Two NIMR scientists elected as EMBO members

19 October 2009

We are pleased to learn that two more NIMR scientists, Anne O'Garra and Steve Smerdon, have been elected as EMBO members this year. Election as an EMBO Member is a tribute to the significant contribution to the advancement of science made by each of these researchers.

EMBO Membership is a life-long honour and scientists are elected annually on the basis of proven excellence in research. This year 66 new members have been elected, and total EMBO membership now comprises 1,420 of the world's foremost molecular biologists. New EMBO Members are invited to present on their research at the 2010 EMBO Members Workshop to be held in Barcelona from 4-7 September 2010.

Anne O'Garra

Anne O'Garra is head of NIMR's Division of Immunoregulation. Dr O'Garra has worked for several years on interleukin-10 (IL-10) and IL-12, cytokines that play crucial roles in defining the immune response. She has made seminal contributions to our understanding of the intricate network of cell-cell and cytokine interactions responsible for inducing and inhibiting cellular immune responses. She first elucidated that interleukin 10 (IL-10) has broad immunosuppressive functions, inhibiting antigen presentation by dendritic cells and macrophages and their production of inflammatory cytokines. She elucidated fundamental mechanisms regulating the activation of T-cell subsets with distinct effector functions, discovering that: IL-12 induced T-helper 1 (Th1) cells secreting IFN, essential for eradication of intracellular pathogens; the key antigen presenting cell, the dendritic cell, produced IL-12, under tight control of IL-10.

Steve Smerdon

Steve Smerdon is joint head of NIMR's Division of Molecular Structure. As a post-doc at Yale with Tom Steitz Dr Smerdon tackled the structural basis of specificity and inhibitor-binding of HIV-1 reverse transcriptase. His work revealed details of the binding site for clinically relevant non-nucleoside inhibitors, and an intrinsic plasticity that is crucial for formation of the p66/p51 heterodimer and viral replication. In 1995 Steve moved to NIMR and his primary interest is now in the significance of phosphorylation as a switch for multi-protein complex assembly, with a focus on signalling events that regulate the response to double-stranded DNA breaks. His studies of FHA, Polo-box and BRCT-repeat domains as phosphorylation-dependent interaction scaffolds have made major contributions to our understanding of serine/threonine kinase signalling networks in the DNA-damage response and how genetic aberrations in these molecules lead to tumour development.

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