Vibrio cholerae ensures function of host proteins required for virulence through consumption of luminal methionine sulfoxide
Fig 7
Vibrio cholerae augments virulence by modulation of host intestinal methionine sulfoxide reductase.
(A) Wild-type V. cholerae (WT) catabolizes dietary methionine sulfoxide (MetO) in the intestinal lumen, leaving host enterocyte methionine sulfoxide reductase (MsrA) free to repair proteins that have been inactivated by methionine oxidation. (B) In a V. cholerae ΔgcvT mutant infection, dietary MetO is not consumed by V. cholerae but rather taken up by host enterocytes. Dietary MetO competitively inhibits reduction of protein-associated MetO by MsrA within enterocytes.
