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Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci

ABSTRACT: Despite lacking a tertiary structure, intrinsically disordered regions (IDRs) of proteins play a range of functional roles including cell signaling and protein folding in eukaryotes. However, the functions of bacterial IDRs are poorly understood. Here, we identify that streptococci possess a subset of proteins harboring long-extracytoplasmic IDRs enriched with serine/threonine residues that are O-glycosylated with N-acetylgalactosamine (GalNAc) by pgf operon in S. mutans, and glucose by GtrB-glycosyltransferase in S. pyogenes and S. pneumoniae. Peptidyl-prolyl isomerase PrsA and penicillin-binding protein Pbp1A are identified as the major glycoproteins. Furthermore, loss of IDR glycosylation in PrsA resulted in a defect in biofilm formation in S. mutans. Biochemical and functional characterization demonstrates that IDR does not affect PrsA stability and is protected with GalNAc from proteolysis by an unknown protease in S. mutans. Also, PrsA expression and the degree of glycosylation in S. mutans strongly depend on the length of IDR.

INSTRUMENT(S): LTQ Orbitrap Velos Pro, Orbitrap Exploris 480

ORGANISM(S): Streptococcus Pneumoniae D39 (ncbitaxon:373153) Streptococcus Pyogenes Mgas2111 (ncbitaxon:561522) Streptococcus Pneumoniae Tigr4 (ncbitaxon:170187) Streptococcus Mutans (ncbitaxon:1309)

SUBMITTER: Natalia Korotkova

PROVIDER: MSV000097289 | MassIVE | Tue Mar 11 10:44:00 GMT 2025

SECONDARY ACCESSION(S): PXD061713

REPOSITORIES: MassIVE

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