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

De Oliveira, David M. P., 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. and Sanderson-Smith, Martina L. (2017) Blood group antigen recognition via the group A Streptococcal M protein mediates host colonization. MBio, 8 1: . doi:10.1128/mBio.02237-16

Author De Oliveira, David M. P.
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.
Title Blood group antigen recognition via the group A Streptococcal M protein mediates host colonization
Journal name MBio   Check publisher's open access policy
ISSN 2150-7511
Publication date 2017-01-24
Sub-type Article (original research)
DOI 10.1128/mBio.02237-16
Open Access Status DOI
Volume 8
Issue 1
Total pages 12
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Language eng
Formatted 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 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.

Importance: There has been a resurgence in group A streptococcal (GAS) invasive disease, which has been paralleled by the emergence of the highly virulent M1T1 GAS clone. Intensive research has focused on mechanisms that contribute to the invasive nature of this serotype, while the mechanisms that contribute to host susceptibility to disease and bacterial colonization and persistence are still poorly understood. The M1T1 GAS clone is frequently isolated from the throat, an environment highly abundant in blood group antigen structures. This work examined the interaction of the M1 protein, the preeminent GAS surface protein, against a wide range of host-expressed glycan structures. Our data suggest that susceptibility to infection by GAS in the oral tract may correlate with phenotypic differences in host blood group antigen expression. Thus, variations in host blood group antigen expression may serve as a selective pressure contributing to the dissemination and overrepresentation of M1T1 GAS.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
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Created: Fri, 27 Jan 2017, 14:03:46 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences