Biochemical basis for activation of virulence genes by bile salts in Vibrio parahaemolyticus.
Gut Microbes
; 8(4): 366-373, 2017 07 04.
Article
in En
| MEDLINE
| ID: mdl-28129014
ABSTRACT
Bile salts act as a stressor to bacteria that transit the intestinal tract. Enteric pathogens have hijacked bile as an intestinal signal to regulate virulence factors. We recently demonstrated that Vibrio parahemolyticus senses bile salts via a heterodimeric receptor formed by the periplasmic domains of inner-membrane proteins VtrA and VtrC. Crystal structures of the periplasmic complex reveal that VtrA and VtrC form a ß-barrel that binds bile salts in its hydrophobic interior to activate the VtrA cytoplasmic DNA-binding domain. Proteins with the same domain arrangement as VtrA and VtrC are widespread in Vibrio and related bacteria, where they are involved in regulating virulence and other unknown functions. Here we discuss our findings and review current knowledge on VtrA and VtrC homologs. We propose that signaling by these membrane-bound transcription factors can be advantageous for the regulation of membrane and secretory proteins.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacterial Proteins
/
Vibrio Infections
/
Vibrio parahaemolyticus
/
Bile Acids and Salts
/
Virulence Factors
Limits:
Animals
/
Humans
Language:
En
Journal:
Gut Microbes
Year:
2017
Document type:
Article
Affiliation country:
United States