TY - JOUR
T1 - Determinants of proteolysis and cell-binding for the shigella flexneri cytotoxin, SigA
AU - Chua, Eng G
AU - Al-Hasani, Keith
AU - Scanlon, Martin J
AU - Adler, Ben
AU - Sakellaris, Harry Harry
PY - 2015
Y1 - 2015
N2 - Shigella flexneri secretes an enterotoxic, SPATE family autotransporter (AT), SigA, which has cytopathic activity towards cultured epithelial cells. Its cytopathic activity is due to its ability to degrade the cytoskeletal protein, alpha-fodrin. The mechanisms by which AT toxins target cells and tissues differ and the details of how SigA acts are not known. In the current study, the determinants of proteolysis and cell-targeting for SigA were determined. We demonstrate that the SigA passenger or alpha-domain consists of two functionally distinct domains, designated alpha1 and alpha2, which are sufficient to specify proteolytic and cell-binding activities, respectively.
AB - Shigella flexneri secretes an enterotoxic, SPATE family autotransporter (AT), SigA, which has cytopathic activity towards cultured epithelial cells. Its cytopathic activity is due to its ability to degrade the cytoskeletal protein, alpha-fodrin. The mechanisms by which AT toxins target cells and tissues differ and the details of how SigA acts are not known. In the current study, the determinants of proteolysis and cell-targeting for SigA were determined. We demonstrate that the SigA passenger or alpha-domain consists of two functionally distinct domains, designated alpha1 and alpha2, which are sufficient to specify proteolytic and cell-binding activities, respectively.
UR - http://link.springer.com/article/10.1007%2Fs00284-015-0893-8
U2 - 10.1007/s00284-015-0893-8
DO - 10.1007/s00284-015-0893-8
M3 - Article
SN - 0343-8651
VL - 71
SP - 613
EP - 617
JO - Current Microbiology
JF - Current Microbiology
IS - 5
ER -