Document Detail


Effect of extension of the cytoplasmic domain of human immunodeficiency type 1 virus transmembrane protein gp41 on virus replication.
MedLine Citation:
PMID:  15113898     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The biological significance of the presence of a long cytoplasmic domain in the envelope (Env) transmembrane protein gp41 of human immunodeficiency virus type 1 (HIV-1) is still not fully understood. Here we examined the effects of cytoplasmic tail elongation on virus replication and characterized the role of the C-terminal cytoplasmic tail in interactions with the Gag protein. Extensions with six and nine His residues but not with fewer than six His residues were found to severely inhibit virus replication through decreased Env electrophoretic mobility and reduced Env incorporation compared to the wild-type virus. These two mutants also exhibited distinct N glycosylation and reduced cell surface expression. An extension of six other residues had no deleterious effect on infectivity, even though some mutants showed reduced Env incorporation into the virus and/or decreased cell surface expression. We further show that these elongated cytoplasmic tails in a format of the glutathione S-transferase fusion protein still interacted effectively with the Gag protein. In addition, the immediate C terminus of the cytoplasmic tail was not directly involved in interactions with Gag, but the region containing the last 13 to 43 residues from the C terminus was critical for Env-Gag interactions. Taken together, our results demonstrate that HIV-1 Env can tolerate extension at its C terminus to a certain degree without loss of virus infectivity and Env-Gag interactions. However, extended elongation in the cytoplasmic tail may impair virus infectivity, Env cell surface expression, and Env incorporation into the virus.
Authors:
Woan-Eng Chan; Ya-Lin Wang; Hui-Hua Lin; Steve S-L Chen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of virology     Volume:  78     ISSN:  0022-538X     ISO Abbreviation:  J. Virol.     Publication Date:  2004 May 
Date Detail:
Created Date:  2004-04-28     Completed Date:  2004-05-27     Revised Date:  2013-04-18    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5157-69     Citation Subset:  IM    
Affiliation:
Institute of Biomedical Sciences, Academia Sinica, 128 Section 2 Yen-Chiu-Yuan Road, Nankang, Taipei 11529, Taiwan, Republic of China.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Cytoplasm / chemistry
Glycosylation
HIV Envelope Protein gp41 / chemistry*,  physiology
HIV-1 / physiology*
HeLa Cells
Humans
Molecular Sequence Data
Recombinant Fusion Proteins / chemistry
Structure-Activity Relationship
Virus Replication*
Chemical
Reg. No./Substance:
0/HIV Envelope Protein gp41; 0/Recombinant Fusion Proteins
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