Abstract
Host-pathogen interactions are fundamental to our understanding of infectious diseases. Protein glycosylation is one kind of common post-translational modification, forming glycoproteins and modulating numerous important biological processes. It also occurs in host-pathogen interaction, affecting host resistance or pathogen virulence often because glycans regulate protein conformation, activity, and stability, etc. This review summarizes various roles of different glycoproteins during the interaction, which include: host glycoproteins prevent pathogens as barriers; pathogen glycoproteins promote pathogens to attack host proteins as weapons; pathogens glycosylate proteins of the host to enhance virulence; and hosts sense pathogen glycoproteins to induce resistance. In addition, this review also intends to summarize the roles of lectin (a class of protein entangled with glycoprotein) in host-pathogen interactions, including bacterial adhesins, viral lectins or host lectins. Although these studies show the importance of protein glycosylation in host-pathogen interaction, much remains to be discovered about the interaction mechanism.
Highlights
Glycosylation is the process by which a carbohydrate is attached to a target macromolecule, typically proteins and lipids
Straight or branched oligosaccharides consisting of 2–20 monosaccharide units are covalently bonded with amino acid side chains in proteins to form glycoproteins, catalyzed by glycosyltransferases which located in the endoplasmic reticulum (ER) and Golgi complex [51]
Host cell adhesion is important for infection initiation, and such a process is mediated by pathogen cell surface glycoproteins [100,101,102,103]
Summary
Glycosylation is the process by which a carbohydrate is attached to a target macromolecule, typically proteins and lipids. Glycoproteins are found in various forms, e.g., enzymes (nuclease, protease, glycosidase) [5,6], peptide hormones (chorionic gonadotropin, luteinizing hormone, thyrotropin, erythropoietin) [7], antibodies [8], lectins [9], membrane bond proteins [10], collagen [11], and fibronectin [12], some of which have great significance for clinical medicine Straight or branched oligosaccharides consisting of 2–20 monosaccharide units are covalently bonded with amino acid side chains in proteins to form glycoproteins, catalyzed by glycosyltransferases which located in the endoplasmic reticulum (ER) and Golgi complex [51].
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