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  • Identification of Bacterial Protein O-Oligosaccharyltransferases and Their Glycoprotein Substrates

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    Author(s)
    Schulz, Benjamin L
    Jen, Freda EC
    Power, Peter M
    Jones, Christopher E
    Fox, Kate L
    Ku, Shan C
    Blanchfield, Joanne T
    Jennings, Michael P
    Griffith University Author(s)
    Jennings, Michael P.
    Jen, Freda E.
    Ku, Shan
    Year published
    2013
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    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 ...
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    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.
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    Journal Title
    PloS One
    Volume
    8
    Issue
    5
    DOI
    https://doi.org/10.1371/journal.pone.0062768
    Copyright Statement
    © 2013 Schulz et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
    Subject
    History and Archaeology
    Publication URI
    http://hdl.handle.net/10072/55578
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    • Journal articles

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