title: Coaggregation of Porphyromonas gingivalis and Prevotella intermedia.
abstract: Porphyromonas gingivalis cells coaggregated with Prevotella intermedia cells. The coaggregation was inhibited with L-arginine, L-lysine, Nalpha-p-tosyl-L-lysine chloromethyl ketone, trypsin inhibitor, and leupeptin. Heat- and proteinase K-treated P. gingivalis cells showed no coaggregation with P. intermedia cells, whereas heat and proteinase K treatments of P. intermedia cells did not affect the coaggregation. The vesicles from P. gingivalis culture supernatant aggregated with P. intermedia cells, and this aggregation was also inhibited by addition of L-arginine or L-lysine and by heat treatment of the vesicles. The rgpA rgpB, rgpA kgp, rgpA rgpB kgp, and rgpA kgp hagA mutants of P. gingivalis did not coaggregate with P. intermedia. On the other hand, the fimA mutant lacking the FimA fimbriae showed coaggregation with P. intermedia as well as the wild type parent. These results strongly imply that a heat-labile and proteinous factor on the cell surface of P gingivalis, most likely the gingipain-adhesin complex, is involved in coaggregation of P. gingivalis and P. intermedia.
authors.affiliation: Department of Oral Microbiology, School of Dentistry, Health Sciences University of Hokkaido, Hokkaido 061-0293, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Kamaguch
authors.forename: K
authors.initials: K
authors.lastname: Nakayama
authors.forename: T
authors.initials: T
authors.lastname: Ohyama
authors.forename: T
authors.initials: T
authors.lastname: Watanabe
authors.forename: M
authors.initials: M
authors.lastname: Okamoto
authors.forename: H
authors.initials: H
authors.lastname: Baba
mesh_terms: D018829:Adhesins, Bacterial / Q000235:genetics; D001120:Arginine / Q000494:pharmacology; D001422:Bacterial Adhesion / Q000187:drug effects; D001426:Bacterial Proteins / Q000235:genetics; D003546:Cysteine Endopeptidases / Q000235:genetics; D019286:Endopeptidase K / Q000494:pharmacology; D036781:Fimbriae Proteins; D000080867:Gingipain Cysteine Endopeptidases; D006388:Hemagglutinins / Q000235:genetics; D006358:Hot Temperature; D006801:Humans; D037102:Lectins; D007976:Leupeptins / Q000494:pharmacology; D008239:Lysine / Q000494:pharmacology; D009154:Mutation; D010940:Plant Proteins / Q000494:pharmacology; D016966:Porphyromonas gingivalis / Q000235:genetics / Q000378:metabolism*; D018713:Prevotella intermedia / Q000235:genetics / Q000378:metabolism*; D014107:Tosyllysine Chloromethyl Ketone / Q000494:pharmacology; D014361:Trypsin Inhibitors; D000516:alpha-Amylases / Q000037:antagonists & inhibitors
chemical_list: D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D000080867:Gingipain Cysteine Endopeptidases; D006388:Hemagglutinins; D037102:Lectins; D007976:Leupeptins; D010940:Plant Proteins; D014361:Trypsin Inhibitors; C063055:fimbrillin; C114923:hemagglutinin A, Porphyromonas gingivalis; D036781:Fimbriae Proteins; D014107:Tosyllysine Chloromethyl Ketone; D001120:Arginine; D000516:alpha-Amylases; D019286:Endopeptidase K; D003546:Cysteine Endopeptidases; C032854:leupeptin; D008239:Lysine