: John Wiley & Sons, (1991)]. Also, a fusion gene coding for a purification leader sequence, such as a poly-(His)/enterokinase cleavage site sequence at the N-terminus of the desired C-terminal truncated C5a peptide, can allow purification of the expressed C-terminal truncated C5a fusion protein by affinity chromatography using, for example, a Ni2+ metal resin. The purification leader sequence can then be subsequently removed by treatment with enterokinase [see e.g., Hochuli et al., J. Chromatography 411:177 (1987)]. Techniques for making fusion genes are well known. Essentially, the joining of various DNA fragments coding for different polypeptide sequences is performed in accordance with conventional molecular biology techniques, employing blunt-ended or stagger-ended termini for ligation, restriction enzyme digestion to provide for appropriate termini, filling-in of cohesive ends as appropriate, alkaline phosphatase treatment to avoid undesirable joining, and enzymatic ligation. The fusion gene is synthesized by conventional techniques including automated DNA synthesizers. Alternatively, in other embodiments of the present invention, PCR amplification of gene fragments can be carried out using anchor primers which give rise to complementary overhangs between two consecutive gene fragments which is subsequently annealed to generate a chimeric gene sequence [see e.g., Current Protocols in Molecular Biology, Eds. Ausubel et al., Joln Wiley & Sons (1992)]. The C-terminal truncated C5a peptide sequences may be synthesized, whole or in part, using chemical methods well known in the art [see e.g., Caruthers et al., Nuc. Acids Res. Symp. Ser. 7:215-233 (1980); Crea and Horn, Nuc. Acids Res. 9:2331 (1980); Matteucci and Caruthers, Tetrahedron Lett 21:719 (1980); and Chow and Kempe, Nuc. Acids Res. 9:2807-2817 (1981)]. For example, C-terminal truncated C5a peptides can be synthesized by solid phase techniques, cleaved from the resin, and purified by preparative high performance liquid chromatography [see e.g., Creighton (1983) Proteins Structures And Molecular Principles, W H Freeman and Co, New York N.Y.]. In other embodiments of the present invention, the composition of the synthetic peptides may be confirmed by amino acid analysis or sequencing (see e.g., Creighton, supra). Direct peptide synthesis can be performed using various solid-phase techniques [Roberge et al., Science 269:202-204 (1995)] and automated synthesis may be achieved, for example, using ABI 431A Peptide Synthesizer (Perkin Elmer, Norwalk Conn.) in accordance with the instructions provided by the manufacturer. Additionally the amino acid sequence of the C-terminal truncated C5a peptide sequences may be altered during direct synthesis yielding various C-terminal