Abstract
The role of the periplasmic disulfide oxidoreductase DsbA in Yop secretion was investigated in
Yersinia pestis
. A
Y. pestis dsbA
mutant secreted reduced amounts of the V antigen and Yops and expressed reduced amounts of the full-sized YscC protein. Site-directed mutagenesis of the four cysteine residues present in the YscC protein resulted in defects similar to those found in the
dsbA
mutant. These results suggest that YscC contains at least one disulfide bond that is essential for the function of this protein in Yop secretion.
