A postdoctoral position is currently available in a research program focused on a variety of key aspects of HIV-1 assembly and release.  Of particular interest are the interplay between viral and host factors in the targeting of assembly to the plasma membrane, the role of lipid rafts in membrane association and virus assembly, and the mechanism by which the viral envelope glycoproteins are incorporated into virions.  Recent studies have been aimed at defining the cellular pathways and host factors involved in the budding of retrovirus particles from the plasma membrane and identifying inhibitors of virus budding and entry.  Studies are also underway to define the target and mechanism of action of a novel HIV-1 maturation inhibitor.

Interested candidates must possess a Ph.D. and/or an M.D. and have a strong background in molecular biology, biochemistry, and/or virology.  The salary range is commensurate with experience.  To apply, click on the button below, or submit a cover letter, curriculum vitae, bibliography, and names of three references to:

1. Waheed, A.A., et al.  Methods for the study of HIV-1 assembly.  In: HIV Protocols, 2nd Ed., Humana Press, in press, 2008.
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3. Viard, M., et al.  Photo-induced reactivity of the HIV-1 envelope glycoprotein with a membrane-embedded probe reveals insertion of portions of the HIV-1 gp41 cytoplasmic tail into the viral membrane.  Biochemistry, in press, 2008.
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5. Luttge, B.G., et al.  Molecular characterization of feline immunodeficiency virus budding.  J. Virol., in press, 2008.
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7. Fujii, K., et al.  Beyond Tsg101: The role of Alix in 'ESCRTing' HIV-1.  Nat. Rev. Microbiol. 5: 912-916, 2007.
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9. Joshi, A., and Freed, E.O.  HIV-1 Gag trafficking.  Future HIV Ther. 1: 427-438, 2007.
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11. Waheed, A.A., and Freed, E.O.  Influenza virus not cRAFTy enough to dodge viperin.  Cell Host Microbe 2: 71-72, 2007.
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13. Garg, H., et al.  Site-specific mutations in HIV-1 gp41 reveal a correlation between HIV-1-mediated bystander apoptosis and fusion/hemifusion.  J. Biol. Chem. 282: 16899-16906, 2007.
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15. Waheed, A.A., et al.  HIV-1 escape from the entry-inhibiting effects of a cholesterol-binding compound via cleavage of gp41 by the viral protease.  Proc. Natl. Acad. Sci. USA 104: 8467-8471, 2007.
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17. Adamson, C.A., and Freed, E.O.  Human immunodeficiency virus type 1 assembly, release, and maturation.  In: HIV-1: Molecular Biogenesis and Pathogenesis: Viral Mechanisms, 2nd Ed., Advances in Pharmacology, Vol. 55, Elsevier Inc. pp. 347-387, 2007.
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19. Lee, S., et al.  Structural basis for viral late-domain binding to Alix.  Nat. Struct. Mol. Biol. 14: 194-199, 2007.
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21. Ono, A., et al.  Depletion of cellular cholesterol inhibits membrane binding and higher-order multimerization of human immunodeficiency virus type 1 Gag.  Virology 360: 27-35, 2007.
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23. Freed, E.O., and Martin, M.A.  HIVs and their replication.  Chapter 57.  In: Fields Virology, 5th Ed., Lippincott, Williams, and Wilkins, pp 2107-2186, 2007.
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25. Munshi, U.M., et al.  An Alix fragment potently inhibits HIV-1 budding: Characterization of binding to retroviral YPXL late domains.  J. Biol. Chem. 282: 3847-3855, 2007.
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27. Saad, J.S., et al.  Point mutations in the HIV-1 matrix protein turn off the myristyl switch.  J. Mol. Biol. 366: 574-585, 2007.
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29. Tang, S., et al.  A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein.  Virology 359: 105-115, 2007.
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31. Freed, E.O., and Mouland, A.O.  Meeting Review: The cell biology of HIV-1 and other retroviruses.  Retrovirology 3: 77-87, 2006.
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33. Li, F., et al.  Determinants of activity of the HIV-1 maturation inhibitor PA-457.  Virology 356: 217-224, 2006.
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35. Adamson, C.S., et al.  In vitro resistance to the human immunodeficiency virus type 1 maturation inhibitor PA-457 (bevirimat).  J. Virol. 80: 10957-10971, 2006.
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37. Liu, F., et al.  Hydrazone- and hydrazide-containing N-substituted glycines as peptoid surrogates for expedited library synthesis: Application to the preparation of Tsg101-directed HIV-1 budding antagonists.  Org. Lett. 8: 5165-5168, 2006.
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39. Waheed, A.A., et al.  Inhibition of HIV-1 replication by amphotericin B methyl ester: Selection for resistant variants.  J. Biol. Chem. 281: 28699-28711, 2006.
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41. Freed, E.O.  HIV-1 Gag: Flipped out for PI(4,5)P2.  Proc. Natl. Acad. Sci. USA 103: 11101-11102, 2006.
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43. Joshi, A., et al.  Mutation of dileucine-like motifs in the human immunodeficiency virus type 1 capsid disrupts virus assembly, Gag-Gag interactions, Gag-membrane binding, and virion maturation.  J. Virol. 80: 7939-7951, 2006.
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45. Davis, M.R., et al.  A mutation in the human immunodeficiency virus type 1 Gag protein destabilizes the interaction of the envelope protein subunits gp120 and gp41.  J. Virol. 80: 2405-2417, 2006.
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47. Fu, W., et al.  Effects of Gag mutation and processing on retroviral dimeric RNA maturation.  J. Virol. 80: 1242-1249, 2006.
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49. Ono, A., et al.  Association of human immunodeficiency virus type 1 Gag with membrane does not require highly basic sequences in the nucleocapsid  Use of a novel Gag multimerization assay.  J. Virol. 79: 14131-14140, 2005.
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51. Ono, A., and Freed, E.O.  Role of lipid rafts in virus replication.  Adv. Virus Res. 64: 311-358, 2005.
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53. Sklar, P.A., et al.  Pravastin does not have a consistent antiviral effect in chronically HIV-infected individuals on antiretroviral therapy.  AIDS 19: 1109-1111, 2005.
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55. Freed, E.O., and Ross, S.R.  Retroviruses 2004:  Review of the 2004 Cold Spring Harbor Retroviruses conference.  Retrovirology 1: 25 (E-pub), 2004.
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57. Demirov, D.G, and Freed, E.O.  Retrovirus budding.  In:  Mechanisms of Enveloped Virus Release (E.O. Freed, ed.), Virus Res. 106: 87-102, 2004.
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59. Ono, A., et al.  Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane.  Proc. Natl. Acad. Sci. USA 101: 14889-14894, 2004.
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61. Freed, E.O.  HIV-1 and the host cell: An intimate association.  Trends Microbiol. 12:170-177, 2004.
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63. Ono, A., and Freed, E.O.  Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and the multivesicular body.  J. Virol. 78:1552-1563, 2004.
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65. Shehu-Xhilaga, M., et al.  Late domain-dependent inhibition of equine infectious anemia virus budding.  J. Virol. 78:724-732, 2004.
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67. Murakami, T., et al.  Regulation of human immunodeficiency virus type 1 Env-mediated membrane fusion by viral protease activity.  J. Virol. 78:1026-1031, 2004.
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69. Li, F., et al.  PA-457: A potent HIV inhibitor that disrupts core condensation by targeting a late step in Gag processing.  Proc. Natl. Acad. Sci. USA 100:13555-13560, 2003.
70. 
    