truncated C5a peptides which are used to generate the anti-C5a antibodies of the present invention. Compounds mimicking the necessary conformation for generating the antibodies of the present invention are also contemplated as within the scope of the invention. For example, mimetics of the C-terminal truncated C5a peptides are contemplated. A variety of designs for such mimetics are possible. For example, cyclic C-terminal truncated C5a peptides, in which the necessary conformation for immunogenicity is stabilized by non-peptides, are specifically contemplated (See e.g. U.S. Pat. No. 5,192,746 to Lobl, et al., U.S. Pat. No. 5,169,862 to Burke, Jr., et al., U.S. Pat. No. 5,539,085 to Bischoff, et al., U.S. Pat. No. 5,576,423 to Aversa et al., U.S. Pat. No. 5,051,448 to Shashoua, and U.S. Pat. No. 5,559,103 to Gaeta et al., all of which describe muliple methods for creating such compounds). The present invention also contemplates non peptide compounds that mimic C-terminal truncated C5a peptides, as well as multimeric compounds that repeat the relevant peptide sequences. TABLE 1 C5a Sequences and Peptides Useful in Generating Antibodies Species SEQ ID NO: Amino Acid Sequence Rat C5a (full seq.) SEQ ID NO:1 DLQLLHQKVEEQAAKYKHRVP KKCCYDGARENKYETCEQRVA RVTIGPHCIRAFNECCTIADK IRKESHHKGMLLGR Rat C5a (residues 17-36) SEQ ID NO:2 KHRVPKKCCYDGARENKYET Human C5a (full seq.) SEQ ID NO:3 MLQKKIEEIAAKYKHSVVKKCC YDGASVNNDETCEQRAARISLG PRCIKAFTECCVVASQLRANIS HKDMQLGR Human C5a (res. 1-20) SEQ ID NO:4 MLQKKIEEIAAKYKHSVVKK Human C5a (res. 21-40) SEQ ID NO:5 CCYDGASVNNDETCEQRAAR Human C5a (res. 55-74) SEQ ID NO:6 CVVASQLRANISHKDMQLGR Human C5a (res. 12-20) SEQ ID NO:14 KYKHSVVKK Human C5a (res. 28-33) SEQ ID NO:15 VNNDET Human C5a (res. 38-46) SEQ ID NO:16 AARISLGPR Bovine C5a (full seq.) SEQ ID NO:7 MILKKKIEEEAAKYRNAWVKKC CYDGAHRNDDETCEERAARIAI GPECIKAFKSCCAIASQFRADE HHKNMQLGR Porcine C5a (full seq.) SEQ ID NO:8 MLQKKIEEEAAKYKYAMLKKC CYDGAYRNDDETCEERAARIK IGPKCVKAFKDCCYIANQVRA EQSHKNIQLGR TABLE 2 Rat and Human C5a Polynucleotide Sequences Useful in Generating C5a Peptides Species SEQ ID NO: Polynucleotide Sequence Human C5a (full seq.) SEQ ID NO:9 GATCCAGTATGTTGCAAAAAA AAATTGAAGAAATTGCTGCTA AATATAAACATTCTGTTGTTA AAAAATGTTGTTATGATGGAG CTTCTGTTAATAATGATGAAA CCTGCGAACAACGCGCTGCTA GAATTTCTTTGGGACCTAGAT GTATTAAAGCATTTACAGAAT GTTGTGTTGTTGCTTCTCAAT TGAGGCGAATATTTCTCATAA AGATATGCAATTGGGAAGATA GGATCCGTCGA Human C5a (for res. 1-20) SEQ ID NO:10 ATGTTGCAAAAAAAAATTG AAGAAATTGCTGCTAAATA TAAACATTCTGTTGTTAAA AAA Human C5a (for res. 21-40) SEQ ID NO:11 TGTTGTTATGATGGAGCTTC TGTTAATAATGATGAAACCT GCGAACAACGCGCTGCTAGA Human C5a (for res. 12-20) SEQ ID NO:17 TTGCTGCTAAATATAAACAT TCTGTTG Human C5a (for res. 28-33) SEQ ID NO:18 GAGCTTCTGTTAATAATG Human C5a (for res. 