Document Detail

Insertion of the two cleavage sites of the respiratory syncytial virus fusion protein in Sendai virus fusion protein leads to enhanced cell-cell fusion and a decreased dependency on the HN attachment protein for activity.
MedLine Citation:
PMID:  18385247     Owner:  NLM     Status:  MEDLINE    
Cell entry by paramyxoviruses requires fusion of the viral envelope with the target cell membrane. Fusion is mediated by the viral fusion (F) glycoprotein and usually requires the aid of the attachment glycoprotein (G, H or HN, depending on the virus). Human respiratory syncytial virus F protein (F(RSV)) is able to mediate membrane fusion in the absence of the attachment G protein and is unique in possessing two multibasic furin cleavage sites, separated by a region of 27 amino acids (pep27). Cleavage at both sites is required for cell-cell fusion. We have investigated the significance of the two cleavage sites and pep27 in the context of Sendai virus F protein (F(SeV)), which possesses a single monobasic cleavage site and requires both coexpression of the HN attachment protein and trypsin in order to fuse cells. Inclusion of both F(RSV) cleavage sites in F(SeV) resulted in a dramatic increase in cell-cell fusion activity in the presence of HN. Furthermore, chimeric F(SeV) mutants containing both F(RSV) cleavage sites demonstrated cell-cell fusion in the absence of HN. The presence of two multibasic cleavage sites may therefore represent a strategy to regulate activation of a paramyxovirus F protein for cell-cell fusion in the absence of an attachment protein.
Joanna Rawling; Blanca García-Barreno; José A Melero
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-04-02
Journal Detail:
Title:  Journal of virology     Volume:  82     ISSN:  1098-5514     ISO Abbreviation:  J. Virol.     Publication Date:  2008 Jun 
Date Detail:
Created Date:  2008-05-23     Completed Date:  2008-08-12     Revised Date:  2013-06-05    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5986-98     Citation Subset:  IM    
Centro Nacional de Microbiología, Instituto de Salud Carlos III, Majadahonda, 28220 Madrid, Spain.
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MeSH Terms
Amino Acid Sequence
Cell Fusion*
Cell Line
DNA, Complementary
Furin / chemistry,  genetics
Genes, Reporter
HN Protein / physiology*
Luciferases / metabolism
Molecular Sequence Data
Mutagenesis, Insertional
Respiratory Syncytial Viruses / physiology*
Sequence Homology, Amino Acid
Trypsin / metabolism
Viral Fusion Proteins / chemistry,  genetics*,  physiology*
Reg. No./Substance:
0/DNA, Complementary; 0/HN Protein; 0/Viral Fusion Proteins; EC 1.13.12.-/Luciferases; EC; EC

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