Document Detail


Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions.
MedLine Citation:
PMID:  8523546     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We recently demonstrated that a single amino acid substitution in matrix residue 12 (12LE) or 30 (30LE) blocks the incorporation of human immunodeficiency virus type 1 (HIV-1) envelope glycoproteins into virions and that this block can be reversed by pseudotyping with heterologous retroviral envelope glycoproteins with short cytoplasmic tails or by truncating the cytoplasmic tail of HIV-1 transmembrane glycoprotein gp41 by 104 or 144 amino acids. In this study, we mapped the domain of the gp41 cytoplasmic tail responsible for the block to incorporation into virions by introducing a series of eight truncation mutations that eliminated 23 to 93 amino acids from the C terminus of gp41. We found that incorporation into virions of a HIV-1 envelope glycoprotein with a deletion of 23, 30, 51, or 56 residues from the C terminus of gp41 is specifically blocked by the 12LE matrix mutation, whereas truncations of greater than 93 amino acids reverse this defect. To elucidate the role of matrix residue 12 in this process, we introduced a number of additional single amino acid substitutions at matrix positions 12 and 13. Charged substitutions at residue 12 blocked envelope incorporation and virus infectivity, whereas more subtle amino acid substitutions resulted in a spectrum of envelope incorporation defects. To characterize further the role of matrix in envelope incorporation into virions, we obtained and analyzed second-site revertants to two different matrix residue 12 mutations. A Val-->Ile substition at matrix amino acid 34 compensated for the effects of both amino acid 12 mutations, suggesting that matrix residues 12 and 34 interact during the incorporation of HIV-1 envelope glycoproteins into nascent virions.
Authors:
E O Freed; M A Martin
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of virology     Volume:  70     ISSN:  0022-538X     ISO Abbreviation:  J. Virol.     Publication Date:  1996 Jan 
Date Detail:
Created Date:  1996-01-25     Completed Date:  1996-01-25     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  341-51     Citation Subset:  IM; X    
Affiliation:
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892-0460, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Base Sequence
Binding Sites
Cell Line
DNA, Viral
Gene Products, env / metabolism
Gene Products, gag / chemistry,  metabolism*
HIV Antigens / chemistry,  metabolism*
HIV Envelope Protein gp160
HIV Envelope Protein gp41 / chemistry,  metabolism*
HIV-1 / metabolism*
Hela Cells
Humans
Molecular Sequence Data
Mutagenesis
Mutation
Protein Precursors / metabolism
Viral Envelope Proteins / metabolism*
Viral Proteins*
Virion / metabolism
gag Gene Products, Human Immunodeficiency Virus
Chemical
Reg. No./Substance:
0/DNA, Viral; 0/Gene Products, env; 0/Gene Products, gag; 0/HIV Antigens; 0/HIV Envelope Protein gp160; 0/HIV Envelope Protein gp41; 0/Protein Precursors; 0/Viral Envelope Proteins; 0/Viral Proteins; 0/gag Gene Products, Human Immunodeficiency Virus; 0/p17 protein, Human Immunodeficiency Virus Type 1
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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