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Bacterial toxins are toxic substances that are produced and released by bacteria to target other bacterial or host cells. Bacteria often have antitoxins to avoid the deleterious effects of toxins.
Streptomyces are discovered to produce antibacterial protein complexes that selectively inhibit the hyphal growth of related species, a function distinct from that of the small-molecule antibiotics they are known for.
The pathogen Legionella pneumophila mediates NAD+-dependent ubiquitination pathways upon infection. Here, the authors show the Legionella effector MavL reverses ubiquitin ADP-ribosylation to regulate these pathways. MavL represents a new macrodomain class specific for reversal of arginine ADP-ribosylation with distinct ADP-ribose binding features.
Paeniclostridium sordellii hemorrhagic toxin (TcsH) targets TMPRSS2 to enter the host cells. Here, authors showed the cryo-EM structures of the TcsH-TMPRSS2 complex, providing a toxin-receptor interaction model for large clostridial toxins.
Bacteroides fragilis employs two different mechanisms, secreted microbe- and host-targeting toxins, that facilitate successful colonization of the mammalian gastrointestinal tract.
This month’s Genome Watch highlights how genome and transcriptome sequencing of newly identified endosymbionts helps to connect genetic information to their protective functions.
A recent study uncovered a new family of Enterococcus pore-forming toxins that use human leukocyte antigen class I or major histocompatibility complex class I as receptors.