Show simple item record

dc.contributor.authorDemuth, Donald R.
dc.contributor.authorIrvine, Douglas C.
dc.contributor.authorCosterton, J. William
dc.contributor.authorCook, Guy S.
dc.contributor.authorLamont, Richard J.
dc.date.accessioned2017-06-20T02:24:21Z
dc.date.available2017-06-20T02:24:21Z
dc.date.issued2001-09
dc.identifier.citationDemuth, D.R., D.C. Irvine, J.W. Costerton, G.S. Cook, and R.J. Lamont, "Discrete Protein Determinant Directs the Species-Specific Adherence of Porphyromonas gingivalis to Oral Streptococci," Infect. Immun., 69(9):571 (2001).en_US
dc.identifier.issn0019-9567
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/13080
dc.description.abstractFor pathogens to survive in the human oral cavity, they must identify a suitable niche in the complex multispecies biofilm that exists on oral tissues. The periodontal pathogenPorphyromonas gingivalis adheres toStreptococcus gordonii by interacting with a specific region of the streptococcal SspB polypeptide, designated BAR. However, it does not adhere to Streptococcus mutans, which expresses SpaP, a highly conserved homolog of SspB. Comparison of the predicted secondary structure of BAR with the corresponding region of SpaP suggested that the substitution of Asn for Gly1182 and Val for Pro1185 in SspB may confer a unique local structure that is not conserved in SpaP. A synthetic peptide of 26 amino acids that encompassed residues 1167 to 1193 of SspB promoted avid adherence of P. gingivalis, whereas a peptide derived from the region corresponding to BAR in SpaP was inactive. Substitution of Gly1182 and Pro1185 for Asn1182 and Val1185 in SspB by site-specific mutation generated proteins that were predicted to assume an SpaP-like secondary structure, and the purified proteins did not promote P. gingivalis adherence. Furthermore,Enterococcus faecalis strains expressing the site-specific mutants did not support adherence of P. gingivalis cells. In contrast, P. gingivalisadhered efficiently to E. faecalis strains expressing intact SspB or SspB-SpaP chimeric proteins containing BAR. These results suggest that a region of SspB consisting of 26 amino acids is sufficient to mediate the adherence of P. gingivalis to S. gordonii and that the species specificity of adherence arises from its interaction with a discrete structural determinant of SspB that is not conserved in SpaP.en_US
dc.titleDiscrete protein determinant directs the species-specific adherence of porphyromonas gingivalis to oral streptococcien_US
dc.typeArticleen_US
mus.citation.extentfirstpage5736en_US
mus.citation.extentlastpage5741en_US
mus.citation.issue9en_US
mus.citation.journaltitleInfection and Immunityen_US
mus.citation.volume59en_US
mus.identifier.categoryEngineering & Computer Scienceen_US
mus.identifier.doi10.1128/iai.69.9.5736-5741.2001en_US
mus.relation.collegeCollege of Engineeringen_US
mus.relation.departmentCenter for Biofilm Engineering.en_US
mus.relation.departmentChemical & Biological Engineering.en_US
mus.relation.departmentChemical Engineering.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.relation.researchgroupCenter for Biofilm Engineering.en_US
mus.data.thumbpage4en_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record