I joined the University of Nottingham Therapeutic Antibody Centre (NUTAC), under the direction of Professor Lindy Durrant, as a Senior Research Fellow in March 2013. Prior to this I was part of the School of Molecular Medical Sciences, based in the Centre for Biomolecular Sciences, in the Antimicrobial Research Group, headed by Professor Richard James.
My first postdoctoral position was at the University of Sheffield Medical School, where I previously obtained my PhD (in 2000) under the supervision of Dr David Buttle, in the Arthritis Research Laboratory of Professor Anthony Hollander.
I gained a Pharmacy Degree (in 1995) from the University of Ghent, Belgium, where I briefly joined the Faculty as a Research Associate.
My main expertise lays within the field of protein biochemistry where I have researched protein-protein and protein-membrane interactions in a range of settings, from cartilage breakdown in arthritis to antimicrobial toxin biology.
More recently, I am expanding this experience to therapeutic antibodies and cancer cell biology.
I currently teach a number of therapeutic antibody modules on the MSc Cancer Immunology and Biotechnology.
My current research is focused on generating therapeutic antibodies against cancer cell - associated glycans and their development for use in the clinic. We are specifically interested in their… read more
VANKEMMELBEKE, M., ZHANG, Y., MOORE, G.R., KLEANTHOUS, C., PENFOLD, C.N. and JAMES, R., 2009. Energy-dependent immunity protein release during tol-dependent nuclease colicin translocation Journal of Biological Chemistry. 284(28), 18932-18941 BONSOR, D.A., HECHT, O., VANKEMMELBEKE, M., SHARMA, A., KRACHLER, A.M., HOUSDEN, N.G., LILLY, K.J., JAMES, R., MOORE, G.R. and KLEANTHOUS, C., 2009. Allosteric β-propeller signalling in TolB and its manipulation by translocating colicins EMBO Journal. 28(18), 2846-2857 ZHANG, Y., LI, C., VANKEMMELBEKE, M.N., BARDELANG, P., PAOLI, M., PENFOLD, C.N. and JAMES, R., 2010. The crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins Molecular Microbiology. 75(3), 623-636
BARDELANG, P., VANKEMMELBEKE, M., ZHANG, Y., JARVIS, H., ANTONIADOU, E., ROCHETTE, S., THOMAS, N.R., PENFOLD, C.N. and JAMES, R., 2009. Design of a polypeptide FRET substrate that facilitates study of the antimicrobial protease lysostaphin Biochemical Journal. 418, 615-624
My current research is focused on generating therapeutic antibodies against cancer cell - associated glycans and their development for use in the clinic. We are specifically interested in their oncolytic mechanisms (immune-mediated and direct) for which we are using in vitro and in vivo studies combined with protein engineering
I trained as a pharmacist at the University of Ghent (Belgium) after which I took up a research position at the faculty. In this post, I characterised antibodies against type II collagen cleavage products with a view to develop them into a diagnostic tool for cartilage breakdown in arthritis. I subsequently moved to Sheffield where I gained a PhD in biochemistry. During this time, I developed an in vitro co-culture model with which to study soft connective tissue-induced cartilage breakdown in arthritis. I followed this up during my first post-doc where I cloned three mammalian enzymes involved in cartilage aggrecan breakdown and studied their activity profile and their inhibition by green tea constituents.
Next, I became involved in bacteriocin research at the University of Nottingham. This research has mainly centred on elucidating the cellular entry mechanisms of colicins (E. coli bacteriocins). I developed a number of sensitive biological assays for colicin cell entry and activity that have enabled me to study the energetic requirements for colicin uptake. We have also been able to study the competition dynamics of different colicin-containing strains in real-time using fluorescence reporters. More recently, I used a range of biochemical and biophysical approaches to study the membrane interactions of colicin cytotoxic domains.