1st National Conference Human Retroviruses and Related Infections Washington, DC - December 12-16, 1993

Natl Conf Hum Retrovir Relat Infect 1993 Dec 12-16;1: (abstract no. 17)

Aldovini A, Jackson W, Young R
Whitehead Institute of Biomedical Research, Cambridge, MA

The N-terminus of myristylated Gag precursors associate with the inner membrane of infected cells to initiate the process of budding. After budding, in a process called condensation, the precursors are cleaved into mature matrix, core, and nucleocapsid proteins concomitant with a rearrangement of the architecture of the inner virion. A better understanding of the intramolecular interactions between the Gag precursor proteins has been the goal of our recent studies in HIV assembly. The yeast two-hybrid system has been used to obtain clues to the interactions between Gag proteins. Two full-length Gag precursor proteins interact well in this system, but neither the processed products of Gag or truncations of the Gag precursor produce positive results. We have used the system to generate and analyze point mutations which affect interactions among the Gag precursor proteins. The results indicate that point mutations which affect sequences destined to become parts of MA p17, CA p24 or NC p7 all adversely affect Gag precursor interactions. These data suggest that multiple protein-protein interactions are involved between Gag precursors during virus assembly and provide a model to explain the molecular force behind budding.

Keywords: AIDS Vaccines, Acquired Immunodeficiency Syndrome, Base Sequence, Cloning, Molecular, Gene Products, gag, Genes, gag, HIV, HIV Antigens, HIV Seropositivity, HIV-1, Protein Binding, Protein Folding, Virion, Virus Assembly, genetics, immunology, virology

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1993-12-12
17

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