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Secretory IgA N-glycans contribute to the protection against E. coli O55 infection of germ-free piglets

Mucosal surfaces are colonized by highly diverse commensal microbiota. Coating with secretory IgA (SIgA) promotes the survival of commensal bacteria while it inhibits the invasion by pathogens. Bacterial coating could be mediated by antigen-specific SIgA recognition, polyreactivity, and/or by the SI...

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Detalles Bibliográficos
Autores principales: Raskova Kafkova, Leona, Brokesova, Diana, Krupka, Michal, Stehlikova, Zuzana, Dvorak, Jiri, Coufal, Stepan, Fajstova, Alena, Srutkova, Dagmar, Stepanova, Katerina, Hermanova, Petra, Stepankova, Renata, Uberall, Ivo, Skarda, Jozef, Novak, Zdenek, Vannucci, Luca, Tlaskalova-Hogenova, Helena, Jiraskova Zakostelska, Zuzana, Sinkora, Marek, Mestecky, Jiri, Raska, Milan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group US 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7946640/
https://www.ncbi.nlm.nih.gov/pubmed/32973324
http://dx.doi.org/10.1038/s41385-020-00345-8
Descripción
Sumario:Mucosal surfaces are colonized by highly diverse commensal microbiota. Coating with secretory IgA (SIgA) promotes the survival of commensal bacteria while it inhibits the invasion by pathogens. Bacterial coating could be mediated by antigen-specific SIgA recognition, polyreactivity, and/or by the SIgA-associated glycans. In contrast to many in vitro studies, only a few reported the effect of SIgA glycans in vivo. Here, we used a germ-free antibody-free newborn piglets model to compare the protective effect of SIgA, SIgA with enzymatically removed N-glycans, Fab, and Fc containing the secretory component (Fc-SC) during oral necrotoxigenic E. coli O55 challenge. SIgA, Fab, and Fc-SC were protective, whereas removal of N-glycans from SIgA reduced SIgA-mediated protection as demonstrated by piglets’ intestinal histology, clinical status, and survival. In vitro analyses indicated that deglycosylation of SIgA did not reduce agglutination of E. coli O55. These findings highlight the role of SIgA-associated N-glycans in protection. Further structural studies of SIgA-associated glycans would lead to the identification of those involved in the species-specific inhibition of attachment to corresponding epithelial cells.