Characterization of the pgf operon involved in the posttranslational modification of Streptococcus mutans surface proteins.

ABSTRACT: Protein glycosylation has been described as the most abundant and complex post-translational modification occurring in nature. Recent studies have enhanced our view of how this modification occurs in bacteria highlighting the role of protein glycosylation in various processes such as biofilm formation, virulence and host-microbe interactions. We recently showed that the collagen- and laminin-binding adhesin Cnm of the dental pathogen Streptococcus mutans is post-translationally modified by the PgfS glycosyltransferase. Following this initial identification of Cnm as a glycoprotein, we have now identified additional genes (pgfM1, pgfE and pgfM2) that are also involved in the posttranslational modification of Cnm. Similar to the previously characterized ΔpgfS strain, inactivation of pgfM1, p

SUBMITTER: Aviles-Reyes A 

PROVIDER: S-EPMC5856776 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature