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, 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.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Avilés-Reyes A,Freires IA,Besingi R,Purushotham S,Deivanayagam C,Brady LJ,Abranches J,Lemos JAdoi
10.1038/s41598-018-23170-3subject
Has Abstractpub_date
2018-03-16 00:00:00pages
4705issue
1issn
2045-2322pii
10.1038/s41598-018-23170-3journal_volume
8pub_type
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