Editorial: The role of glycans in infectious disease, Volume II.

Abstract

Volume 2 of “The role of glycans in infectious disease” Research Topic offers a continuity of research articles highlighting the evolving relevance of the glycocode at the interphase of pathogens and human disease, where it modulates the dynamics of bacterial, viral and fungal infections through finely tuned mechanisms. In this sense, mucosal surfaces are probably the sites where the most complex host-microbe interactions take place. In an original research article, Suwandi et al. characterize the role of the beta-1,4-N-acetylgalactosaminyltransferase enzyme (B4galnt2) in modulating infections by Citrobacter rodentium, a murine model pathogen for human enteropathogenic and enterohemorrhagic Escherichia coli. Escherichia coli is a gram-negative bacteria that can usually colonizes the human gut, but can cause intestinal or extraintestinal infections, including severe invasive disease such as bacteremia and sepsis. In this regard, E. coli is the most common cause of bacteremia in high-income countries and is a leading cause of meningitis in neonates (Bonten et al., 2021). Through the use of adhesion assays based on intestinal epithelial organoid-derived monolayers from B4galnt2−/− and B4galnt2+/+ mice the authors show that lack of this enzyme causes increased C. rodentium adherence, promoting increased inflammation and less proficiency in pathogen clearance by the host. The enhanced pathogen adhesion is dependent on the interaction of type 1 fimbriae and host mannosylated glycans that are increased as a result of deficient B4galnt2, as revealed by increased staining of the Galanthus nivalis lectin. These novel findings contribute to establish a more precise role of this enzyme in modulating host-pathogen interactions, but also in the establishment of gut microbiota.