38-46) SEQ ID NO:19 AACAACGCGCTGCTAGAATT TCTTTGG Rat C5a (full seq.) SEQ ID NO:12 GACCTGCAGCTCCTGCATCAG AAAGTGGAAGAACAAGCTGCT AAATACAAACACCGTGTGCCC AAGAAATGCTGTTATGATGGA GCCCGAGAAAACAAATACGAA ACCTGTGAGCAGCGAGTTGCC CGGGTGACCATAGGCCCACAC TGCATCAGGGCCTTCAACGAG TGTTGTACTATTGCGGATAAG ATCCGAAAAGAAAGCCACCAC AAAGGCATGCTGTTGGGAAGG Rat C5a (for res. 17-36) SEQ ID NO:13 AAACACCGTGTGCCCAAGAAA TGCTGTTATGATGGAGCCCGA GAAAACAAATACGAAACC TABLE 3 C-Terminal Truncated C5a Peptide Sequences SEQ ID NO: Amino Acid Sequence SEQ ID NO:20 KYKHTVVKK SEQ ID NO:21 KYKHSAVKK SEQ ID NO:22 KYKHSAAKK SEQ ID NO:23 KYKHSVAKK SEQ ID NO:24 VNNQET SEQ ID NO:25 VNNDES SEQ ID NO:26 VNNQES SEQ ID NO:27 ANNDET SEQ ID NO:28 AARISIGPR SEQ ID NO:29 AARISVGPR SEQ ID NO:30 AARITLGPR SEQ ID NO:31 AVRISLGPR SEQ ID NO:32 VARISLGPR SEQ ID NO:33 VVRISLGPR SEQ ID NO:34 MLQKKIEEIAAKYKHSVVK SEQ ID NO:35 MLQKKIEEIAAKYKHSVV SEQ ID NO:36 MLQKKIEEIAAKYKHSV SEQ ID NO:37 MLQKKIEEIAAKYKHS SEQ ID NO:38 MLQKKIEEIAAKYKH SEQ ID NO:39 LQKKIEEIAAKYKHSVVKK SEQ ID NO:40 QKKIEEIAAKYKHSVVKK SEQ ID NO:41 KKIEEIAAKYKHSVVKK SEQ ID NO:42 KIEEIAAKYKHSVVKK SEQ ID NO:43 IEEIAAKYKHSVVKK SEQ ID NO:44 MIQKKIEEIAAKYKHSVVKK SEQ ID NO:45 MVQKKIEEIAAKYKHSVVKK SEQ ID NO:46 MLDKKIEEIAAKYKHSVVKK SEQ ID NO:47 MLQKKIEEIAAKYKHTVVKK SEQ ID NO:48 MLQKKIEEIVAKYKHSVVKK SEQ ID NO:49 MLQKKIEEIVVKYKHSVVKK SEQ ID NO:50 MLQKKIEEIAAKYKHSVAKK SEQ ID NO:51 MLQKKIEEIAAKYKHSAAKK SEQ ID NO:52 MLQKKIEEIAAKYKHSAVKK SEQ ID NO:53 MLQKKIEEIAVKYKHSVVKK SEQ ID NO:54 CCYDGASVNNDETCEQRAA SEQ ID NO:55 CCYDGASVNNDETCEQRA SEQ ID NO:56 CCYDGASVNNDETCEQR SEQ ID NO:57 CCYDGASVNNDETCEQ SEQ ID NO:58 CCYDGASVNNDETCE SEQ ID NO:59 CYDGASVNNDETCEQRAAR SEQ ID NO:60 YDGASVNNDETCEQRAAR SEQ ID NO:61 DGASVNNDETCEQRAAR SEQ ID NO:62 GASVNNDETCEQRAAR SEQ ID NO:63 ASVNNDETCEQRAAR SEQ ID NO:64 CCYQGASVNNDETCEQRAAR SEQ ID NO:65 CCYDGASVNNQETCEQRAAR SEQ ID NO:66 CCYQGASVNNQETCEQRAAR SEQ ID NO:67 CCYDGASVNNDESCEQRAAR SEQ ID NO:68 CCYDGATVNNDETCEQRAAR SEQ ID NO:69 CCYDGVSVNNDETCEQRAAR SEQ ID NO:70 CCYDGASANNDETCEQRAAR SEQ ID NO:71 CCYDGASVNNDETCEQRVAR SEQ ID NO:72 CCYDGASVNNDETCEQRVVR SEQ ID NO:73 CCYDGASVNNDETCEQRAVR SEQ ID NO:74 CCYDGVSANNDETCEQRVVR In one embodiment, the present invention contemplates a method of producing polygonal antibodies, comprising; providing an animal and an immunogenic composition, wherein the composition comprises C-terminal truncated C5a peptides; and immunizing the animal with the immunogenic composition in order to generate antibodies. It is not intended that the present invention be limited to particular C-terminal truncated peptides. A variety of C-terminal truncated peptides are contemplated. In one embodiment, the C-terminal truncated peptide corresponds to the entire N-terminal
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