investigator=s abstract): The goal of this proposal is to elucidate the role of Gag proteins in virion assembly, virus-induced cytopathicity, virus host -range and early steps of virus transmission. Preliminary studies indicate the Gag polyprotein, and in particular its matrix domain, has a central role in controlling HIV-1 induced cytopathicity. Furthermore, data show that matrix, and its interaction partner, the cytoplasmic domain of the viral envelope glycoprotein, can have major effects on the target cell tropism of HIV-1. To elucidate the basis for this novel role of Gag, which may have important implications for HIV-1 pathogenicity, the investigator proposes to investigate whether there is a connection between the role of Gag in viral cytopathicity and viral host range. In addition, the investigator has developed a method for efficient purification of intact HIV-1 virion cores and proposes to examine their protein composition and structure.

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
2R01AI029873-10
Application #
2873744
Study Section
Special Emphasis Panel (ZRG1-AARR-1 (01))
Program Officer
Plaeger, Susan F
Project Start
1990-03-01
Project End
2004-05-31
Budget Start
1999-06-01
Budget End
2000-05-31
Support Year
10
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Dana-Farber Cancer Institute
Department
Type
DUNS #
149617367
City
Boston
State
MA
Country
United States
Zip Code
02215
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Ma, Yu May; Boucrot, Emmanuel; Villen, Judit et al. (2007) Targeting of AMSH to endosomes is required for epidermal growth factor receptor degradation. J Biol Chem 282:9805-12
Calistri, Arianna; Sette, Paola; Salata, Cristiano et al. (2007) Intracellular trafficking and maturation of herpes simplex virus type 1 gB and virus egress require functional biogenesis of multivesicular bodies. J Virol 81:11468-78

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