Following a BSc and PhD in Chemistry (Birmingham), Roy moved to the Medical School to initiate a research programme investigating the structure and function of antibody molecules, in health and disease. Latterly, studies have elucidated the crucial role that glycosylation of the IgG antibody has on the activation of downstream effector mechanisms, both in vitro and in vivo. These findings have substantial implications for protein/glycosylation engineering in the design of recombinant antibody therapeutics and led to a number of consultancies within the biopharmaceutical industry. A current focus is mechanisms potentiating immunogenicity of therapeutic IgG molecules, including the impact of aggregates, immune complexes and allotype mismatches, between therapeutic IgG and the patient’s IgG haplotype. Roy’s expertise is reflected in ~300 publications; in consideration of published research; he has been awarded the degree of Doctor of Science (DSc) and elected a Member of the Royal College of Physicians (MRCP) and Fellow of the Royal College of Pathologists (FRCPath).
Antibody structure and function; antibody engineering; antibody therapeutics; biologics; recombinant antibodies; biosimilar and bio-better antibodies; post-translational modification; glycosylation; deglycosylation; oligosaccharide engineering; glycoforms; immunoglobulin domains; immunoglobulin free light chains; immunodiagnostics.
In addition to leading his own research group, Roy holds consultancies with a number of pharmaceutical companies in relation to therapeutic antibody optimization, and antibody engineering.
Jefferis R. Protein heterogeneity and the immunogenicity of biotherapeutics. GaBi J 7: 2018 In press.
Jefferis R. Glyco-Engineering of Human IgG-Fc to Modulate Biologic Activities. Curr Pharm Biotechnol. 2016;17(15):1333-1347. doi:10.2174/1389201017666161029225929.
Jefferis R. Posttranslational Modifications and the Immunogenicity of Biotherapeutics. J Immunol Res. 2016;2016:5358272. doi: 10.1155/2016/5358272. Epub 2016 Apr 14. Review.
Chang DK, Kurella VB, Biswas S, Avnir Y, Sui J, Wang X, Sun J, Wang Y, Panditrao M, Peterson E, Tallarico A, Fernandes S, Goodall M, Zhu Q, Brown JR, Jefferis R, Marasco WA. Humanized mouse G6 anti-idiotypic monoclonal antibody has therapeutic potential against IGHV1-69 germline gene-based B-CLL. MAbs. 2016 May-Jun;8(4):787-98. doi: 10.1080/19420862.2016.1159365. Epub 2016 Mar 10.
Mimura Y, Kelly RM, Unwin L, Albrecht S, Jefferis R, Goodall M, Mizukami Y, Mimura-Kimura Y, Matsumoto T, Ueoka H, Rudd PM. Enhanced sialylation of a human chimeric IgG1 variant produced in human and rodent cell lines. J Immunol Methods. 2016 Jan;428:30-6. doi: 10.1016/j.jim.2015.11.009. Epub 2015 Nov 26.
Wuhrer M, Stavenhagen K, Koeleman CA, Selman MH, Harper L, Jacobs BC, Savage CO, Jefferis R, Deelder AM, Morgan M. Skewed Fc glycosylation profiles of anti-proteinase 3 immunoglobulin G1 autoantibodies from granulomatosis with polyangiitis patients show low levels of bisection, galactosylation, and sialylation. J Proteome Res. 2015 Apr 3;14(4):1657-65. doi: 10.1021/pr500780a. Epub 2015 Mar 24.
Davies AM, Rispens T, Ooijevaar-de Heer P, Gould HJ, Jefferis R, Aalberse RC, Sutton BJ. Structural determinants of unique properties of human IgG4-Fc. J Mol Biol. 2014 Feb 6;426(3):630-44. doi: 10.1016/j.jmb.2013.10.039. Epub 2013 Nov 6.
Campbell JP, Cobbold M, Wang Y, Goodall M, Bonney SL, Chamba A, Birtwistle J, Plant T, Afzal Z, Jefferis R, Drayson MT. Development of a highly-sensitive multi-plex assay using monoclonal antibodies for the simultaneous measurement of kappa and lambda immunoglobulin free light chains in serum and urine. J Immunol Methods. 2013 May 31;391(1-2):1-13.