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Coaggregation between Porphyromonas gingivalis and Mutans Streptococci
Author(s) -
Kamaguchi Arihide,
Baba Hisae,
Hoshi Masaaki,
Inomata Koshiro
Publication year - 1994
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1994.tb01807.x
Subject(s) - porphyromonas gingivalis , streptococcus mutans , lysozyme , saliva , trypsin , arginine , microbiology and biotechnology , bacteroidaceae , biology , lysine , proteinase k , biochemistry , bacteria , enzyme , amino acid , genetics
Coaggregation occurred between Porphyromonas gingivalis and mutans streptococci. The coaggregation was completely inhibited by l ‐arginine, Nα‐ p ‐tosyl‐ l ‐lysine chloromethyl ketone (TLCK), and a trypsin inhibitor, and weakly inhibited by l ‐lysine, N ‐ethylmaleimide, lysozyme, and human whole saliva. The results of heat and proteinase K treatment suggested that a heat‐labile proteinaceous substance of P. gingivalis and a heat‐stable substance of mutans streptococci may play a role in the coaggregation. Mutans streptococci also aggregated in the presence of the heat‐labile factor in the supernatant of P. gingivalis. The aggregation was also inhibited by l ‐arginine, TLCK, and a trypsin inhibitor.