Document Detail

Residues in a highly conserved claudin-1 motif are required for hepatitis C virus entry and mediate the formation of cell-cell contacts.
MedLine Citation:
PMID:  19297469     Owner:  NLM     Status:  MEDLINE    
Claudin-1, a component of tight junctions between liver hepatocytes, is a hepatitis C virus (HCV) late-stage entry cofactor. To investigate the structural and functional roles of various claudin-1 domains in HCV entry, we applied a mutagenesis strategy. Putative functional intracellular claudin-1 domains were not important. However, we identified seven novel residues in the first extracellular loop that are critical for entry of HCV isolates drawn from six different subtypes. Most of the critical residues belong to the highly conserved claudin motif W(30)-GLW(51)-C(54)-C(64). Alanine substitutions of these residues did not impair claudin-1 cell surface expression or lateral protein interactions within the plasma membrane, including claudin-1-claudin-1 and claudin-1-CD81 interactions. However, these mutants no longer localized to cell-cell contacts. Based on our observations, we propose that cell-cell contacts formed by claudin-1 may generate specialized membrane domains that are amenable to HCV entry.
Lisa Cukierman; Laurent Meertens; Claire Bertaux; Francis Kajumo; Tatjana Dragic
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2009-03-18
Journal Detail:
Title:  Journal of virology     Volume:  83     ISSN:  1098-5514     ISO Abbreviation:  J. Virol.     Publication Date:  2009 Jun 
Date Detail:
Created Date:  2009-05-13     Completed Date:  2009-05-29     Revised Date:  2013-06-02    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5477-84     Citation Subset:  IM    
Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
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MeSH Terms
Amino Acid Motifs
Cell Communication*
Cell Line
Cell Membrane / metabolism
Extracellular Space / metabolism
Hepacivirus / physiology*
Membrane Proteins / chemistry,  genetics,  metabolism*
Molecular Sequence Data
Mutation / genetics
Virus Internalization*
Grant Support
Reg. No./Substance:
0/CLDN1 protein, human; 0/Claudin-1; 0/Membrane Proteins

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