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  • Blood group antigen recognition via the group A Streptococcal M Protein mediates host colonization

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    Author(s)
    De Oliveira, David MP
    Hartley-Tassell, Lauren
    Everest-Dass, Arun
    Day, Christopher J
    Dabbs, Rebecca A
    Ve, Thomas
    Kobe, Bostjan
    Nizet, Victor
    Packer, Nicolle H
    Walker, Mark J
    Jennings, Michael P
    Sanderson-Smith, Martina L
    Griffith University Author(s)
    Jennings, Michael P.
    Hartley-Tassell, Lauren E.
    Day, Christopher J.
    Ve, Thomas
    Everest-Dass, Arun
    Packer, Nicki
    Year published
    2017
    Metadata
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    Abstract
    Streptococcus pyogenes (group A streptococcus [GAS]) is responsible for over 500,000 deaths worldwide each year. The highly virulent M1T1 GAS clone is one of the most frequently isolated serotypes from streptococcal pharyngitis and invasive disease. The oral epithelial tract is a niche highly abundant in glycosylated structures, particularly those of the ABO(H) blood group antigen family. Using a high-throughput approach, we determined that a strain representative of the globally disseminated M1T1 GAS clone 5448 interacts with numerous, structurally diverse glycans. Preeminent among GAS virulence factors is the surface-expressed ...
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    Streptococcus pyogenes (group A streptococcus [GAS]) is responsible for over 500,000 deaths worldwide each year. The highly virulent M1T1 GAS clone is one of the most frequently isolated serotypes from streptococcal pharyngitis and invasive disease. The oral epithelial tract is a niche highly abundant in glycosylated structures, particularly those of the ABO(H) blood group antigen family. Using a high-throughput approach, we determined that a strain representative of the globally disseminated M1T1 GAS clone 5448 interacts with numerous, structurally diverse glycans. Preeminent among GAS virulence factors is the surface-expressed M protein. M1 protein showed high affinity for several terminal galactose blood group antigen structures. Deletion mutagenesis shows that M1 protein mediates glycan binding via its B repeat domains. Association of M1T1 GAS with oral epithelial cells varied significantly as a result of phenotypic differences in blood group antigen expression, with significantly higher adherence to those cells expressing H antigen structures compared to cells expressing A, B, or AB antigen structures. These data suggest a novel mechanism for GAS attachment to host cells and propose a link between host blood group antigen expression and M1T1 GAS colonization.
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    Journal Title
    mBio
    Volume
    8
    Issue
    1
    DOI
    https://doi.org/10.1128/mBio.02237-16
    Copyright Statement
    © 2017 De Oliveira et al. This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license (http://creativecommons.org/licenses/by/4.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
    Subject
    Microbiology not elsewhere classified
    Microbiology
    Publication URI
    http://hdl.handle.net/10072/339650
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    • Journal articles

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