Identification of bacterial protein O-Oligosaccharyltransferases and their glycoprotein substrates

Schulz, Benjamin L., Jen, Freda E. C., Power, Peter M., Jones, Christopher E., Fox, Kate L., Ku, Shan C., Blanchfield, Joanne T. and Jennings, Michael P. (2013) Identification of bacterial protein O-Oligosaccharyltransferases and their glycoprotein substrates. PLoS One, 8 5: e62768.1-e62768.11. doi:10.1371/journal.pone.0062768


Author Schulz, Benjamin L.
Jen, Freda E. C.
Power, Peter M.
Jones, Christopher E.
Fox, Kate L.
Ku, Shan C.
Blanchfield, Joanne T.
Jennings, Michael P.
Title Identification of bacterial protein O-Oligosaccharyltransferases and their glycoprotein substrates
Formatted title
Identification of bacterial protein O-Oligosaccharyltransferases and their glycoprotein substrates
Journal name PLoS One   Check publisher's open access policy
ISSN 1932-6203
Publication date 2013-05-03
Year available 2013
Sub-type Article (original research)
DOI 10.1371/journal.pone.0062768
Open Access Status DOI
Volume 8
Issue 5
Start page e62768.1
End page e62768.11
Total pages 11
Place of publication San Francisco, United States
Publisher Public Library of Science
Collection year 2014
Language eng
Formatted abstract
O-glycosylation of proteins in Neisseria meningitidis is catalyzed by PglL, which belongs to a protein family including WaaL O-antigen ligases. We developed two hidden Markov models that identify 31 novel candidate PglL homologs in diverse bacterial species, and describe several conserved sequence and structural features. Most of these genes are adjacent to possible novel target proteins for glycosylation. We show that in the general glycosylation system of N. meningitidis, efficient glycosylation of additional protein substrates requires local structural similarity to the pilin acceptor site. For some Neisserial PglL substrates identified by sensitive analytical approaches, only a small fraction of the total protein pool is modified in the native organism, whereas others are completely glycosylated. Our results show that bacterial protein O-glycosylation is common, and that substrate selection in the general Neisserial system is dominated by recognition of structural homology.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Article number e62768

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
School of Chemistry and Molecular Biosciences
 
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Citation counts: TR Web of Science Citation Count  Cited 17 times in Thomson Reuters Web of Science Article | Citations
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Created: Fri, 24 May 2013, 14:56:12 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences