Abstract
The role in virulence of the Shigella flexneri ospB-phoN2 operon has been evaluated. Here we confirm that OspB is an effector and show that apyrase, the product of phoN2, may be a virulence factor, since it is required for efficient intercellular spreading. Apyrase may be important in a deoxynucleoside triphosphate-hydrolyzing activity-independent manner, suggesting that it may act as an interaction partner in the process of IcsA localization.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Apyrase / genetics
-
Apyrase / physiology*
-
Bacterial Outer Membrane Proteins / physiology
-
Bacterial Proteins / metabolism*
-
Biological Transport
-
DNA-Binding Proteins / metabolism*
-
Operon
-
Shigella flexneri / metabolism*
-
Shigella flexneri / pathogenicity
-
Transcription Factors / metabolism*
-
Virulence Factors
Substances
-
Bacterial Outer Membrane Proteins
-
Bacterial Proteins
-
DNA-Binding Proteins
-
Transcription Factors
-
Virulence Factors
-
virG protein, Shigella flexneri
-
Apyrase