Document Detail

Identification of a 40- to 42-kDa attachment polypeptide for canine parvovirus in A72 cells.
MedLine Citation:
PMID:  7975239     Owner:  NLM     Status:  MEDLINE    
The attachment of canine parvovirus (CPV) to different cell lines was quantitated by a fluorescence-activated cell sorter assay. The viral attachment was observed to both permissive A72 and nonpermissive ST cells but not to nonpermissive MDBK cells. The binding of and infectivity for CPV to A72 cells was reduced upon prior treatment of cells with Vibrio cholerae neuraminidase or lectins, specific for sialic acid. Similarly, treatment of cells with any of several proteases reduced virus binding; however, phospholipase treatment had no effect indicating that one or more membrane glycoproteins were involved in virus binding. These proteins were characterized with a virus overlay protein blot assay. Virus bound to a protein with a molecular mass of 40 to 42 kDa in membranes prepared from A72 and ST cells and not from MDBK cells. The binding to this polypeptide was specific since increasing amounts of unlabeled virions competitively inhibited binding of radiolabeled virions in a dose-dependent manner. A polypeptide of similar molecular mass was immunoprecipitated from radiolabeled octyl glucoside (OG) extract of A72 cells using purified virions, virion-specific antiserum, and protein A. The binding to this polypeptide was decreased but not abolished upon prior treatment of the membrane with V. cholerae neuraminidase. CPV preferentially recognized a polypeptide of similar molecular size in the OG extract prepared from the biotinylated basolateral surface of polarized MDCK monolayer. Hence, we propose that the 40- to 42-kDa glycoprotein represents a specific attachment molecule for CPV in A72 cells.
S Basak; H Turner; S Parr
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Virology     Volume:  205     ISSN:  0042-6822     ISO Abbreviation:  Virology     Publication Date:  1994 Nov 
Date Detail:
Created Date:  1994-12-06     Completed Date:  1994-12-06     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0110674     Medline TA:  Virology     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  7-16     Citation Subset:  IM    
Department of Microbiology, University of Alabama at Birmingham 35294.
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MeSH Terms
Cell Line
Cell Polarity
Lectins / metabolism,  pharmacology
N-Acetylneuraminic Acid
Neuraminidase / metabolism,  pharmacology
Parvovirus, Canine / metabolism*,  pathogenicity
Peptides / metabolism*
Sialic Acids / metabolism
Tumor Cells, Cultured
Vibrio cholerae / enzymology
Grant Support
Reg. No./Substance:
0/Lectins; 0/Peptides; 0/Sialic Acids; 131-48-6/N-Acetylneuraminic Acid; EC

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