| Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection. | |
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MedLine Citation:
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PMID: 18353944 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The membrane-spanning domain (MSD) of the human immunodeficiency virus type 1 (HIV-1) gp41 glycoprotein is critical for its biological activity. Previous C-terminal truncation studies have predicted an almost invariant core structure of 12 amino acid residues flanked by basic amino acids in the HIV-1 MSD that function to anchor the glycoprotein in the lipid bilayer. To further understand the role of specific amino acids within the MSD core, we initially replaced the core region with 12 leucine residues and then constructed recovery-of-function mutants in which specific amino acid residues (including a GGXXG motif) were reintroduced. We show here that conservation of the MSD core sequence is not required for normal expression, processing, intracellular transport, and incorporation into virions of the envelope glycoprotein (Env). However, the amino acid composition of the MSD core does influence the ability of Env to mediate cell-cell fusion and plays a critical role in the infectivity of HIV-1. Replacement of conserved amino acid residues with leucine blocked virus-to-cell fusion and subsequent viral entry into target cells. This restriction could not be released by C-terminal truncation of the gp41 glycoprotein. These studies imply that the highly conserved core residues of the HIV Env MSD, in addition to serving as a membrane anchor, play an important role in mediating membrane fusion during viral entry. |
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Authors:
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Liang Shang; Ling Yue; Eric Hunter |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2008-03-19 |
Journal Detail:
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Title: Journal of virology Volume: 82 ISSN: 1098-5514 ISO Abbreviation: J. Virol. Publication Date: 2008 Jun |
Date Detail:
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Created Date: 2008-05-15 Completed Date: 2008-06-11 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 0113724 Medline TA: J Virol Country: United States |
Other Details:
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Languages: eng Pagination: 5417-28 Citation Subset: IM |
Affiliation:
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Emory Vaccine Center, Department of Pathology and Laboratory Medicine, and Yerkes National Primate Research Center, Emory University, Atlanta, Georgia 30329, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Cell Line Cell Membrane / metabolism* Cercopithecus aethiops Consensus Sequence Gene Expression Regulation HIV-1 / chemistry, genetics, metabolism* Humans Membrane Proteins / metabolism Molecular Sequence Data Mutation / genetics Sequence Alignment Viral Envelope Proteins / chemistry, genetics, metabolism* Virus Internalization* |
| Grant Support | |
ID/Acronym/Agency:
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P30 AI050409/AI/NIAID NIH HHS; R01 AI33319/AI/NIAID NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Membrane Proteins; 0/Viral Envelope Proteins |
| Comments/Corrections | |
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