Premium
A general protein O ‐glycosylation system within the B urkholderia cepacia complex is involved in motility and virulence
Author(s) -
Lithgow Karen V.,
Scott Nichollas E.,
Iwashkiw Jeremy A.,
Thomson Euan L. S.,
Foster Leonard J.,
Feldman Mario F.,
Dennis Jonathan J.
Publication year - 2014
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.12540
Subject(s) - burkholderia cenocepacia , biology , virulence , glycosylation , microbiology and biotechnology , burkholderia cepacia complex , n linked glycosylation , escherichia coli , campylobacter jejuni , glycan , biochemistry , glycoprotein , biofilm , burkholderia , bacteria , gene , genetics
Summary Bacteria of the B urkholderia cepacia complex ( Bcc ) are pathogens of humans, plants, and animals. B urkholderia cenocepacia is one of the most common Bcc species infecting cystic fibrosis ( CF ) patients and its carriage is associated with poor prognosis. In this study, we characterized a general O ‐linked protein glycosylation system in B . cenocepacia K 56‐2. The PglL Bc O ‐oligosaccharyltransferase ( O ‐ OT ase), encoded by the cloned gene bcal0960 , was shown to be capable of transferring a heptasaccharide from the C ampylobacter jejuni N ‐glycosylation system to a N eisseria meningitides ‐derived acceptor protein in an E scherichia coli background, indicating that the enzyme has relaxed specificities for both the sugar donor and protein acceptor. In B cenocepacia K 56‐2, PglL Bc is responsible for the glycosylation of 23 proteins involved in diverse cellular processes. Mass spectrometry analysis revealed that these proteins are modified with a trisaccharide HexNAc ‐ HexNAc ‐ Hex , which is unrelated to the O ‐antigen biosynthetic process. The glycosylation sites that were identified existed within regions of low complexity, rich in serine, alanine, and proline. Disruption of bcal0960 abolished glycosylation and resulted in reduced swimming motility and attenuated virulence towards both plant and insect model organisms. This study demonstrates the first example of post‐translational modification in Bcc with implications for pathogenesis.