Open AccessInhibition of adhesion‐promoting activity of a human salivary protein which promotes adhesion of Streptococcus mutans JBP to hydroxyapatite
Author(s) -
Kishimoto Etsuo,
Hay Donald I.,
Gibbons Ronald J.
Publication year - 1991
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1991.tb05118.x
Subject(s) - streptococcus mutans , chemistry , adhesion , biochemistry , ammonium chloride , ammonium , putrescine , galactosamine , microbiology and biotechnology , bacteria , glucosamine , biology , organic chemistry , enzyme , genetics
The adhesion‐promoting proteins (APP) (molecular mass approx. 300 kDa), which promote adhesion of Streptococcus mutans . JBF (serotype c) to hydroxyapatite, were isolated from human submandidular‐sublingual (SMSL) saliva by gel filtration on a Trisacryl GP2000 M column. The effects of hexoses, pentoses, methyl‐pentoses, hexosamines, N‐acetylhexosamines, a basic amino acid, polyamines and ammonium chloride on the bacterial adhesion‐promoting activity of the APP were examined. Galactosamine, mannosamine, l ‐lysine, spermine, putrescine, and ammonium chloride inhibited the adhesion‐promoting activities of the APP. The other sugars, including the N‐acetylhexosamines, were without effect. Thus, compounds containing a primary amino‐group appear to have a specific inhibitory effect on adhesion of S. mutans JBP to APP adsorbed onto hydroxyapatite, an activity which is lost if the amino‐group is acetylated.