TY - JOUR
T1 - Determinants of Proteolysis and Cell-Binding for the Shigella flexneri Cytotoxin, SigA
AU - Chua, Eng
AU - Al-Hasani, K.
AU - Scanlon, M.
AU - Adler, B.
AU - Sakellaris, Harry
PY - 2015
Y1 - 2015
N2 - © 2015, Springer Science+Business Media New York. 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, α-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 α-domain consists of two functionally distinct domains, designated α1 and α2, which are sufficient to specify proteolytic and cell-binding activities, respectively.
AB - © 2015, Springer Science+Business Media New York. 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, α-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 α-domain consists of two functionally distinct domains, designated α1 and α2, which are sufficient to specify proteolytic and cell-binding activities, respectively.
U2 - 10.1007/s00284-015-0893-8
DO - 10.1007/s00284-015-0893-8
M3 - Article
C2 - 26297175
SN - 0343-8651
VL - 71
SP - 613
EP - 617
JO - Current microbiology
JF - Current microbiology
IS - 5
ER -