Remodeling of host glycoproteins during bacterial infection

Abstract

Protein glycosylation is a common post-translational modification found in all living organisms. This modification in bacterial pathogens plays a pivotal role in their infectious processes including pathogenicity, immune evasion, and host-pathogen interactions. Importantly, many key proteins of host immune systems are also glycosylated and bacterial pathogens can notably modulate glycosylation of these host proteins to facilitate pathogenesis through the induction of abnormal host protein activity and abundance. In recent years, interest in studying the regulation of host protein glycosylation caused by bacterial pathogens is increasing to fully understand bacterial pathogenesis. In this review, we focus on how bacterial pathogens regulate remodeling of host glycoproteins during infections to promote the pathogenesis. [

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“…Glycosyltransferases execute essential cellular modifications, adjusting the glycosylation processes of proteins, lipids, and nucleic acids, thereby influencing their functional integrity and stability ( 60 – 62 ). These enzymes are involved in a wide range of biological activities, including cell signaling, cellular interactions, adhesion, tissue development, and cancerous transformations ( 63 – 66 ).…”