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A wide variety of bacterial pore-forming toxins (PFTs) can mediate virulence through epithelial cell barrier dysfunction, immune cell cytotoxicity, and direct tissue damage. Structurally, PFTs are composed of alpha-helices or beta-barrels. Beta-barrel PFTs selectively bind to host protein receptors, thereby defining specific host species and cell-specific targets.
Xiong and colleagues identified Epxs, a family of small beta-barrel PFTs homologous to known hemolysins in Enterococcus faecalis, E. faecium, and E. hirae. Using a genome-wide CRISPR-Cas9 screen, they identified human leukocyte antigen class 1 (HLA-1) complex as a receptor for two of these toxins, Epx2 and Epx3. Homologous major histocompatibility complex class 1 (MHC 1) from equin…