AB5 toxin

Enterotoxin (OB-fold B subunit)
Identifiers
SymbolEnterotoxin
InterProIPR008992
SCOP22bos / SCOPe / SUPFAM

The AB5 toxins are six-component protein complexes secreted by certain pathogenic bacteria known to cause human diseases such as cholera, dysentery, and hemolytic–uremic syndrome. One component is known as the A subunit, and the remaining five components are B subunits. All of these toxins share a similar structure and mechanism for entering targeted host cells. The B subunit is responsible for binding to receptors to open up a pathway for the A subunit to enter the cell. The A subunit is then able to use its catalytic machinery to take over the host cell's regular functions.[1][2]

  1. ^ Le Nours, J.; Paton, A. W.; Byres, E.; Troy, S.; Herdman, B. P.; Johnson, M. D.; Paton, J. C.; Rossjohn, J.; Beddoe, T. (6 August 2013). "Structural Basis of Subtilase Cytotoxin SubAB Assembly". Journal of Biological Chemistry. 288 (38): 27505–27516. doi:10.1074/jbc.M113.462622. PMC 3779744. PMID 23921389.
  2. ^ Middlebrook, JL; Dorland, RB (Sep 1984). "Bacterial toxins: cellular mechanisms of action". Microbiological Reviews. 48 (3): 199–221. doi:10.1128/mr.48.3.199-221.1984. PMC 373009. PMID 6436655.

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