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O ‐linked protein glycosylation in mycoplasma
Author(s) -
Jordan David S.,
Daubenspeck James M.,
Laube Audra H.,
Renfrow Matthew B.,
Dybvig Kevin
Publication year - 2013
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12415
Subject(s) - glycoprotein , glycosylation , biology , biochemistry , mycoplasma pneumoniae , threonine , glycolipid , glycoconjugate , serine , glycosyltransferase , mycoplasma , mollicutes , peptide sequence , microbiology and biotechnology , enzyme , gene , archaeology , history , pneumonia
Summary Although mycoplasmas have a paucity of glycosyltransferases and nucleotidyltransferases recognizable by bioinformatics, these bacteria are known to produce polysaccharides and glycolipids. We show here that mycoplasmas also produce glycoproteins and hence have glycomes more complex than previously realized. Proteins from several species of M ycoplasma reacted with a glycoprotein stain, and the murine pathogen M ycoplasma arthritidis was chosen for further study. The presence of M . arthritidis glycoproteins was confirmed by high‐resolution mass spectrometry. O ‐linked glycosylation was clearly identified at both serine and threonine residues. No consensus amino acid sequence was evident for the glycosylation sites of the glycoproteins. A single hexose was identified as the O ‐linked modification, and glucose was inferred by 13 C ‐labelling to be the hexose at several of the glycosylation sites. This is the first study to conclusively identify sites of protein glycosylation in any of the mollicutes.