Mutations of the human immunodeficiency virus type 1 p6(Gag) domain result in reduced retention of pol proteins during virus assembly

Xiao Fang Yu, Liza Dawson, Chun Juan Tian, Charles Flexner, Markus Dettenhofer

Research output: Contribution to journalArticlepeer-review

Abstract

One of the crucial steps in the assembly of the human immunodeficiency virus type I (HIV-1) and other retroviruses is the incorporation and retention of all the key viral enzymes in released virions. The vital enzymes protease, reverse transcriptase, and integrase of HIV-1 are initially synthesized as Gag-Pol fusion polyproteins. It has been shown that the incorporation of Gag-Pol polyproteins during virus assembly requires the Gag domains that are shared by the Gag and Gag-Pol precursors. We now report that truncation of the C-terminal p6 domain of HIV-1 Gag, which is present in the Gag precursor but not in the Gag-Pol precursor, drastically reduced the amount of Pol proteins in the mutant virions. Mutations in the lentivirus conserved motif P(T/S)APP in p6 also drastically reduced the amount of Pol proteins in mutant virions. The steady-state levels of Gag-Pol precursors and cleaved Pol proteins in the transfected cells were not affected by mutations in p6. The incorporation of unprocessed Gag-Pol precursors into p6 mutant virions was detected when the viral protease was mutated, suggesting that the interactions among mutant Gag molecules and Gag-Pol precursors were not significantly affected. These results suggest that the p6 domain of HIV-1 Gag may play an important role in recruiting or retaining cleaved Pol proteins during virus assembly.

Original languageEnglish (US)
Pages (from-to)3412-3417
Number of pages6
JournalJournal of virology
Volume72
Issue number4
DOIs
StatePublished - Apr 1998

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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