Vibrio cholerae colonization factor TcpF
From Proteopedia
(New page: <!-- Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page. Or use the four-green-boxes-button to insert scrollable text adjacent to a Jmol applet. Che...) |
|||
| Line 5: | Line 5: | ||
--> | --> | ||
1 | 1 | ||
| + | <Structure load='3OC8' size='500' frame='true' align='right' caption='Insert caption here' scene='3D TcpF' /> | ||
| + | |||
| + | [[Image:3oc5 bio r 500.jpg|left|200px|thumb|Crystal Structure of the TcpF[[1xtc]]]] | ||
| + | == Introduction == | ||
| + | |||
| + | 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--to cause the gastrointestinal disease cholera. TCP is a type IV pilus that mediates bacterial autoagglutination and colonization of the intestine. TcpF is secreted from bacterial cell by the TCP apparatus and is also essential for colonization. | ||
| + | |||
| + | |||
| + | |||
| + | == Structure == | ||
| + | |||
| + | |||
| + | By looking the X-ray crystal structure of native TcpF, the structure of TcpF is consisted with an N-terminal domain (NTD;residues 1–185) and a C-terminal domain (CTD; residues 190–318) joined 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. | ||
| + | |||
| + | |||
| + | |||
| + | == Function == | ||
| + | |||
| + | |||
| + | 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. | ||
| + | |||
| + | |||
| + | |||
| + | |||
| + | == Application == | ||
| + | [[Image:TcpF hydrophic model.png|left|200px|thumb| TcpF Hydrophobic model[[1xtc]]]] | ||
Revision as of 03:15, 4 May 2012
1
|
Contents |
Introduction
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--to cause the gastrointestinal disease cholera. TCP is a type IV pilus that mediates bacterial autoagglutination and colonization of the intestine. TcpF is secreted from bacterial cell by the TCP apparatus and is also essential for colonization.
Structure
By looking the X-ray crystal structure of native TcpF, the structure of TcpF is consisted with an N-terminal domain (NTD;residues 1–185) and a C-terminal domain (CTD; residues 190–318) joined 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.
Function
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.
