Analysing the structural effect of point mutations of cytotoxic necrotizing factor 1 (Cnf1) on lu/bcam adhesion glycoprotein association

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Abstract

Cytotoxic Necrotizing Factor 1 (CNF1) was identified in 1983 as a protein toxin produced by certain pathogenic strains of Escherichia coli. Since then, numerous studies have investigated its particularities. For instance, it is associated with the single chain AB-toxin family, and can be divided into different functional and structural domains, e.g., catalytic and transmembrane domain and interaction sites. A few years ago, the identification of the Lutheran (Lu) adhesion glycoprotein/basal cell adhesion molecule (BCAM) as a cellular receptor for CNF1 provided new insights into the adhesion process of CNF1. Very recently, the Ig-like domain 2 of Lu/BCAM was confirmed as the main interaction site using protein-protein interaction and competition studies with various different mutants. Here, I present in silico approaches that precisely explain the impact of these mutations, leading to a better explanation of these experimental studies. These results can be used in the development of future antitoxin strategies.

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APA

De Brevern, A. G. (2018, March 13). Analysing the structural effect of point mutations of cytotoxic necrotizing factor 1 (Cnf1) on lu/bcam adhesion glycoprotein association. Toxins. MDPI AG. https://doi.org/10.3390/toxins10030122

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