Secretory IgAN-glycans contribute to the protection againstE. coliO55 infection of germ-free piglets

0550089 - MBÚ 2022 RIV GB eng J - Článek v odborném periodiku
Raskova Kafkova, L. - Brokešová, D. - Křupka, M. - Stehlíková, Zuzana - Dvořák, Jiří - Coufal, Štěpán - Fajstová, Alena - Šrůtková, Dagmar - Štěpánová, Kateřina - Hermanová, Petra - Štěpánková, Renata - Überall, I. - Škarda, J. - Novák, Z. - Vannucci, Luca - Tlaskalová-Hogenová, Helena - Jirásková Zákostelská, Zuzana - Šinkora, Marek - Městecký, Jiří - Raška, M.
Secretory IgAN-glycans contribute to the protection againstE. coliO55 infection of germ-free piglets.
Mucosal Immunology. Roč. 14, č. 2 (2021), s. 511-522. ISSN 1933-0219. E-ISSN 1935-3456
Grant CEP: GA ČR GA17-11275S
Institucionální podpora: RVO:61388971
Klíčová slova: escherichia-coli * immunoglobulin-a * o-glycosylation * small-intestine * hinge-region * n-glycan * component * antibodies * binding * pig
Obor OECD: Microbiology
Impakt faktor: 9.020, rok: 2021
Způsob publikování: Open access
https://www.nature.com/articles/s41385-020-00345-8

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 removedN-glycans, Fab, and Fc containing the secretory component (Fc-SC) during oral necrotoxigenicE. coliO55 challenge. SIgA, Fab, and Fc-SC were protective, whereas removal ofN-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 ofE. coliO55. These findings highlight the role of SIgA-associatedN-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.
Trvalý link: http://hdl.handle.net/11104/0325942