Abstract
Human pathogenic yersiniae organisms export and translocate the Yop virulence proteins and V antigen upon contact with a eukaryotic cell. Yersinia pestis mutants defective for production of YscX or YscY were unable to export the Yops and V antigen. YscX and YscY were both present in the Y. pestis cell pellet fraction; however, YscX was also found in the culture supernatant. YscY showed structural and amino acid sequence similarities to the Syc family of proteins. YscY specifically recognized and bound to a region of YscX that included a predicted coiled-coil region. These data suggest that YscY may function as a chaperone for YscX in Y. pestis.
Original language | English (US) |
---|---|
Pages (from-to) | 1834-1843 |
Number of pages | 10 |
Journal | Journal of bacteriology |
Volume | 182 |
Issue number | 7 |
DOIs | |
State | Published - Apr 2000 |
ASJC Scopus subject areas
- Microbiology
- Molecular Biology