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CFP-10
View on Wikipedia | This article needs additional citations for verification. (October 2025) |
| 10 kDa culture filtrate antigen CFP-10 | |||||||
|---|---|---|---|---|---|---|---|
 Structure of the CFP10-ESAT6 complex from M. tuberculosis.[1] | |||||||
| Identifiers | |||||||
| Organism | |||||||
| Symbol | esxB | ||||||
| Entrez | 886194 | ||||||
| PDB | 3FAV | ||||||
| RefSeq (Prot) | NP_218391 | ||||||
| UniProt | P0A566 | ||||||
| Other data | |||||||
| Chromosome | genome: 4.35 - 4.35 Mb | ||||||
| |||||||
CFP-10 within bacterial proteins (also known as ESAT-6-like protein esxB or secreted antigenic protein MTSA-10 or 10 kDa culture filtrate antigen CFP-10) is a protein that is encoded by the esxB gene.[2]
CFP-10 is a 10 kDa secreted antigen from Mycobacterium tuberculosis. It forms a 1:1 heterodimeric complex with ESAT-6. Both genes are expressed from the RD1 region of the bacterial genome and play a key role in the virulence of the infection.[3]
Function
[edit]10-kDa culture filtrate protein (CFP-10) is an antigen that contributes to the virulence of Mycobacterium tuberculosis. CFP-10 forms a tight 1:1 heterodimeric complex with 6kDaA early secreted antigen target (ESAT-6). In the mycobacterial cell, these two proteins are interdependent for their stability. The ESAT-6/CFP-10 complex is secreted by the ESX-1 secretion system, also known as the RD1 region. Mycobacterium tuberculosis uses this ESX-1 secretion system to deliver virulence factors into host macrophage and monocyte white blood cells during infection.
In Mycobacterium tuberculosis, the ESX-1 secretion system, a type VII bacterial secretion system, includes Rv3877 and two AAA ATPases, Rv3870 and Rv3871, the latter a cytosolic protein,[4] as subunits. The ESAT-6/CFP-10 heterodimer complex is targeted for secretion by a C-terminal signal sequence on CFP-10 that is recognized by the cytosolic Rv3871 protein.[4] Rv3871 then interacts with the CFP-10 C-terminal, and escorts the ESAT-6/CFP-10 complex to Rv3870 and Rv3877,[citation needed] a multi-transmembrane protein which may make up a pore that spans the inner membrane of the bacterium.[5] Once ESAT-6/CFP-10 is next to the membrane of the host cell, the CFP-10 C-terminal attaches and binds itself to the cell surface.[citation needed] The ESAT-6/CFP-10 complex’s secretion and attachment to the host cell shows its contribution to the pathogenicity of Mycobacterium tuberculosis.[citation needed]
Structure
[edit]![[icon]](https://en.wikipedia.org/wiki/File:Wiki_letter_w_cropped.svg){kind=small} | This section is empty. You can help by adding to it. (July 2024) |
See also
[edit]References
[edit]- ^ PDB: 1WA8; Renshaw PS, Lightbody KL, Veverka V, Muskett FW, Kelly G, Frenkiel TA, Gordon SV, Hewinson RG, Burke B, Norman J, Williamson RA, Carr MD (July 2005). "Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6". The EMBO Journal. 24 (14): 2491–8. doi:10.1038/sj.emboj.7600732. PMC 1176459. PMID 15973432.
- ^ "esxB ESAT-6-like protein EsxB [ Mycobacterium tuberculosis H37Rv ]". Entrez gene. National Library of Medicine National Center for Biotechnology Information. Retrieved 15 October 2025.
- ^ Meher AK, Bal NC, Chary KV, Arora A (Apr 2006). "Mycobacterium tuberculosis H37Rv ESAT-6–CFP-10 complex formation confers thermodynamic and biochemical stability". The FEBS Journal. 273 (7): 1445–62. doi:10.1111/j.1742-4658.2006.05166.x. PMID 16689931.
- ^ a b Digiuseppe Champion PA, Champion MM, Manzanillo P, Cox JS (2009). "ESX-1 Secreted Virulence Factors Are Recognized by Multiple Cytosolic AAA ATPases in Pathogenic Mycobacteria". Molecular Microbiology. 73 (5): 950–62. doi:10.1111/j.1365-2958.2009.06821.x. PMC 3023814. PMID 19682254.
- ^ Lalani S (2009). Characterization of the ESX-1 (SNM) secretion system in Mycobacteria (Master of Science thesis). The University of British Columbia. doi:10.14288/1.0067093. hdl:2429/6904.
Further reading
[edit]- DiGiuseppe Champion PA, Champion MM, Manzanillo P, Cox JS (September 2009). "ESX-1 secreted virulence factors are recognized by multiple cytosolic AAA ATPases in pathogenic mycobacteria". Mol. Microbiol. 73 (5): 950–62. doi:10.1111/j.1365-2958.2009.06821.x. PMC 3023814. PMID 19682254.