Gabuzda D, Lever A, Haseltine W, Sodroski J; International Conference on AIDS.

Int Conf AIDS. 1991 Jun 16-21; 7: 24 (abstract no. M.A.12).

Dana-Farber Cancer Institute and Harvard Medical School, Boston, MA, USA

OBJECTIVE: The HIV-1 envelope glycoprotein carboxyl terminus contains sequences which are essential for efficient viral replication. To determine the function of this domain in the virus life cycle, the effect of mutations in the carboxy terminal 160 amino acids of gp41 on viral replication, envelope glycoprotein synthesis and processing, syncytium for mutation, and incorporation of envelope glycoproteins into virions was investigated. METHODS: An HIV-1 envelope expressor plasmid was used to identify and characterize replication-defective carboxyl terminus mutants in transfected Cos-I and Jurkat cells. The replicative potential of the mutant envelope glycoproteins was tested using viruses produced in Cos-1 cells in a transient trans-complementation assay. (Helseth et al, J. Virol. 64:2416-2420, 1990). Radioimunoprecipitation was used to study the synthesis, processing, and virion incorporation of the mutant envelope glycoproteins in transfected cos-1 cells. Syncytium forming ability was studied in Cos-1 cells and Jurkat-Tat cells. RESULTS: Deletions involving the 42 amino acids at the 3' c-terminus reduced cell-free virus transmission to less than 25% of the wild-type level. The c-terminal 160 amino acids were not required for syncytium formation or for incorporation of the envelope glycoproteins into virions. CONCLUSIONS: The HIV-1 envelope glycoprotein C-terminus is not essential for syncytium formation or efficient incorporation of envelope into virions. This region may be involved in an early stage in the virus life cycle following CD4 binding and membrane fusion.

Publication Types:

• Meeting Abstracts

Keywords:

• Acquired Immunodeficiency Syndrome
• Antigens, CD4
• Base Sequence
• Gene Products, tat
• Genes, tat
• Giant Cells
• Greece
• HIV
• HIV Antigens
• HIV-1
• Humans
• Membrane Fusion
• Mutation
• Viral Envelope Proteins
• Virion
• genetics
• glycoprotein gC, herpes simplex virus type 1
• immunology
• physiology

Other ID:

• 1001291

UI: 102181742

From Meeting Abstracts