Rizkallah, Pierre - Cardiff University

个人简介

I am a Chemistry graduate, at BSc and PhD level. I use Physics applications to study biological macromolecules, a field known as Structural Biology. I have extensive experience with X-ray crystallography and 3D structure determination using synchrotron radiation. I have used the allied techniques of Small Angle X-ray Scattering (SAXS) and Circular Dichroism (CD) to shed light on biological mechanisms. I have served on committees and participated in programs at national and international levels. I have conducted many outreach and media exercises during the course of my career, communicating the immediacy relevance and importance of Science in everyday life. I had a brief period of experience in the cosmetics industry, leading a production line team.

研究领域

Immune System Proteins: This work aims to determine the structural factors involved in the cross-reactivity of Thymus-derived cell receptors, TCRs, when they recognise more than one antigen presented in the context of the Major Histocompatibility complex, a mechanism underlying autoimmunity. A second aspect is the degeneracy of TCR binding to various antigens presented by one MHC to allow wide coverage of possible antigens with the limited number of MHCs an individual has. The project involves using X-ray crystallography for solving 3D structures of these entities, and conducting binding studies with surface plasmon resonance, isothermal titration calorimetry and naive T-cell activation. The research is carried out within the T-cell Modulation Group led by Prof Andrew Sewell, in the Institute of Infection and Immunology.

近期论文

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Cole, D.et al. 2017. Structural mechanism underpinning cross-reactivity of a CD8+ T-cell clone that recognises a peptide derived from human telomerase reverse transcriptase. Journal of Biological Chemistry 292(3), pp. 802-813. (10.1074/jbc.M116.741603) pdf Nomikos, M.et al. 2016. Mutations in PLCd1 associated with hereditary leukonychia display divergent PIP2 hydrolytic function. FEBS Journal 283(24), pp. 4502-4514. (10.1111/febs.13939) pdf Hartley, A.et al. 2016. Molecular basis for functional switching of GFP by two disparate non-native post-translational modifications of a phenyl azide reaction handle. Chemical Science 7(10), pp. 6484-6491. (10.1039/C6SC00944A) Cole, D.et al. 2016. Hotspot autoimmune T cell receptor binding underlies pathogen and insulin peptide cross-reactivity. The Journal of Clinical Investigation 126(6), pp. 2191-2204. (10.1172/JCI85679) pdf Bianchi, V.et al. 2016. A Molecular Switch Abrogates Glycoprotein 100 (gp100) T-cell Receptor (TCR) Targeting of a Human Melanoma Antigen. Journal of Biological Chemistry 291(17), pp. 8951-8959. (10.1074/jbc.M115.707414) pdf Raman, M.et al. 2016. Direct molecular mimicry enables off-target cardiovascular toxicity by an enhanced affinity TCR designed for cancer immunotherapy. Scientific Reports 6, article number: 18851. (10.1038/srep18851) pdf Reddington, S.et al. 2015. Genetically encoded phenyl azide photochemistry drives positive and negative functional modulation of a red fluorescent protein. RSC Advances 5(95), pp. 77734-77738. (10.1039/C5RA13552D) pdf Adams, S.et al. 2015. Conformationally restricted calpain inhibitors. Chemical Science 6(12), pp. 6865-6871. (10.1039/c5sc01158b) pdf Motozono, C.et al. 2015. Distortion of the major histocompatibility complex class I binding groove to accommodate an insulin-derived 10-Mer peptide. Journal of Biological Chemistry 290(31), pp. 18924-18933. (10.1074/jbc.M114.622522) pdf Reid, R.et al. 2015. CD8+ T-cell recognition of a synthetic epitope formed by t-butyl modification. Immunology 144(3), pp. 495-505. (10.1111/imm.12398) pdf Reid, R.et al. 2015. CD8+T-cell recognition of a synthetic epitope formed byt-butyl modification. Immunology 144(3), pp. 495-505. (10.1111/imm.12398)