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Article: The surface proteinase of Treponema denticola may mediate attachment of the bacteria to epithelial cells

TitleThe surface proteinase of Treponema denticola may mediate attachment of the bacteria to epithelial cells
Authors
KeywordsAttachment
Epithelial cells
Periodontal disease
Proteinase
Treponema
Issue Date1996
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/anaerobe
Citation
Anaerobe, 1996, v. 2 n. 1, p. 39-46 How to Cite?
AbstractAttachment of Treponema denticola ATCC 35405 was studied using a new epithelial model consisting of cultured periodontal ligament epithelial cells. T. denticola bound rapidly but selectively to the epithelial cells. Even at a high concentration of 1 x 1011 bacteria/mL, 31% of the epithelial cells did not bind any treponemes in confluent cultures. However, some of the cells bound large numbers of spirochetes. In sparse cultures with migrating epithelial cells, higher amounts of T. denticola were bound than in confluent cultures. Electron microscopy showed direct contact of T. denticola and epithelial cell membranes without apparent preference in the adhesion sites in either of the cell types. Fibronectin and bovine serum albumin did not inhibit binding of T. denticola to the epithelial cells. In contrast, serum and fibrinogen markedly inhibited binding. Pretreatment of T. denticola with proteinase K, heating at 60°C or exposure to pH 3.2 inhibited the attachment by 30, 78 and 89%, respectively, suggesting that T. denticola proteins were involved in the attachment. Protease inhibitors, phenylmethylsulfonyl fluoride and p-chloromercuribenzoic acid that inhibited the chymotrypsin-like proteinase of T. denticola, also inhibited the attachment of the spirochetes to the epithelial cells. Purified chymotrypsin-like proteinase bound rapidly to the epithelial cells and specific antibodies against the proteinase inhibited attachment of the treponemes to the epithelial cells. The results suggest that the T. denticola surface-bound chymotrypsin-like proteinase is involved in the binding of the bacteria to epithelial cells.
Persistent Identifierhttp://hdl.handle.net/10722/55453
ISSN
2015 Impact Factor: 2.424
2015 SCImago Journal Rankings: 1.066
References

 

DC FieldValueLanguage
dc.contributor.authorLeung, WKen_HK
dc.contributor.authorHaapasalo, Men_HK
dc.contributor.authorUitto, VJen_HK
dc.contributor.authorHannam, PMen_HK
dc.contributor.authorMcBride, BCen_HK
dc.date.accessioned2009-08-06T03:37:55Z-
dc.date.available2009-08-06T03:37:55Z-
dc.date.issued1996en_HK
dc.identifier.citationAnaerobe, 1996, v. 2 n. 1, p. 39-46en_HK
dc.identifier.issn1075-9964en_HK
dc.identifier.urihttp://hdl.handle.net/10722/55453-
dc.description.abstractAttachment of Treponema denticola ATCC 35405 was studied using a new epithelial model consisting of cultured periodontal ligament epithelial cells. T. denticola bound rapidly but selectively to the epithelial cells. Even at a high concentration of 1 x 1011 bacteria/mL, 31% of the epithelial cells did not bind any treponemes in confluent cultures. However, some of the cells bound large numbers of spirochetes. In sparse cultures with migrating epithelial cells, higher amounts of T. denticola were bound than in confluent cultures. Electron microscopy showed direct contact of T. denticola and epithelial cell membranes without apparent preference in the adhesion sites in either of the cell types. Fibronectin and bovine serum albumin did not inhibit binding of T. denticola to the epithelial cells. In contrast, serum and fibrinogen markedly inhibited binding. Pretreatment of T. denticola with proteinase K, heating at 60°C or exposure to pH 3.2 inhibited the attachment by 30, 78 and 89%, respectively, suggesting that T. denticola proteins were involved in the attachment. Protease inhibitors, phenylmethylsulfonyl fluoride and p-chloromercuribenzoic acid that inhibited the chymotrypsin-like proteinase of T. denticola, also inhibited the attachment of the spirochetes to the epithelial cells. Purified chymotrypsin-like proteinase bound rapidly to the epithelial cells and specific antibodies against the proteinase inhibited attachment of the treponemes to the epithelial cells. The results suggest that the T. denticola surface-bound chymotrypsin-like proteinase is involved in the binding of the bacteria to epithelial cells.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/anaerobeen_HK
dc.relation.ispartofAnaerobeen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectAttachmenten_HK
dc.subjectEpithelial cellsen_HK
dc.subjectPeriodontal diseaseen_HK
dc.subjectProteinaseen_HK
dc.subjectTreponemaen_HK
dc.titleThe surface proteinase of Treponema denticola may mediate attachment of the bacteria to epithelial cellsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1075-9964&volume=2&issue=1&spage=39&epage=46&date=1996&atitle=The+Surface+Proteinase+of+Treponema+denticola+may+Mediate+Attachment+of+the+Bacteria+to+Epithelial+Cellsen_HK
dc.identifier.emailLeung, WK:ewkleung@hkucc.hku.hken_HK
dc.identifier.authorityLeung, WK=rp00019en_HK
dc.description.naturepostprinten_HK
dc.identifier.doi10.1006/anae.1996.0005en_HK
dc.identifier.scopuseid_2-s2.0-0029869134en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0029869134&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume2en_HK
dc.identifier.issue1en_HK
dc.identifier.spage39en_HK
dc.identifier.epage46en_HK
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridLeung, WK=25224691800en_HK
dc.identifier.scopusauthoridHaapasalo, M=7003569249en_HK
dc.identifier.scopusauthoridUitto, VJ=7004455896en_HK
dc.identifier.scopusauthoridHannam, PM=6602614873en_HK
dc.identifier.scopusauthoridMcBride, BC=7102465580en_HK

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