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A plasma membrane localization signal in the HIV-1 envelope cytoplasmic domain prevents localization at sites of vesicular stomatitis virus budding and incorporation into VSV virions.
Johnson JE; Rodgers W; Rose JK; Departments of Genetics, Opthalmology
March 30, 1999
Virology. 1998 Nov 25;251(2):244-52. Unique Identifier : AIDSLINE

Previous studies showed that the HIV-1 envelope (Env) protein was not incorporated into vesicular stomatitis virus (VSV) virions unless its cytoplasmic tail was replaced with that of the VSV glycoprotein (G). To determine whether the G tail provided a positive incorporation signal for Env, or if sequences in the Env tail prevented incorporation, we generated mutants of Env with its 150-amino-acid tail shortened to 29, 10, or 3 amino acids (Envtr mutants). Cells infected with VSV recombinants expressing these proteins or an Env-G tail hybrid showed similar amounts of Env protein at the surface. The Env-G tail hybrid or the Envtr3 mutant were incorporated at the highest levels into budding VSV virions. In contrast, the Envtr29 or Envtr10 mutants were incorporated poorly. These results defined a signal preventing incorporation within the 10 membrane-proximal amino acids of the Env tail. Confocal microscopy revealed that this signal functioned by causing localization of human immunodeficiency virus type 1 Env to plasma membrane domains distinct from the VSV budding sites, where VSV proteins were concentrated. Copyright 1998 Academic Press.

JOURNAL ARTICLE Amino Acid Sequence Animal Cell Membrane/METABOLISM Cells, Cultured Cytoplasm/METABOLISM Gene Products, env/GENETICS/*METABOLISM Hamsters Human HIV Envelope Protein gp120/METABOLISM HIV-1/*METABOLISM Microscopy, Confocal Molecular Sequence Data Recombinant Proteins/CHEMISTRY Signal Peptides/*METABOLISM Structure-Activity Relationship Support, U.S. Gov't, P.H.S. Vesicular Stomatitis-Indiana Virus/*METABOLISM Viral Envelope Proteins/GENETICS/*METABOLISM Virion/*METABOLISM