A bipartite late-budding domain in human immunodeficiency virus type 1

J Virol. 2003 Nov;77(22):12373-7. doi: 10.1128/jvi.77.22.12373-12377.2003.

Abstract

Human immunodeficiency virus type 1 (HIV-1) encodes a PTAP motif within the p6 domain of Gag that recruits Tsg101 and associated factors to facilitate virion budding. In this study, we use trans-complementation assays to demonstrate that the PTAP motif acts synergistically with additional p6 sequences to mediate the formation of infectious extracellular HIV-1 virions. These studies suggest that Tsg101 recruitment is necessary but not sufficient to account for late-budding activity exhibited by HIV-1 p6.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Motifs
  • Gene Products, gag / chemistry
  • Gene Products, gag / physiology*
  • HIV-1 / physiology*
  • Ubiquitin / metabolism
  • Virion / physiology

Substances

  • Gene Products, gag
  • Ubiquitin