Abstract

The long range goal of our proposed research is to understand the details of the HIV assembly process at a molecular level to provide the groundwork for rationale drug design. Towards achieving this goal, the research proposed in this program focuses on several key but no-so-well understood aspects of the HIV assembly process. The formation of HIV particles is complex and involves the interaction of several different virus-specified components. Because of this it seems likely that as we learn more about assembly, many novel targets for anti HIV drugs will emerge. Although the overall outline of HIV assembly is understood, many of the details are lacking. Specifically we are interested in; 1) defining in detail how the HIV core protein precursors interact to form virus particles. 2) Studying the effect of the viral envelope proteins and vpu on virus release and assembly and examining the mechanisms which underlie the targeting of the viral envelope proteins and core precursors to apposing sites of the plasma membrane 3) Determining in more detail than is presently known how viral RNA is packaged and. 4) Comparing the assembly process for HIV-1 to HIV-2. to determine if """"""""phenotypic mixing"""""""" between these two viruses can occur.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project--Cooperative Agreements (U01)
Project #
7U01AI025721-06
Application #
3791091
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
6
Fiscal Year
1992
Total Cost
Indirect Cost

  Institution

Name
University of Virginia
Department
Type
DUNS #
001910777
City
Charlottesville
State
VA
Country
United States
Zip Code
22904

  Publications

Dundr, M; Meier, U T; Lewis, N et al. (1997) A class of nonribosomal nucleolar components is located in chromosome periphery and in nucleolus-derived foci during anaphase and telophase. Chromosoma 105:407-17
Dundr, M; Leno, G H; Lewis, N et al. (1996) Location of the HIV-1 Rev protein during mitosis: inactivation of the nuclear export signal alters the pathway for postmitotic reentry into nucleoli. J Cell Sci 109 ( Pt 9):2239-51
Srinivasakumar, N; Hammarskjold, M L; Rekosh, D (1995) Characterization of deletion mutations in the capsid region of human immunodeficiency virus type 1 that affect particle formation and Gag-Pol precursor incorporation. J Virol 69:6106-14
Dundr, M; Leno, G H; Hammarskjold, M L et al. (1995) The roles of nucleolar structure and function in the subcellular location of the HIV-1 Rev protein. J Cell Sci 108 ( Pt 8):2811-23
Berkowitz, R D; Hammarskjold, M L; Helga-Maria, C et al. (1995) 5' regions of HIV-1 RNAs are not sufficient for encapsidation: implications for the HIV-1 packaging signal. Virology 212:718-23
Mak, J; Jiang, M; Wainberg, M A et al. (1994) Role of Pr160gag-pol in mediating the selective incorporation of tRNA(Lys) into human immunodeficiency virus type 1 particles. J Virol 68:2065-72
Hammarskjold, M L; Li, H; Rekosh, D et al. (1994) Human immunodeficiency virus env expression becomes Rev-independent if the env region is not defined as an intron. J Virol 68:951-8
Bray, M; Prasad, S; Dubay, J W et al. (1994) A small element from the Mason-Pfizer monkey virus genome makes human immunodeficiency virus type 1 expression and replication Rev-independent. Proc Natl Acad Sci U S A 91:1256-60
Smith, A J; Srinivasakumar, N; Hammarskjold, M L et al. (1993) Requirements for incorporation of Pr160gag-pol from human immunodeficiency virus type 1 into virus-like particles. J Virol 67:2266-75
Keefer, M C; Bonnez, W; Roberts Jr, N J et al. (1991) Human immunodeficiency virus (HIV-1) gp160-specific lymphocyte proliferative responses of mononuclear leukocytes from HIV-1 recombinant gp160 vaccine recipients. J Infect Dis 163:448-53

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