Structural characterization of HIV-host interaction
HIV (Human Defficiency Virus) is the causative agent of AIDS, a disease that causes an estimated 1.3 M deaths annually. There is currently no cure or vaccine, although antiretroviral therapy has largely reduced mortality in western countries. Nonetheless more therapeutics are required to overcome drug resistance and prevent transmission.
Although HIV is a small virus, that encodes for only 9 genes, it forms a broad range of interactions with its host. I am interested in the structural and biochemical characterization of human proteins that interact with HIV, either as co-factors that promote HIV infection (Elongin B, Elongin C, Cullin 5, CRM1) or as restriction factors that prevent HIV replication (APOBEC3G, MX2).
Dicks MD, Goujon C, Pollpeter D, Betancor G, Apolonia L, Bergeron JR, Malim MH. Oligomerization requirements for MX2 mediated suppression of HIV-1 infection. Journal of Virology 2015.
Lu Z, Bergeron JR, Atkinson RA, Schaller T, Veselkov DA, Oregioni A, Yang Y, Matthews SJ, Malim MH, Sanderson MR. Insight into the HIV-1 Vif SOCS-box-ElonginBC interaction. Open Biology 2013.
Sherer NM, Swanson CM, Hué S, Roberts RG, Bergeron JR, Malim MH. Evolution of a species-specific determinant within human CRM1 that regulates the post-transcriptional phases of HIV-1 replication. PLoS Pathogens 2011.
Autore F, Bergeron JR, Malim MH, Fraternali F, Huthoff H. Rationalisation of the differences between APOBEC3G structures from crystallography and NMR studies by molecular dynamics simulations. PLoS One 2010.
Bergeron JR, Huthoff H, Veselkov DA, Beavil RL, Simpson PJ, Matthews SJ, Malim MH, Sanderson MR. The SOCS-box of HIV-1 Vif interacts with ElonginBC by induced-folding to recruit its Cul5-containing ubiquitin ligase complex. PLoS Pathogens 2010.