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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 Δ pgfS  strain, inactivation of  pgfM1 ,  pgfE  or  pgfM2  directly impacts Cnm by altering its migration pattern, proteolytic stability and function. In addition, we identified the wall-associated protein A (WapA) as an additional substrate of Pgf-dependent modification. We conclude that the  pgS-pgfM1-pgfE-pgfM2  operon encodes for a protein machinery that can modify, likely through the addition of glycans, both core and non-core gene products in  S .  mutans .

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