TY - JOUR
T1 - Human glycan expression patterns influence Group A streptococcal colonization of epithelial cells
AU - De Oliveira, David M. P.
AU - Everest-Dass, Arun
AU - Hartley-Tassell, Lauren
AU - Day, Christopher J.
AU - Indraratna, Anuk
AU - Brouwer, Stephan
AU - Cleary, Ailish
AU - Kautto, Liisa
AU - Gorman, Jody
AU - Packer, Nicolle H.
AU - Jennings, Michael P.
AU - Walker, Mark J.
AU - Sanderson-Smith, Martina L.
PY - 2019/10
Y1 - 2019/10
N2 - Colonization of the oropharynx is the initial step in Group A Streptococcus (GAS) pharyngeal infection. We have previously reported that the highly virulent M1T1 GAS clone attaches to oral epithelial cells via M1 protein interaction with blood group antigen carbohydrate structures. Here, we have identified that colonization of human oral epithelial cells by GAS serotypes M3 and M12 is mediated by human blood group antigens [ABO(H)] and Lewis (Le) antigen expression. Removal of linkage-specific fucose, galactose, N-acetylgalactosamine, and sialic acid modulated GAS colonization, dependent on host ABO(H) blood group and Le expression profile. Furthermore, N-linked glycans from human salivary glycoproteins, when released and purified, were potent inhibitors of M1, M3, and M12 GAS colonization ex vivo. These data highlight the important role played by human protein glycosylation patterns in GAS attachment to oral epithelial cell surfaces.
AB - Colonization of the oropharynx is the initial step in Group A Streptococcus (GAS) pharyngeal infection. We have previously reported that the highly virulent M1T1 GAS clone attaches to oral epithelial cells via M1 protein interaction with blood group antigen carbohydrate structures. Here, we have identified that colonization of human oral epithelial cells by GAS serotypes M3 and M12 is mediated by human blood group antigens [ABO(H)] and Lewis (Le) antigen expression. Removal of linkage-specific fucose, galactose, N-acetylgalactosamine, and sialic acid modulated GAS colonization, dependent on host ABO(H) blood group and Le expression profile. Furthermore, N-linked glycans from human salivary glycoproteins, when released and purified, were potent inhibitors of M1, M3, and M12 GAS colonization ex vivo. These data highlight the important role played by human protein glycosylation patterns in GAS attachment to oral epithelial cell surfaces.
KW - glycosylation
KW - M protein
KW - pathogenesis
KW - blood group antigens
UR - http://www.scopus.com/inward/record.url?scp=85072716495&partnerID=8YFLogxK
UR - http://purl.org/au-research/grants/nhmrc/1143266
UR - http://purl.org/au-research/grants/nhmrc/1071659
U2 - 10.1096/fj.201900559R
DO - 10.1096/fj.201900559R
M3 - Article
C2 - 31262188
AN - SCOPUS:85072716495
SN - 0892-6638
VL - 33
SP - 10808
EP - 10818
JO - FASEB journal : official publication of the Federation of American Societies for Experimental Biology
JF - FASEB journal : official publication of the Federation of American Societies for Experimental Biology
IS - 10
ER -