Document Detail


Borrelia burgdorferi bind to epithelial cell proteoglycans.
MedLine Citation:
PMID:  8113413     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Borrelia burgdorferi adhere to mammalian cells in vitro but neither the ligand(s) nor the receptor(s) has (have) been clearly established. Using an in vitro attachment-inhibition assay, a B. burgdorferi attachment mechanism has been identified. Heparin, heparan sulfate, and dermatan sulfate reduced the attachment of virulent B. burgdorferi strain 297 to HeLa cells by approximately 60%. In addition, virulent, but not avirulent, B. burgdorferi strains B31, N40, and HB19 demonstrated heparin attachment-inhibition. Attachment to Chinese hamster ovary cells deficient in heparan sulfate proteoglycans was reduced by 68% compared to attachment to wild-type cells and was identical to attachment at maximum heparin inhibition to the wild-type cells. Pretreatment of HeLa cell monolayers with heparitinase, heparinase, and chondroitinase ABC, but not with chondroitinase AC, reduced borrelial attachment by approximately 50%. A moderately high affinity, low copy number, promiscuous B. burgdorferi glycosaminoglycan receptor was demonstrated by equilibrium binding studies. A 39-kD polypeptide, purified by heparin affinity chromatography from Triton X-100 extracts derived from virulent borrelia, was a candidate for this receptor. These studies indicate that one mode of B. burgdorferi attachment to eukaryotic cells is mediated by a borrelial glycosaminoglycan receptor attaching to surface-exposed proteoglycans on mammalian cells.
Authors:
R D Isaacs
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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 clinical investigation     Volume:  93     ISSN:  0021-9738     ISO Abbreviation:  J. Clin. Invest.     Publication Date:  1994 Feb 
Date Detail:
Created Date:  1994-03-30     Completed Date:  1994-03-30     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  7802877     Medline TA:  J Clin Invest     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  809-19     Citation Subset:  AIM; IM    
Affiliation:
Department of Medicine, Department of Veterans Affairs Medical Center, Jackson, Mississippi 39216.
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MeSH Terms
Descriptor/Qualifier:
Animals
Bacterial Adhesion*
Bacterial Proteins / isolation & purification,  metabolism
Borrelia burgdorferi Group / drug effects,  pathogenicity,  physiology*
CHO Cells
Cell Line
Cricetinae
Electrophoresis, Polyacrylamide Gel
Epithelium / microbiology,  physiology
Glycosaminoglycans / pharmacology*
Hela Cells
Heparin / metabolism
Humans
Kinetics
Mammals
Molecular Weight
Proteoglycans / metabolism*
Receptors, Cell Surface / isolation & purification,  metabolism*
Virulence
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Glycosaminoglycans; 0/Proteoglycans; 0/Receptors, Cell Surface; 0/glycosaminoglycan receptor; 9005-49-6/Heparin
Comments/Corrections
Comment In:
J Clin Invest. 1994 Feb;93(2):460   [PMID:  8113383 ]

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


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