Dr Fiyaz Mohammed

Institute of Immunology and Immunotherapy
Lecturer in Biomedical Structural Biology

Contact details

Address
Institute of Immunology and Immunotherapy
College of Medical and Dental Sciences
Robert Aitken Institute of Clinical Research
University of Birmingham
Edgbaston
Birmingham
B15 2TT
UK

Fiyaz is a Lecturer in Biomedical Structural Biology in the Institute of Immunology and Immunotherapy, University of Birmingham. His research focuses on investigating immune cell surface receptor/ligand interactions relevant to cancer using X-ray crystallography.

He has published a number of peer reviewed research papers on clinically relevant immune receptor recognition events including those underpinning alloreactive T cell receptor/peptide-MHC recognition and T cell recognition of post-translationally modified peptides. His currently focussed on understanding the molecular and structural basis gamma delta T cell recognition.

Qualifications

  • Lecturer in Biomedical Structural Biology, 2012
  • PhD in X-ray Crystallography, 2001
  • BSc (Hons) in Biochemistry, 1996

Biography

Fiyaz obtained a BSc (Hons) in Biochemistry (1996) from the University of Wolverhampton. He gained extensive experience in protein X-ray crystallography methods whilst undertaking a PhD and subsequent postdoctoral studies in the groups of Professors Steve Wood and Jon Cooper at the University of Southampton. His research focused on determining the structure and catalytic mechanism of key enzymes linked to bipolar disorder, acute intermittent porphyria, degradation of xenobiotic compounds and the bacterial electron transport chain.

In 2004 he came to the University of Birmingham to join the laboratory of Professor Benjamin Willcox as a research fellow studying the molecular and structural basis of clinically important immune receptor recognition events. In particular, he made significant contributions to those underpinning alloreactive TCR-pMHC recognition events and T cell recognition of post-translationally modified peptides.

In 2012 he was appointed a Lecturer in Biomedical Structural Biology focused on investigating the immune cell surface receptor/ligand interactions relevant to cancer using X-ray Crystallography. His current focus is on understanding the molecular basis of gamma delta T cell recognition, an area that is of growing interest to industry.

He is also exploring the structural and molecular basis of CD248 and CLEC14A function, two key family members that have roles in tumour angiogenesis and inflammation. Finally, Fiyaz has a growing interest in understanding the structure and function of desmosomal proteins which is important for understanding the biology of epithelial tissues and cardiac muscle in normal development and disease.

Teaching

Dr Mohammed currently leads the Cancer Immunology and Immunotherapy module as part of the MRes in Cancer Sciences course. He also contributes to the following programmes:

Postgraduate supervision

Dr Mohammed supervises PhD and MSc students.

If you are interesting in studying any of these subject areas please contact Dr Fiyaz Mohammed directly, or for any general doctoral research enquiries, please email mds-gradschool@contacts.bham.ac.uk.

For a full list of available Doctoral Research opportunities, please visit our Doctoral Research programme listings.

Research

Dr Mohammed’ research focus is on investigating immune cell surface receptor/ligand interactions relevant to cancer using structural biology approaches such as X-ray crystallography. In particular, he has a long standing interest in the following key areas:

Gamma delta T cell recognition

γδ T cells are poorly understood class of lymphocyte strongly implicated in surveillance of cellular stress recognizing target cells that are infected or transformed. In collaboration with Professor Ben Willcox, Dr Mohammed is focused on understanding how γδ T cell ligands are recognized at a molecular level.

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”. 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.

Stem Cell Transplantation (SCT)

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 SCT. Dr Mohammed, in collaboration with Professors Paul Moss and Ben 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.

Tumour Angiogenesis

Dr Mohammed is interested in examining the structure, function and ligand identification of CLEC14A and CD248 (in collaboration with Professors Roy Bicknell and Chris Buckley), a group of receptors that are heavily implicated in tumour angiogenesis and progression. This is likely to facilitate design of small molecule drugs as novel anti-angiogenic therapeutics for cancer.

Other activities

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

Recent publications

Article

Odintsova, E, Mohammed, F, Trieber, C, Rodriguez-Zamora, P, Al-Jassa, C, Huang, T-H, Fogl, C, Knowles, T, Sridhar, P, Kumar, J, Jeeves, M, Chidgey, M & Overduin, M 2020, 'Binding of the periplakin linker requires vimentin acidic residues D176 and E187', Communications Biology, vol. 3, no. 1, 83. https://doi.org/10.1038/s42003-020-0810-y

Karunakaran, MM, Willcox, CR, Salim, M, Paletta, D, Fichtner, AS, Noll, A, Starick, L, Nöhren, A, Begley, CR, Berwick, KA, Chaleil, RAG, Pitard, V, Déchanet-merville, J, Bates, PA, Kimmel, B, Knowles, TJ, Kunzmann, V, Walter, L, Jeeves, M, Mohammed, F, Willcox, BE & Herrmann, T 2020, 'Butyrophilin-2A1 directly binds germline-encoded regions of the Vγ9Vδ2 TCR and is essential for phosphoantigen sensing', Immunity, vol. 52, no. 3, pp. 487-498.e6. https://doi.org/10.1016/j.immuni.2020.02.014

