Unknown

Dataset Information

0

The sigA gene which is borne on the she pathogenicity island of Shigella flexneri 2a encodes an exported cytopathic protease involved in intestinal fluid accumulation.


ABSTRACT: In this study, the sigA gene situated on the she pathogenicity island of Shigella flexneri 2a was cloned and characterized. Sequence analysis showed that sigA encodes a 139.6-kDa protein which belongs to the SPATE (serine protease autotransporters of Enterobacteriaceae) subfamily of autotransporter proteins. The demonstration that SigA is autonomously secreted from the cell to yield a 103-kDa processed form and possesses a conserved C-terminal domain for export from the cell were consistent with the autotransporter pathway of secretion. Functional analysis showed that SigA is a secreted temperature-regulated serine protease capable of degrading casein. SigA was cytopathic for HEp-2 cells, suggesting that it may be a cell-altering toxin with a role in the pathogenesis of Shigella infections. SigA was at least partly responsible for the ability of S. flexneri to stimulate fluid accumulation in ligated rabbit ileal loops.

SUBMITTER: Al-Hasani K 

PROVIDER: S-EPMC97446 | biostudies-literature | 2000 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

The sigA gene which is borne on the she pathogenicity island of Shigella flexneri 2a encodes an exported cytopathic protease involved in intestinal fluid accumulation.

Al-Hasani K K   Henderson I R IR   Sakellaris H H   Rajakumar K K   Grant T T   Nataro J P JP   Robins-Browne R R   Adler B B  

Infection and immunity 20000501 5


In this study, the sigA gene situated on the she pathogenicity island of Shigella flexneri 2a was cloned and characterized. Sequence analysis showed that sigA encodes a 139.6-kDa protein which belongs to the SPATE (serine protease autotransporters of Enterobacteriaceae) subfamily of autotransporter proteins. The demonstration that SigA is autonomously secreted from the cell to yield a 103-kDa processed form and possesses a conserved C-terminal domain for export from the cell were consistent with  ...[more]

Similar Datasets

| S-EPMC95444 | biostudies-literature
| S-EPMC1550401 | biostudies-literature
| S-EPMC175661 | biostudies-literature
2011-06-27 | GSE22800 | GEO
| PRJDB2601 | ENA
2011-06-27 | E-GEOD-22800 | biostudies-arrayexpress
| S-EPMC137130 | biostudies-literature
| PRJNA379672 | ENA
| S-EPMC10529421 | biostudies-literature
| PRJNA947612 | ENA