Fadila Bouamr, Ph.D.

Viral Budding Unit

Fadila Bouamr, Ph.D.

Chief, Viral Budding Unit

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Fadila Bouamr, Ph.D.

Major Areas of Research

  • We examine in detail the recruitment and function of cellular factors that facilitate virus separation from cells.
  • We conduct structure-function studies of proteins involved in these processes.
  • We screen for new host factors involved in virus release.
  • We study the role of ubiquitin in virus egress and membrane scission and other cellular processes important for various steps of virus life cycle.
  • We are also interested in virus assembly and trafficking to sites of virus budding.

Program Description

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.

Electron micrographs showing the different steps of HIV-1 morphogenesis and budding

Electron micrographs showing the different steps of HIV-1 morphogenesis and budding (Kunio Nagashima and Fadila Bouamr)

Credit: NIAID

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.



Ph.D., 1997, Victor Segalen Bordeaux University, Bordeaux, France

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.

Selected Publications

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.

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Research Group

Vincent Dussupt, Ph.D., Research Fellow

Paola Sette, Ph.D., Visiting Fellow

Stig Jensen, Ph.D., Visiting Fellow

Sarah O’Connor, Post-baccalaureate IRTA

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