title: Treponema denticola improves adhesive capacities of Porphyromonas gingivalis.
abstract: Porphyromonas gingivalis, an important etiological agent of periodontal disease, is frequently found associated with Treponema denticola, an anaerobic spirochete, in pathogenic biofilms. However, interactions between these two bacteria are not well understood at the molecular level. In this study, we seek to link the influence of T. denticola on the expression of P. gingivalis proteases with its capacities to adhere and to form biofilms. The P. gingivalis genes encoding Arg-gingipain A (RgpA), Lys-gingipain (Kgp), and hemagglutinin A (HagA) were more strongly expressed after incubation with T. denticola compared with P. gingivalis alone. The amounts of the three resulting proteins, all of which contain hemagglutinin adhesion domains, were increased in culture supernatants. Moreover, incubation of P. gingivalis with T. denticola promoted static and dynamic biofilm formation, primarily via a time-dependent enhancement of P. gingivalis adhesion capacities on bacterial partners such as Streptococcus gordonii. Adhesion of P. gingivalis to human cells was also increased. These results showed that interactions of P. gingivalis with other bacterial species, such as T. denticola, induce increased adhesive capacities on various substrata by hemagglutinin adhesion domain-containing proteins.
authors.affiliation: Equipe de Microbiologie, UPRES-EA 1254, Université Européenne de Bretagne, Université de Rennes 1, Rennes, France.
authors.forename: V
authors.initials: V
authors.lastname: Meuric
authors.forename: B
authors.initials: B
authors.lastname: Martin
authors.forename: H
authors.initials: H
authors.lastname: Guyodo
authors.forename: A
authors.initials: A
authors.lastname: Rouillon
authors.forename: Z
authors.initials: Z
authors.lastname: Tamanai-Shacoori
authors.forename: F
authors.initials: F
authors.lastname: Barloy-Hubler
authors.forename: M
authors.initials: M
authors.lastname: Bonnaure-Mallet
mesh_terms: D018829:Adhesins, Bacterial / Q000032:analysis; D001422:Bacterial Adhesion / Q000502:physiology*; D001426:Bacterial Proteins / Q000032:analysis; D001431:Bacteriological Techniques; D018441:Biofilms / Q000254:growth & development; D018920:Coculture Techniques; D003546:Cysteine Endopeptidases / Q000032:analysis; D010861:Fimbriae, Bacterial / Q000737:chemistry; D015964:Gene Expression Regulation, Bacterial / Q000235:genetics; D000080867:Gingipain Cysteine Endopeptidases; D006388:Hemagglutinins / Q000032:analysis; D006801:Humans; D007624:KB Cells; D037102:Lectins / Q000032:analysis; D056265:Microbial Interactions; D016966:Porphyromonas gingivalis / Q000201:enzymology / Q000472:pathogenicity / Q000502:physiology*; D054773:Streptococcus gordonii / Q000502:physiology; D013997:Time Factors; D048373:Treponema denticola / Q000502:physiology*; D037521:Virulence Factors / Q000032:analysis
chemical_list: D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D000080867:Gingipain Cysteine Endopeptidases; D006388:Hemagglutinins; D037102:Lectins; D037521:Virulence Factors; C114923:hemagglutinin A, Porphyromonas gingivalis; D003546:Cysteine Endopeptidases