Dr Antony Antoniou Research Group
Dr Antoniou has held an ARC Fellowship since 2004.
His research group is focussed on research into the biology of the Major Histocompatibility Complex (MHC) Class I molecule HLA-B27 (picture). HLA-B27 exhibits a strong association with the inflammatory arthritic disorder, Ankylosing Spondylitis (AS). Approx. 95% of AS patients express HLA-B27.
The Group is investigating the unusual biochemistry of HLA-B27 and trying to determine whether the biochemical characteristics exhibited by HLA-B27 could explain the association with AS.
Dr Antoniou works with UCL's Centre for Rheumatology.
Dr Antony N Antoniou
Research Group: Members
Current: Dr David Guiliano; Izabela Lenart, PhD student
Past: Dr Helen North
Our research is focused on the biology of the Major Histocompatibility Complex (MHC) Class I molecule HLA-B27 (picture). MHC class I molecules function to present peptides primarily derived from endogenous proteins to cytotoxic T cells at the cell surface and act as ligands for Natural Killer cells. MHC class I molecules assembly and acquire peptide within the lumen of the endoplasmic reticulum (pictures: MHC Molecules; Peptide Loading Complex).
HLA-B27 exhibits a strong association with the inflammatory arthritic disorder, Ankylosing Spondylitis (AS). Approx. 95% of AS patients express HLA-B27. Many theories have been proposed to explain the role of HLA-B27 in the disease process. My lab is investigating the unusual biochemistry of HLA-B27 and trying to determine whether the biochemical characteristics exhibited by HLA-B27 could explain the association with AS.
The lab is especially interested in the enhanced propensity for HLA-B27 to misfold and in defining the consequences of misfolding. Recently, toxicity caused by protein misfolding has been linked to pathogenesis in a variety of diseases such as cystic fibrosis and Alzheimer’s disease, by inducing the unfolded protein response (UPR). It is possible that HLA-B27 misfolding could similarly induce the UPR. The lab is therefore investigating how HLA-B27 misfolds, folds and traffics within the cell.
HLA-B27 also exhibits a strong association with another inflammatory arthritic disorder referred to as Reactive Arthritis (ReA). This arthritic condition follows infections by bacteria such as Salmonella and Campylobacter. The lab, in collaboration with Dr. Noursadeghi and Dr. Bajaj-Elliott is interested in trying to understand the relationship between Salmonella/Campylobacter and HLA-B27 both at the cellular (picture) and biochemical level.
As well as HLA-B27, the lab is also investigating the folding of MHC class I molecules and how ER resident chaperones aid in this process, in particular the oxidoreductase ERp57, calnexin and BiP.
The lab also has a general interest in investigating how viral gene products can interfere and inhibit MHC class I molecule expression. We currently have interests in the role of Human Immunodeficiency Virus (HIV) accessory proteins such as Vpu and Nef in this process, the human cytomegalovirus (HCMV) genes US2 and US11 and the Kaposi’s sarcoma-associated herpes virus (KSHV) products K3 and K5.
UCL: Prof. A. Segal, Dr M. Nouradeghi
ICH: Dr. Bajaj-Elliott
National: Dr Simon Powis, St Andrews University, Dr. Keith Gould Imperial College, Prof. Salim Khakoo Imperial, Dr Stuart Neil, Kings College
International: Dr. N Garbi (Heidelberg, Germany), Prof. G. Hammerling (Heidelberg, Germany), Dr. M. Molinari (Basel, Switzerland)
Page last modified on 23 feb 11 12:54 by Karen Rumsey