20062019
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Personal profile

Biography

Dr. Richard Berry is an NHMRC Career Development Fellow based in the Dept. Biochemistry and Molecular Biology at Monash University. He received his PhD within the Wellcome Trust Centre for Cell-Matrix Research at the University of Manchester, UK in 2009 before moving to Australia in the laboratory of Prof. Jamie Rossjohn. In the subsequent 9 years, Richard’s research has focused on structural immunology. Within this theme, his research has resulted in a number of significant publications (e.g. Nature, Cell, Nature Immunology and PNAS) and awards including two NHMRC fellowships, a Young Scientist Program Fellowship from the IUBMB and a Lorne Proteins Young Investigator award.

Research interests

The specificity of the immune system is determined by cell surface receptors that recognise molecules of self- and/or viral origin. Understanding these interactions at the molecular level can provide profound insights into the basic processes underpinning immunity and how these may be modulated to treat infection or disease. My research is focused on three broad areas within this theme; 1. understanding the mechanistic basis of immune receptor triggering, with a particular focus on the T-cell receptor-CD3 signalling apparatus, 2. investigating how natural killer cell receptors function in both healthy and virally infected organisms, and 3. understanding the structural basis of immune checkpoints. To investigate these processes, my lab uses a wide range of structural and biophysical techniques including surface plasmon resonance, X-ray crystallography, cryo-EM, small angle X-ray scattering and analytical ultracentrifugation. Importantly, we strive to link our structural insights to biological function, and have developed a network or national and international collaborators (immunologists, cell biologists and virologist) to aid in this endeavour.

Keywords

  • Immune System, Protein chemistry, structural biology, Natural killer cell receptors, T cell receptor, innate immunity, cryo-electron microscopy

Network Recent external collaboration on country level. Dive into details by clicking on the dots.

Research Output 2006 2019

A subset of HLA-DP molecules serve as ligands for the natural cytotoxicity receptor NKp44

Niehrs, A., Garcia-Beltran, W. F., Norman, P. J., Watson, G. M., Hölzemer, A., Chapel, A., Richert, L., Pommerening-Röser, A., Körner, C., Ozawa, M., Martrus, G., Rossjohn, J., Lee, J-H., Berry, R., Carrington, M. & Altfeld, M., 29 Jul 2019, (Accepted/In press) In : Nature Immunology. 9 p.

Research output: Contribution to journalArticleResearchpeer-review

Structural Basis for CD96 Immune Receptor Recognition of Nectin-like Protein-5, CD155

Deuss, F. A., Watson, G. M., Fu, Z., Rossjohn, J. & Berry, R., 5 Feb 2019, In : Structure. 27, 2, p. 219-228 10 p.

Research output: Contribution to journalArticleResearchpeer-review

Structural basis for the recognition of nectin-like protein-5 by the human-activating immune receptor, DNAM-1

Deuss, F. A., Watson, G. M., Goodall, K. J., Leece, I., Chatterjee, S., Fu, Z., Thaysen-Andersen, M., Andrews, D. M., Rossjohn, J. & Berry, R., 16 Aug 2019, In : Journal of Biological Chemistry. 294, 33, p. 12534-12546 13 p.

Research output: Contribution to journalArticleResearchpeer-review

Open Access
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Recognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition

Balaji, G. R., Aguilar, O. A., Tanaka, M., Shingu-Vazquez, M. A., Fu, Z., Gully, B. S., Lanier, L. L., Carlyle, J. R., Rossjohn, J. & Berry, R., 5 Nov 2018, In : Nature Communications. 9, 1, 12 p., 4623.

Research output: Contribution to journalArticleResearchpeer-review

Open Access
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A highly conserved sequence of the viral TAP inhibitor ICP47 is required for freezing of the peptide transport cycle

Matschulla, T., Berry, R., Gerke, C., Döring, M., Busch, J., Paijo, J., Kalinke, U., Momburg, F., Hengel, H. & Halenius, A., 1 Dec 2017, In : Scientific Reports. 7, 1, 13 p., 2933.

Research output: Contribution to journalArticleResearchpeer-review

Open Access
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