TY - JOUR
T1 - Adhesin degradation accelerates delivery of heat-labile toxin by enterotoxigenic Escherichia coli
AU - Roy, Koushik
AU - Kansal, Rita
AU - Bartels, Scott R.
AU - Hamilton, David J.
AU - Shaaban, Salwa
AU - Fleckenstein, James M.
PY - 2011/8/26
Y1 - 2011/8/26
N2 - Many enteric pathogens, including enterotoxigenic Escherichia coli (ETEC), produce one or more serine proteases that are secreted via the autotransporter (or type V) bacterial secretion pathway. These molecules have collectively been referred to as SPATE proteins (serine protease autotransporter of the Enterobacteriaceae). EatA, an autotransporter previously identifiedinETEC, possessesafunctionalserineproteasemotifwithinits secreted amino-terminal passenger domain. Although this protein is expressed by many ETEC strains and is highly immunogenic, its precise function is unknown. Here, we demonstrate that EatA degrades a recently characterized adhesin, EtpA, resulting in modulation of bacterial adhesion and accelerated delivery of the heatlabile toxin, a principal ETEC virulence determinant. Antibodies raised against the passenger domain of EatA impair ETEC delivery of labile toxin to epithelial cells suggesting that EatA may be an effective target for vaccine development.
AB - Many enteric pathogens, including enterotoxigenic Escherichia coli (ETEC), produce one or more serine proteases that are secreted via the autotransporter (or type V) bacterial secretion pathway. These molecules have collectively been referred to as SPATE proteins (serine protease autotransporter of the Enterobacteriaceae). EatA, an autotransporter previously identifiedinETEC, possessesafunctionalserineproteasemotifwithinits secreted amino-terminal passenger domain. Although this protein is expressed by many ETEC strains and is highly immunogenic, its precise function is unknown. Here, we demonstrate that EatA degrades a recently characterized adhesin, EtpA, resulting in modulation of bacterial adhesion and accelerated delivery of the heatlabile toxin, a principal ETEC virulence determinant. Antibodies raised against the passenger domain of EatA impair ETEC delivery of labile toxin to epithelial cells suggesting that EatA may be an effective target for vaccine development.
UR - http://www.scopus.com/inward/record.url?scp=80051940624&partnerID=8YFLogxK
U2 - 10.1074/jbc.M111.251546
DO - 10.1074/jbc.M111.251546
M3 - Article
C2 - 21757737
AN - SCOPUS:80051940624
VL - 286
SP - 29771
EP - 29779
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 34
ER -