3OC5: Crystal Structure Of The Vibrio Cholerae Secreted Colonization Factor Tcpf

Vibrio cholerae relies on two main virulence factors-toxin-coregulated pilus (TCP) and cholera toxin-to cause the gastrointestinal disease cholera. TCP is a type IV pilus that mediates bacterial autoagglutination and colonization of the intestine. TCP is encoded by the tcp operon, which also encodes TcpF, a protein of unknown function that is secreted by V. cholerae in a TCP-dependent manner. Although TcpF is not required for TCP biogenesis, a tcpF mutant has a colonization defect in the infant mouse cholera model that is as severe as a pilus mutant. Furthermore, TcpF antisera protect against V. cholerae infection. TcpF has no apparent sequence homology to any known protein. Here, we report the de novo X-ray crystal structure of TcpF and the identification of an epitope that is critical for its function as a colonization factor. A monoclonal antibody recognizing this epitope is protective against V. cholerae challenge and adds to the protection provided by an anti-TcpA antibody. These data suggest that TcpF has a novel function in V. cholerae colonization and define a region crucial for this function.
PDB ID: 3OC5Download
MMDB ID: 90000
PDB Deposition Date: 2010/8/9
Updated in MMDB: 2011/05
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Similar Structures:
Biological Unit for 3OC5: monomeric; determined by author
Molecular Components in 3OC5
Label Count Molecule
Protein (1 molecule)
Toxin Coregulated Pilus Biosynthesis Protein F(Gene symbol: VC0837)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB