Document Detail


Lectin-like binding of pertussis toxin to a 165-kilodalton Chinese hamster ovary cell glycoprotein.
MedLine Citation:
PMID:  3350815     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Chinese hamster ovary (CHO) cells cluster in the presence of pertussis toxin, a response that is correlated with the ADP-ribosylation of a Mr = 41,000 membrane protein by the toxin. A ricin-resistant line of CHO cells (CHO-15B) which specifically lacks the terminal NeuAc----Gal beta 4GlcNAc oligosaccharide sequence on glycoproteins did not cluster in response to pertussis toxin. These cells do contain the Mr = 41,000 protein substrate for the enzymatic activity of the toxin which suggests that pertussis toxin, like certain plant lectins, does not bind to or is not internalized by the CHO-15B cells. There was no evidence of pertussis toxin binding to gangliosides or neutral glycolipids isolated from CHO cells but the toxin bound to a Mr = 165,000 component in N-octyglucoside extracts of CHO cells that had been separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and electroblotted to nitrocellulose. Plant lectins from Ricinus communis and Erythina cristagalli detected a similar size band in CHO cells and also did not react with CHO-15B cells. Unlike pertussis toxin, these plant lectins recognized two other major bands in CHO cell extracts and reacted best after sialidase treatment of nitrocellulose transfers containing CHO cell extracts. Conversely, sialidase treatment abolished binding a pertussis toxin and wheat germ agglutinin, a plant lectin that reacts with multivalent sialic acid residues on glycoproteins, to the Mr = 165,000 band. Purified B oligomer of pertussis toxin also uniquely detected a Mr = 165,000 component in CHO cell extracts while the A subunit of pertussis toxin was unreactive. These results indicate that pertussis toxin binds to a CHO cell glycoprotein with N-linked oligosaccharides and that sialic acid contributes to the complementary receptor site for the toxin. In addition, they suggest that a glycoprotein may serve as a cell surface receptor for pertussis toxin and that this interaction is mediated by a lectin-like binding site located on the B oligomer.
Authors:
M J Brennan; J L David; J G Kenimer; C R Manclark
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  263     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1988 Apr 
Date Detail:
Created Date:  1988-05-02     Completed Date:  1988-05-02     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  4895-9     Citation Subset:  IM    
Affiliation:
Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, Maryland 20892.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Diphosphate Ribose / metabolism
Animals
Cell Line
Cholera Toxin / metabolism
Cricetinae
Cricetulus
Female
Gangliosides / metabolism
Membrane Glycoproteins / isolation & purification,  metabolism*
Molecular Weight
Ovary
Pertussis Toxin*
Protein Binding
Receptors, Mitogen / metabolism*
Virulence Factors, Bordetella / metabolism*
Wheat Germ Agglutinins / metabolism*
Chemical
Reg. No./Substance:
0/Gangliosides; 0/Membrane Glycoproteins; 0/Receptors, Mitogen; 0/Virulence Factors, Bordetella; 0/Wheat Germ Agglutinins; 20762-30-5/Adenosine Diphosphate Ribose; 9012-63-9/Cholera Toxin; EC 2.4.2.31/Pertussis Toxin

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


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