Mohammed, F, Trieber, C, Overduin, M & Chidgey, M 2020, 'Molecular mechanism of intermediate filament recognition by plakin proteins', Biochimica et Biophysica Acta. Molecular Cell Research, vol. 1867, no. 11, 118801. https://doi.org/10.1016/j.bbamcr.2020.118801

Willcox, CR, Mohammed, F & Willcox, BE 2020, 'The distinct MHC‐unrestricted immunobiology of innate‐like and adaptive‐like human γδ T cell subsets—Nature's CAR‐T cells', Immunological Reviews, vol. 298, no. 1, pp. 25-46. https://doi.org/10.1111/imr.12928

Willcox, BE, Mohammed, F & Willcox, CR 2020, 'γδ TCR Recognition of MR1: Adapting to Life on the Flip Side', Trends in Biochemical Sciences, vol. 45, no. 7, pp. 551-553. https://doi.org/10.1016/j.tibs.2020.03.012

Willcox, C, Vantourout, P, Salim, M, Zlatareva, I, Melandri, D, Zanardo, L, George, R, Kjaer, S, Jeeves, M, Mohammed, F, Hayday, AC & Willcox, B 2019, 'Butyrophilin-like 3 directly binds a human Vγ4+ t cell receptor using a modality distinct from clonally-restricted antigen', Immunity, vol. 51, no. 5, pp. 813-825.e4. https://doi.org/10.1016/j.immuni.2019.09.006

Thomas, S, Mohammed, F, Reijmers, R, Woolston, A, Stauss, T, Kennedy, A, Stirling, D, Holler, A, Green, L, Jones, D, Matthews, KK, Price, DA, Chain, B, Heemskerk, MHM, Morris, E, Willcox, B & Stauss, HJ 2019, 'Framework engineering to produce dominant T cell receptors with enhanced antigen-specific function', Nature Communications, vol. 10, no. 1, 4451. https://doi.org/10.1038/s41467-019-12441-w

Ramasamy, R, Mohammed, F & Meier, U-C 2019, 'HLA DR2b-binding peptides from human endogenous retrovirus envelope, Epstein-Barr virus and brain proteins in the context of molecular mimicry in multiple sclerosis', Immunology Letters, vol. 217, pp. 15-24. https://doi.org/10.1016/j.imlet.2019.10.017

Jamshad, M, Knowles, TJ, White, SA, Ward, DG, Mohammed, F, Rahman, KF, Wynne, M, Hughes, GW, Kramer, G, Bukau, B & Huber, D 2019, 'The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity', eLife, vol. 8, e48385. https://doi.org/10.7554/eLife.48385.001

Mohammed, F, Stones, D & Willcox, B 2018, 'Application of the immunoregulatory receptor LILRB1 as a crystallisation chaperone for human class I MHC complexes', Journal of Immunological Methods. https://doi.org/10.1016/j.jim.2018.10.011

Zuo, J, Mohammed, F & Moss, P 2018, 'The Biological Influence and Clinical Relevance of Polymorphism Within the NKG2D Ligands', Frontiers in immunology, vol. 9, 1820. https://doi.org/10.3389/fimmu.2018.01820

Davey, M, Willcox, C, Hunter, S, Kasatskaya, SA, Remmerswaal, EBM, Salim, M, Mohammed, F, Bemelman, FJ, Chudakov, DM, Oo, YH & Willcox, B 2018, 'The human Vδ2+ T-cell compartment comprises distinct innate-like Vγ9+ and adaptive Vγ9- subsets', Nature Communications, vol. 9, no. 1, 1760. https://doi.org/10.1038/s41467-018-04076-0

Zuo, J, Willcox, C, Mohammed, F, Davey, M, Hunter, S, Khan, K, Antoun , A, Katakia, P, Croudace, J, Inman, C, Parry, H, Briggs, D, Malladi, R, Willcox, B & Moss, P 2017, 'A disease-linked ULBP6 polymorphism inhibits NKG2D-mediated target cell killing by enhancing the stability of NKG2D ligand binding', Science signaling, vol. 10, no. 481, eaai8904. https://doi.org/10.1126/scisignal.aai8904

Review article

Mohammed, F & Chidgey, M 2021, 'Desmosomal protein structure and function and the impact of disease-causing mutations', Journal of Structural Biology, vol. 213, no. 3, 107749. https://doi.org/10.1016/j.jsb.2021.107749

Khan, KA, McMurray, JL, Mohammed, F & Bicknell, R 2019, 'C-type lectin domain group 14 proteins in vascular biology, cancer and inflammation', The FEBS journal, vol. 286, no. 17, pp. 3299-3332. https://doi.org/10.1111/febs.14985

View all publications in research portal