71. Goila-Gaur, R., et al.  Defects in human immunodeficiency virus budding and endosomal sorting induced by TSG101 overexpression.  J. Virol. 77:6507-6519, 2003.
72. 
    
73. Freed, E.O.  The HIV-TSG101 interface: Recent advances in a budding field.  Trends Microbiol. 11:56-59, 2003.
74. 
    
75. Freed, E.O.  Rafting with Ebola.  Science 296:279, 2002.
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77. Freed, E.O.  Viral late domains.  J. Virol. 76:4679-4687, 2002.
78. 
    
79. Demirov, D.G., et al.  Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function.  Proc. Natl. Acad. Sci. USA 99:955-960, 2002.
80. 
    
81. Demirov, D.G., et al.  The late domain of human immunodeficiency virus type 1 p6 promotes virus release in a cell type-dependent manner.  J. Virol. 76:105-117, 2002.
82. 
    
83. Ono, A., and Freed, E.O.  Plasma membrane rafts play a critical role in HIV-1 assembly and release.  Proc. Natl. Acad. Sci. USA 98:13925-13930, 2001.
84. 
    
85. Freed, E.O., and Martin, M.A.  HIVs and their replication.  In:  Fields Virology, Chap. 59, 4th Ed., Lippincott, Williams, and Wilkins, pp. 1971-2041, 2001.
86. 
    
87. Ono, A., et al.  Relationship between human immunodeficiency virus type 1 Gag multimerization and membrane binding.  J. Virol. 74:5142-5150, 2000.
88. 
    
89. Murakami, T., and Freed, E.O.  Genetic evidence for an interaction between human immunodeficiency virus type 1 matrix and alpha-helix 2 of the gp41 cytoplasmic tail.  J. Virol. 74:3548-3554, 2000.
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91. Murakami, T., and Freed, E.O.  The long cytoplasmic tail of gp41 is required in a cell type-dependent manner for HIV-1 envelope glycoprotein incorporation into virions.  Proc. Natl. Acad. Sci. USA 97:343-348, 2000.

To apply:

The National Cancer Institute coordinates the National Cancer Program, which conducts and supports research, training, health information dissemination, and other programs with respect to the cause, diagnosis, prevention, and treatment of cancer, rehabilitation from cancer, and the continuing care of cancer patients and the families of cancer patients. Specifically, the Institute:

• Supports and coordinates research projects conducted by universities, hospitals, research foundations, and businesses throughout this country and abroad through research grants and cooperative agreements.
• Conducts research in its own laboratories and clinics.
• Supports education and training in fundamental sciences and clinical disciplines for participation in basic and clinical research programs and treatment programs relating to cancer through career awards, training grants, and fellowships.
• Supports research projects in cancer control.
• Supports a national network of cancer centers.
• Collaborates with voluntary organizations and other national and foreign institutions engaged in cancer research and training activities.
• Encourages and coordinates cancer research by industrial concerns where such concerns evidence a particular capability for programmatic research.
• Collects and disseminates information on cancer.
• Supports construction of laboratories, clinics, and related facilities necessary for cancer research through the award of construction grants.