Document Detail


The cowpox virus fusion regulator proteins SPI-3 and hemagglutinin interact in infected and uninfected cells.
MedLine Citation:
PMID:  16378629     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The serpin SPI-3 and the hemagglutinin (HA) encoded by cowpox virus (CPV) block cell-cell fusion, and colocalize at the cell surface. wtCPV does not fuse cells, but inactivation of either gene leads to fusion. SPI-3 mAb added to wtCPV-infected cells caused fusion, confirming that SPI-3 protein at the cell surface prevents fusion. The SPI-3 mAb epitope mapped to an 85-amino acid region at the C-terminus. Removal of either 44 residues from the SPI-3 C-terminus or 48 residues following the N-terminal signal sequence resulted in fusion. Interaction between SPI-3 and HA proteins in infected cells was shown by coimmunoprecipitation. SPI-3/HA was not associated with the A27L "fusion" protein. SPI-3 and HA were able to associate in uninfected cells in the absence of other viral proteins. The HA-binding domain in SPI-3 resided in the C-terminal 229 residues, and did not include helix D, which mediates cofactor interaction in many other serpins.
Authors:
Peter C Turner; Richard W Moyer
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2005-12-27
Journal Detail:
Title:  Virology     Volume:  347     ISSN:  0042-6822     ISO Abbreviation:  Virology     Publication Date:  2006 Mar 
Date Detail:
Created Date:  2006-03-23     Completed Date:  2006-05-02     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0110674     Medline TA:  Virology     Country:  United States    
Other Details:
Languages:  eng     Pagination:  88-99     Citation Subset:  IM    
Affiliation:
Department of Molecular Genetics and Microbiology, Box 100266/1600 SW Archer Road, ARB R2-231, University of Florida, Gainesville, FL 32610-0266, USA. pturner@mgm.ufl.edu
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Antibodies, Monoclonal
Antibodies, Viral
Cell Line
Cell Membrane / virology
Cercopithecus aethiops
Cowpox virus / genetics,  immunology,  pathogenicity*,  physiology*
Epitope Mapping
Hemagglutinins, Viral / genetics,  immunology,  physiology*
Membrane Fusion / genetics,  physiology
Models, Molecular
Molecular Sequence Data
Mutation
Protein Conformation
Recombinant Proteins / genetics,  immunology,  metabolism
Sequence Homology, Amino Acid
Serpins / chemistry,  genetics,  immunology,  physiology*
Transfection
Viral Proteins / chemistry,  genetics,  immunology,  physiology*
Grant Support
ID/Acronym/Agency:
AI 057157/AI/NIAID NIH HHS; AI-15722/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Antibodies, Monoclonal; 0/Antibodies, Viral; 0/Hemagglutinins, Viral; 0/Recombinant Proteins; 0/Serpins; 0/Viral Proteins

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


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