Identification of bacterial protein O-oligosaccharyltransferases and their glycoprotein substrates.

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 a...

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Autores principales:	Benjamin L Schulz, Freda E C Jen, Peter M Power, Christopher E Jones, Kate L Fox, Shan C Ku, Joanne T Blanchfield, Michael P Jennings
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c5644d8ac81c4a25917daf0aa55e2761
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spelling	oai:doaj.org-article:c5644d8ac81c4a25917daf0aa55e27612021-11-18T07:46:56ZIdentification of bacterial protein O-oligosaccharyltransferases and their glycoprotein substrates.1932-620310.1371/journal.pone.0062768https://doaj.org/article/c5644d8ac81c4a25917daf0aa55e27612013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23658772/?tool=EBIhttps://doaj.org/toc/1932-6203O-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.Benjamin L SchulzFreda E C JenPeter M PowerChristopher E JonesKate L FoxShan C KuJoanne T BlanchfieldMichael P JenningsPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 5, p e62768 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Benjamin L Schulz Freda E C Jen Peter M Power Christopher E Jones Kate L Fox Shan C Ku Joanne T Blanchfield Michael P Jennings Identification of bacterial protein O-oligosaccharyltransferases and their glycoprotein substrates.
description	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.
format	article
author	Benjamin L Schulz Freda E C Jen Peter M Power Christopher E Jones Kate L Fox Shan C Ku Joanne T Blanchfield Michael P Jennings
author_facet	Benjamin L Schulz Freda E C Jen Peter M Power Christopher E Jones Kate L Fox Shan C Ku Joanne T Blanchfield Michael P Jennings
author_sort	Benjamin L Schulz
title	Identification of bacterial protein O-oligosaccharyltransferases and their glycoprotein substrates.
title_short	Identification of bacterial protein O-oligosaccharyltransferases and their glycoprotein substrates.
title_full	Identification of bacterial protein O-oligosaccharyltransferases and their glycoprotein substrates.
title_fullStr	Identification of bacterial protein O-oligosaccharyltransferases and their glycoprotein substrates.
title_full_unstemmed	Identification of bacterial protein O-oligosaccharyltransferases and their glycoprotein substrates.
title_sort	identification of bacterial protein o-oligosaccharyltransferases and their glycoprotein substrates.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/c5644d8ac81c4a25917daf0aa55e2761
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Identification of bacterial protein O-oligosaccharyltransferases and their glycoprotein substrates.

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