Structural Basis of the Pore-Forming Toxin/Membrane Interaction

Overview

Journal Toxins (Basel)

Publisher MDPI

Specialty Toxicology

Date 2021 Feb 12

PMID 33572271

Citations 17

Authors

Yajuan Li

Yuelong Li

Hylemariam Mihiretie Mengist

Cuixiao Shi

Caiying Zhang

Bo Wang

Tingting Li

Ying Huang

Yuanhong Xu

Tengchuan Jin

Affiliations

Soon will be listed here.

Abstract

With the rapid growth of antibiotic-resistant bacteria, it is urgent to develop alternative therapeutic strategies. Pore-forming toxins (PFTs) belong to the largest family of virulence factors of many pathogenic bacteria and constitute the most characterized classes of pore-forming proteins (PFPs). Recent studies revealed the structural basis of several PFTs, both as soluble monomers, and transmembrane oligomers. Upon interacting with host cells, the soluble monomer of bacterial PFTs assembles into transmembrane oligomeric complexes that insert into membranes and affect target cell-membrane permeability, leading to diverse cellular responses and outcomes. Herein we have reviewed the structural basis of pore formation and interaction of PFTs with the host cell membrane, which could add valuable contributions in comprehensive understanding of PFTs and searching for novel therapeutic strategies targeting PFTs and interaction with host receptors in the fight of bacterial antibiotic-resistance.

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