Fadila Bouamr, Ph.D.Building 4, Room 3374 Memorial DriveBethesda, MD 20892-1576Phone: 301-496-4099Fax: email@example.com
Chief, Viral Budding Unit, LMM
We study the molecular mechanisms that govern the assembly and egress of an infectious HIV-1 and the proteins involved in these processes. HIV-1 and other retroviruses assemble and release viral particles from the plasma membrane of infected cells. We study the regions responsible for viral particle assembly and budding with an emphasis on domains that act in late steps of viral particle morphogenesis to facilitate virus abscission from the cell.
HIV-1 and other enveloped viruses such as hepatitis B and C, Ebola, and herpes simplex 1 acquire their membranes during cell exit. Such process involves factors belonging to the endosomal sorting complex required for transport (ESCRT), a host cell pathway involved in a variety of cellular processes including surface receptor downregulation, endocytosis, cytokinesis, and autophagy. Because of their involvement in these various cellular processes, ESCRT function or dysfunction has been associated with human diseases including those caused by viruses, cancer, and neurodegeneration.
Studies aim at piecing together the different aspects of membrane rearrangements involved in virus scission and completion of cytokinesis. We hope to gain a better understanding of the mechanisms that control the functional interplay between viral and host factors.
back to top
Dr. Fadila Bouamr received her Ph.D. from Victor Segalen Bordeaux University in 1997. She performed her postdoctoral research with Dr. Carol Carter at the State University of New York at Stony Brook and with Dr. Steve Goff at Columbia University. She joined the Laboratory of Molecular Microbiology in December 2004.
Vincent Dussupt, Ph.D., Research FellowPaola Sette, Ph.D., Visiting FellowStig Jensen, Ph.D., Visiting FellowSarah O’Connor, Post-baccalaureate IRTA
Mu R, Dussupt V, Jiang J, Sette P, Rudd V, Bello FT, Bouamr. F*, Xiao ST*. Two distinct binding modes define the interaction of Brox with the C-terminal tails of CHMP5 and CHMP4B. Structure. 2012 May 9;20(5):887-98. *co-senior authors
Bello NF, Dussupt V, Sette P, Rudd V, Nagashima K, Bibollet-Ruche F, Chen C, Montelaro RC, Hahn BH, Bouamr F. Budding of retroviruses utilizing divergent L domains requires nucleocapsid. J Virol. 2012 Apr;86(8):4182-93
Sette P, Mu R, Dussupt V, Jiang J, Snyder G, Smith P, Xiao TS, Bouamr F. The Phe105 loop of Alix Bro1 domain plays a key role in HIV-1 release. Structure. 2011 Oct 12;19(10):1485-95.
Bello NF, Wu F, Sette P, Dussupt V, Hirsch VM, Bouamr F. Distal leucines are key functional determinants of Alix-binding simian immunodeficiency virus SIV(smE543) and SIV(mac239) type 3 L domains. J Virol. 2011 Nov;85(21):11532-7.
Dussupt V, Sette P, Bello NF, Javid MP, Nagashima K, Bouamr F. Basic residues in the nucleocapsid domain of Gag are critical for late events of HIV-1 budding. J Virol. 2011 Mar;85(5):2304-15.
Dussupt V, Javid MP, Abou-Jaoudé G, Jadwin JA, de La Cruz J, Nagashima K, Bouamr F. The nucleocapsid region of HIV-1 Gag cooperates with the PTAP and LYPXnL late domains to recruit the cellular machinery necessary for viral budding. PLoS Pathog. 2009 Mar;5(3):e1000339.
Visit PubMed for a complete publication listing.
Last Updated March 14, 2014