Streptococcal adhesin SspA/B analogue peptide inhibits adherence and impacts biofilm formation of Streptococcus mutans.

ABSTRACT: Streptococcus mutans, the major causative agent of dental caries, adheres to tooth surfaces via the host salivary glycoprotein-340 (gp340). This adherence can be competitively inhibited by peptides derived from the SspA/B adhesins of Streptococcus gordonii, a human commensal microbe that competes for the same binding sites. Ssp(A4K-A11K), a double-lysine substituted SspA/B peptide analogue, has been shown to exhibit superior in vitro binding affinity for a gp340-derived peptide (SRCRP2), suggesting that Ssp(A4K-A11K) may be of clinical interest. In the present work, we tested the inhibitory effects of Ssp(A4K-A11K) on adherence and biofilm formation of S. mutans by reconstructing an artificial oral environment using saliva-coated polystyrene plates and hydroxyapatite disks. Bacterial adher

SUBMITTER: Ito T 

PROVIDER: S-EPMC5386287 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature