TY - JOUR
T1 - The enteropathogenic Escherichia coli effector protein EspF decreases sodium hydrogen exchanger 3 activity
AU - Hodges, Kim
AU - Alto, Neal M.
AU - Ramaswamy, K.
AU - Dudeja, Pradeep K.
AU - Hecht, Gail
PY - 2008/8
Y1 - 2008/8
N2 - Enteropathogenic Escherichia coli (EPEC) have been previously shown to alter sodium hydrogen exchanger 3 (NHE3) activity in human intestinal epithelial cells. To further characterize these observations, PS120 fibroblasts transfected with NHE3 were studied. EPEC E2348/69 infection decreased NHE3 activity in PS120 fibroblasts. The effect on NHE3 was enhanced when PS120 cells were co-transfected with the scaffolding/ regulatory proteins NHERF1 or NHERF2 or EBP50 and E3KARP respectively. The decrease in NHE3 activity was dependent on an intact type III secretion system, although intimate attachment mediated by translocated intimin receptor was not required. Despite its ability to bind to NHERF proteins, the EPEC effector Map had no impact on the regulation of NHE activity. Instead, EspF was found to be responsible for decreased NHE3 activity. However, neither EspF-induced apoptosis nor the interaction of EspF with sorting nexin-9, an endocytic protein, were involved.
AB - Enteropathogenic Escherichia coli (EPEC) have been previously shown to alter sodium hydrogen exchanger 3 (NHE3) activity in human intestinal epithelial cells. To further characterize these observations, PS120 fibroblasts transfected with NHE3 were studied. EPEC E2348/69 infection decreased NHE3 activity in PS120 fibroblasts. The effect on NHE3 was enhanced when PS120 cells were co-transfected with the scaffolding/ regulatory proteins NHERF1 or NHERF2 or EBP50 and E3KARP respectively. The decrease in NHE3 activity was dependent on an intact type III secretion system, although intimate attachment mediated by translocated intimin receptor was not required. Despite its ability to bind to NHERF proteins, the EPEC effector Map had no impact on the regulation of NHE activity. Instead, EspF was found to be responsible for decreased NHE3 activity. However, neither EspF-induced apoptosis nor the interaction of EspF with sorting nexin-9, an endocytic protein, were involved.
UR - http://www.scopus.com/inward/record.url?scp=47549095681&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=47549095681&partnerID=8YFLogxK
U2 - 10.1111/j.1462-5822.2008.01163.x
DO - 10.1111/j.1462-5822.2008.01163.x
M3 - Article
C2 - 18433466
AN - SCOPUS:47549095681
SN - 1462-5814
VL - 10
SP - 1735
EP - 1745
JO - Cellular Microbiology
JF - Cellular Microbiology
IS - 8
ER -