Professor Roy Jefferis is Professor Emeritus at University of Birmingham and an expert on antibody structure and function.
Emeritus Professor of Molecular Immunology
Background and Research focus
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.
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.
Jefferis R. Isotype and glycoform selection for antibody therapeutics. Arch Biochem Biophys. 2012 Oct 15;526(2):159-66. doi: 10.1016/j.abb.2012.03.021. Epub 2012 Mar 23. Review. PubMed PMID: 22465822.
Jefferis R. The antibody paradigm: present and future development as a scaffold for biopharmaceutical drugs. Biotechnol Genet Eng Rev. 2010;26:1-42. Review.
Jefferis R. Glycosylation as a strategy to improve antibody-based therapeutics. Nat Rev Drug Discov. 2009 Mar;8(3):226-34.
Jefferis R, Lefranc MP. Human immunoglobulin allotypes: possible implications for immunogenicity. MAbs. 2009 Jul-Aug;1(4):332-8. Review.
Jefferis R. Aglycosylated antibodies and the methods of making and using them: WO2008030564. Expert Opin Ther Pat. 2009 Jan;19(1):101-5.
Jefferis R. Glycosylation of recombinant antibody therapeutics. Biotechnol Prog. 2005 Jan-Feb;21(1):11-6. Review.
Jefferis R, Lund J. Interaction sites on human IgG-Fc for FcgammaR: current models. Immunol Lett. 2002 Jun 3;82(1-2):57-65. Review.
Mimura Y, Sondermann P, Ghirlando R, Lund J, Young SP, Goodall M, Jefferis R.Role of oligosaccharide residues of IgG1-Fc in Fc gamma RIIb binding. J Biol Chem. 2001 Dec 7;276(49):45539-47.
Jefferis R, Lund J, Pound JD. IgG-Fc-mediated effector functions: molecular definition of interaction sites for effector ligands and the role of glycosylation. Immunol Rev. 1998 Jun;163:59-76. Review.