Dr Fiyaz Mohammed

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Dr Fiyaz Mohammed is a protein crystallographer with a long standing interest in immune receptor structure and function.
Position:

Lecturer in Biomedical Structural Biology, School of Cancer Sciences, College of Medical Sciences and Dentistry, University of Birmingham

Email: f.mohammed@bham.ac.uk

Background and Research focus

Dr Mohammed is a Lecturer in Biomedical Structural Biology who is focussed on investigating immune cell surface receptor/ligand interactions relevant to cancer using X-ray crystallography. In particular, he has a long standing interest in post translational immunology. Phosphopeptide antigens are emerging as a novel class of tumour-associated antigen presented by MHC molecules and recognised by T cells. Since disregulated phosphorylation is a hallmark of malignant transformation, presentation of an altered repertoire of phosphopeptide antigens on cancer cells may represent a distinct and therapeutically targetable immunological signature of “transformed self”. In collaboration with Professor Willcox and Dr Cobbold, Fiyaz is investigating the molecular basis of phosphopeptide presentation by MHC molecules and recognition by T-cells. These studies should establish the mode of presentation for a key subset of MHC-restricted tumour associated phosphopeptides and facilitate attempts to target them therapeutically. Latterly, Dr Mohammed has developed an interest in understanding the role of NKG2D ligands in lymphoid stress recognition in cancer. NKG2D is an activatory receptor that is expressed on a range of immune effector cells which engages stress induced ligands which include members of the ULBP family. Recent studies have highlighted that polymorphisms in the stress induced molecule, ULBP6, in patients with haematological malignancies play a critical role in determining the outcome of Stem Cell Transplantation (SCT). Dr Mohammed, in collaboration with Professors Moss and Willcox, is examining the molecular properties of the NKG2D/ULBP6 complex interaction with the aim of defining the mechanisms underlying curative anti-tumour responses following SCT.

Expertise

X-ray crystallography; tumour immunology; post-translational immunology; receptor/ligand interactions; protein expression and purification.

Other activities

In collaboration with Professor Roy Bicknell, Fiyaz is interested examining the structure, function and ligand identification of CLEC14A, a receptor that is heavily implicated in tumour angiogenesis. This study is likely to facilitate design of small molecule drugs as novel anti-angiogenic therapeutics for cancer. In addition to starting his own research group, Fiyaz makes substantial contributions to teaching at many levels. He is currently the module lead in Molecular Approaches to Drug Development of the new MSc in Translational Medicine. Moreover, he lectures on structural biology techniques and tumour immunology to undergraduates and postgraduates reading Biochemistry, Biology and Medicine. He is also closely affiliated with the Cancer Immunology and Immunotherapy Centre (CIIC) with a major role in developing and maintaining the CIIC website. Finally, he sits on the University of Birmingham Protein Expression Facility Advisory Board.

Publications

Willcox C, Mohammed F and Willcox B.E. (2013). Resolving the mystery of pyrophosphate antigen presentation. Nat Immunol 14, 886-887 (2013)

Mohammed-F*, Simpson-AA*, Salim-M, Tranter-A, Rickinson-AB, Stauss-HJ, Moss-PAH, Steven-NM and Willcox-BE. (2011). Structural and energetic evidence for highly peptide-specific tumor antigen targeting via Allo-MHC-restriction. Proc Natl Acad Sci 108(52):21176-81

Cheng-H, Mohammed-F, Nam-G, Chen-C, Qi-J, Garner-LI, Allen-RL, Yan-J, Willcox-BE and Gao-GF. (2011). Crystal structure of Leukocyte Immunoglobulin-like Receptor LILRB4: a myeloid inhibitory receptor involved in immune tolerance.  J Biol Chem 286(20): 18013-25

Nicholls-S, Piper-KP, Mohammed-F, Dafforn-TR, Salim-M, Tenzer-S, van Endert-P, Schild-H, Cobbold-M, Engelhard-VH, Moss-PAH and Willcox-BE. (2009). Secondary anchor polymorphism in the HA-1 minor histocompatibility antigen critically affects MHC stability and TCR recognition. Proc Natl Acad Sci 106(10):3889-94.

Mohammed-F*, Cobbold-M*, Zarling-AL, Salim-M, Barret-Wilt-GA, Shabanowitz-J, Hunt-DF, Engelhard-VH and Willcox-BE. (2008). Phosphorylation-dependent interaction between antigenic peptides and MHC class I: a molecular basis for the presentation of transformed self. Nat Immunol 9(11): 1236-43

*These authors contributed equally