Systemic Lectin-Glycan Interaction of Pathogenic Enteric Bacteria in the Gastrointestinal Tract

Abstract

Microorganisms, such as bacteria, viruses, and fungi, and host cells, such as plants and animals, have carbohydrate chains and lectins that reciprocally recognize one another. In hosts, the defense system is activated upon non-self-pattern recognition of microbial pathogen-associated molecular patterns. These are present in Gram-negative and Gram-positive bacteria and fungi. Glycan-based PAMPs are bound to a class of lectins that are widely distributed among eukaryotes. The first step of bacterial infection in humans is the adhesion of the pathogen’s lectin-like proteins to the outer membrane surfaces of host cells, which are composed of glycans. Microbes and hosts binding to each other specifically is of critical importance. The adhesion factors used between pathogens and hosts remain unknown; therefore, research is needed to identify these factors to prevent intestinal infection or treat it in its early stages. This review aims to present a vision for the prevention and treatment of infectious diseases by identifying the role of the host glycans in the immune response against pathogenic intestinal bacteria through studies on the lectin-glycan interaction.

Glycan-Adhering Lectins and Experimental Evaluation of a Lectin FimH Inhibitor in Enterohemorrhagic Escherichia coli (EHEC) O157:H7 Strain EDL933

“…Several studies have elucidated the interaction between pathogen lectins and host glycans during the early stages of infection [ 6 , 7 , 26 ]. We established an experimental strategy and method to characterize the systemic LGI of pathogenic intestinal bacteria in the gastrointestinal tract.…”

“…These protein-ligand and sugar chain-lectin ligand docking approaches were used to estimate the binding structure of ligands. Additionally, these strategies were used to identify and optimize binding sites and candidate materials [ 6 , 7 , 26 ].…”

“…Other lectin-like proteins include: Escherichia coli’s surface antigen 20 (CS20) and fimbriae protein SfaS; Hemophilus influenzae’s surface-adhesin protein E; Neisseria meningitidis’s autotransporter adhesin; and Salmonella enterica serovar Enteritidis’s ShdA, MisL, Sad, and BapA [ 6 ]. These proteins adhere to the host gut by the binding of lectin-like adhesins to host cell receptors that comprise glycans, resulting in lectin-glycan interactions (LGIs) [ 7 ].…”

Editorial: Mechanisms during bacterial infection: cellular recognition, signalling, and regulation

“…Most studies have focused on pathogenic factors-related symptoms in the pathogenesis of bacterial infections. Glycan-based pathogenicity, a lectin-glycan interaction (LGI) concept, has been proposed (Cho et al, 2022). LGIs can be systemically expanded during the immune response by the host glycans in the pathogenesis of infectious diseases (Kim, 2022a;Kim, 2022b). Notably, hosts and bacteria have evolved and use the same machinery, in which bacterial pathogens and hosts reciprocally utilize own proteins and glycans to invade and progress, respectively.…”

“…Most studies have focused on pathogenic factors-related symptoms in the pathogenesis of bacterial infections. Glycan-based pathogenicity, a lectin-glycan interaction (LGI) concept, has been proposed ( Cho et al., 2022 ). LGIs can be systemically expanded during the immune response by the host glycans in the pathogenesis of infectious diseases ( Kim, 2022a ; Kim, 2022b ).…”