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Article: Conservation of msp, the gene encoding the major outer membrane protein of oral Treponema spp.

TitleConservation of msp, the gene encoding the major outer membrane protein of oral Treponema spp.
Authors
Issue Date1997
PublisherAmerican Society for Microbiology.
Citation
Journal Of Bacteriology, 1997, v. 179 n. 4, p. 1082-1089 How to Cite?
AbstractThe major surface protein (Msp) of Treponema denticola has been implicated as a mediator of the interaction between the spirochete and the gingival epithelium in periodontal diseases. Previous studies showed that the Msp of T. denticola ATCC 35405 had porin activity, depolarized epithelial cell membranes, bound to extracellular matrix components of epithelial cells, and formed a regular hexagonal surface array in the treponemal outer membrane. The gene encoding Msp in ATCC 35405 was recently cloned, sequenced, and expressed in Escherichia coli (J. C. Fenno, K.-H. Muller, and B.C. McBride, J. Bacteriol. 178:2489-2496. 1996). In the present study, we identified genes encoding Msp-like proteins in several oral spirochetes. A prominent heat-modifiable Msp-like protein having an apparent molecular mass of between 43 and 64 kDa was present in all oral spirochete strains tested. Antibodies raised against the ATCC 35405 Msp reacted strongly with the Msp proteins of T. denticola ATCC 35404 and T. vincentii, reacted very weakly with the Msp protein of T. denticola ATCC 33520, and did not react with K denticola OTK, T. socranskii, and T pectinovorum. The msp loci of the T. denticola strains and T. vincentii were identified in analyses using PCR with oligonucleotide primers derived from the DNA sequence flanking msp in ATCC 35405. Southern blot analysis showed at least three groups of related rasp DNA sequences. Comparison of DNA sequences of the 5' and 3' ends of the msp genes showed high sequence homology in the flanking regions and signal peptide coding regions, while the homologies between regions encoding the mature peptide were as low as 50%. The entire msp DNA sequences of T. denticola ATCC 33520 and OTK were determined, and the deduced Msp amine acid sequences were compared to the sequence of the previously reported Msp of ATCC 35405. The results show that the rasp locus is conserved in oral treponemes but that there are significant differences between the mature Msp peptides of different strains. Further studies of the antigenic domains, functional domains, and physical structures of Msp proteins, based on these results, will enhance understanding of the rule of Msp in the cytopathology, associated with oral spirochetes.
Persistent Identifierhttp://hdl.handle.net/10722/48924
ISSN
2015 Impact Factor: 3.198
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References

 

DC FieldValueLanguage
dc.contributor.authorFenno, JCen_HK
dc.contributor.authorWong, GWKen_HK
dc.contributor.authorHannam, PMen_HK
dc.contributor.authorMüller, KHen_HK
dc.contributor.authorLeung, WKen_HK
dc.contributor.authorMcBride, BCen_HK
dc.date.accessioned2008-06-12T06:29:48Z-
dc.date.available2008-06-12T06:29:48Z-
dc.date.issued1997en_HK
dc.identifier.citationJournal Of Bacteriology, 1997, v. 179 n. 4, p. 1082-1089en_HK
dc.identifier.issn0021-9193en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48924-
dc.description.abstractThe major surface protein (Msp) of Treponema denticola has been implicated as a mediator of the interaction between the spirochete and the gingival epithelium in periodontal diseases. Previous studies showed that the Msp of T. denticola ATCC 35405 had porin activity, depolarized epithelial cell membranes, bound to extracellular matrix components of epithelial cells, and formed a regular hexagonal surface array in the treponemal outer membrane. The gene encoding Msp in ATCC 35405 was recently cloned, sequenced, and expressed in Escherichia coli (J. C. Fenno, K.-H. Muller, and B.C. McBride, J. Bacteriol. 178:2489-2496. 1996). In the present study, we identified genes encoding Msp-like proteins in several oral spirochetes. A prominent heat-modifiable Msp-like protein having an apparent molecular mass of between 43 and 64 kDa was present in all oral spirochete strains tested. Antibodies raised against the ATCC 35405 Msp reacted strongly with the Msp proteins of T. denticola ATCC 35404 and T. vincentii, reacted very weakly with the Msp protein of T. denticola ATCC 33520, and did not react with K denticola OTK, T. socranskii, and T pectinovorum. The msp loci of the T. denticola strains and T. vincentii were identified in analyses using PCR with oligonucleotide primers derived from the DNA sequence flanking msp in ATCC 35405. Southern blot analysis showed at least three groups of related rasp DNA sequences. Comparison of DNA sequences of the 5' and 3' ends of the msp genes showed high sequence homology in the flanking regions and signal peptide coding regions, while the homologies between regions encoding the mature peptide were as low as 50%. The entire msp DNA sequences of T. denticola ATCC 33520 and OTK were determined, and the deduced Msp amine acid sequences were compared to the sequence of the previously reported Msp of ATCC 35405. The results show that the rasp locus is conserved in oral treponemes but that there are significant differences between the mature Msp peptides of different strains. Further studies of the antigenic domains, functional domains, and physical structures of Msp proteins, based on these results, will enhance understanding of the rule of Msp in the cytopathology, associated with oral spirochetes.en_HK
dc.format.extent418 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherAmerican Society for Microbiology.en_HK
dc.relation.ispartofJournal of Bacteriologyen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsJournal of Bacteriology. Copyright © American Society for Microbiology.en_HK
dc.rightsCopyright © American Society for Microbiology, Journal of Bacteriology, 1997, v. 179 n. 4, p. 1082-1089en_HK
dc.subject.meshBacterial Proteinsen_HK
dc.subject.meshConserved Sequenceen_HK
dc.subject.meshGenes, Bacterialen_HK
dc.subject.meshPorins - analysis - chemistry - geneticsen_HK
dc.subject.meshTreponema - chemistry - genetics - ultrastructureen_HK
dc.titleConservation of msp, the gene encoding the major outer membrane protein of oral Treponema spp.en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9193&volume=179&issue=4&spage=1082&epage=1089&date=1997&atitle=Conservation+of+msp,+the+gene+encoding+the+major+outer+membrane+protein+of+oral+Treponema+sppen_HK
dc.identifier.emailLeung, WK:ewkleung@hkucc.hku.hken_HK
dc.identifier.authorityLeung, WK=rp00019en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.pmid9023187-
dc.identifier.pmcidPMC178801-
dc.identifier.scopuseid_2-s2.0-0031054308en_HK
dc.identifier.hkuros24962-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0031054308&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume179en_HK
dc.identifier.issue4en_HK
dc.identifier.spage1082en_HK
dc.identifier.epage1089en_HK
dc.identifier.isiWOS:A1997WG58200013-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridFenno, JC=6602072985en_HK
dc.identifier.scopusauthoridWong, GWK=37022197800en_HK
dc.identifier.scopusauthoridHannam, PM=6602614873en_HK
dc.identifier.scopusauthoridMüller, KH=7403204791en_HK
dc.identifier.scopusauthoridLeung, WK=25224691800en_HK
dc.identifier.scopusauthoridMcBride, BC=7102465580en_HK

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