This is a continuation application, centering on the role of HIV capsid protein (CA) in virion structure and post-assembly events, and how the host protein cyclophilin A (CyP A) facilitates this role.
The specific aims of the projects are:
AIM 1 : to identify the basis of Gag (precursor) and CA recognition by cellular chaperons such as CyP A and to determine the role of CyP A in maturation of the Gag precursor.
AIM 2 : to identify the CyP A-dependent CA proteins in viral particles and to determine their function, through reconstitution experiments.
AIM 3 : to define, using X-ray structure and genetic analysis, the structural changes that result from CyP A-induced alterations of the mature CA protein.
AIM 4 : to distinguish regions in the Gag and CA proteins involved in different CyP A interactions, using mutants defective in folding and assays distinguishing the chaperon versus isomerization activities of CyP A.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM048294-06
Application #
2857161
Study Section
AIDS and Related Research Study Section 3 (ARRC)
Project Start
1993-09-29
Project End
2000-12-31
Budget Start
1999-01-01
Budget End
1999-12-31
Support Year
6
Fiscal Year
1999
Total Cost
Indirect Cost
Name
State University New York Stony Brook
Department
Genetics
Type
Schools of Medicine
DUNS #
804878247
City
Stony Brook
State
NY
Country
United States
Zip Code
11794
Watanabe, Susan M; Medina, Gisselle N; Eastep, Gunnar N et al. (2018) The matrix domain of the Gag protein from avian sarcoma virus contains a PI(4,5)P2-binding site that targets Gag to the cell periphery. J Biol Chem 293:18841-18853
Medina, Gisselle; Zhang, Yongjun; Tang, Yi et al. (2005) The functionally exchangeable L domains in RSV and HIV-1 Gag direct particle release through pathways linked by Tsg101. Traffic 6:880-94