Vibrio cholerae colonization factor TcpF
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IntroductionIntroduction
Molecule: Toxin coregulated pilus biosynthesis protein F
Type:protein Length: 318 Organism:Vibrio Cholerae
TcpF is a toxin-coregulated pilus that facilitates colonization of vibrio cholerae in the intestine. Vibrio cholerae relies on two main virulence factors: toxin-coregulated pilus (TCP) and cholera toxin (CT) to cause the gastrointestinal disease cholera. TCP, encoded by the tcp operon, is a type IV pilus that mediates bacterial autoagglutination and colonization of the intestine.
StructureStructure
The structure of TcpF is consisted with an and a connected by an extended linker segment (residues 186–189). In detail, the NTD is composed of a short twisted β-sheet encapsulated by seven short α-helices with a second twisted β-sheet forming the floor of this domain. The NTD is connected with The CTD, which consists of two twisted antiparallel β-sheets. TCP is a filamentous structure belongs. The architecture of TcpF, with discrete NTD and CTD joined by a linker, is flexible that allow to accommodate a larger substrate. By looking at the homology of TcpF, the NTD and the CTD together form a unique interface that interacts with partner proteins to function in V. cholerae colonization.
FunctionFunction
TcpF, identified in classical isolates of V. cholerae O1 is an essential factor for colonization in the infant mouse cholera model. Bacteria lacking tcpF are deficient in colonization, and anti-TcpF antibodies are protective in the infant mouse cholera model. TcpF is expressed in vivo during human infection and generates a substantial immune response in patients infected with V. cholera. The mechanism for the action of TcpF remains to be elucidated.
Multiply Sequence AlignmentMultiply Sequence Alignment
ApplicationApplication