| 词条 | CFP-10 |
| 释义 |
| Name = 10 kDa culture filtrate antigen CFP-10 | image = CFP-10.jpg | width = | caption = Structure of the CFP10-ESAT6 complex from M. tuberculosis.[1] | Organism = Mycobacterium tuberculosis | TaxID = 83332 | Symbol = esxB | AltSymbols = | IUPHAR_id = | ATC_prefix = | ATC_suffix = | ATC_supplemental = | CAS_number = | CAS_supplemental = | DrugBank = | EntrezGene = 886194 | PDB = 3FAV | RefSeqmRNA = | RefSeqProtein = NP_218391 | UniProt = P0A566 | ECnumber = | Chromosome = genome | EntrezChromosome = NC_000962.2 | GenLoc_start = 4352228 | GenLoc_end = 4352620 }}CFP-10 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] Function10-kDa culture filtrate protein (CFP-10) is an antigen that contributes to the virulence 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 on each other for 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 core components of the whole ESX-1 secretion system include Rv3877, and two AAA ATPases, including Rv3870 and Rv3871, a cytosolic protein. 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. Rv3871 then interacts with the CFP-10 C-terminal, and escorts the ESAT-6/CFP-10 complex to Rv3870 and Rv3877, a multi-transmembrane protein which makes up the pore that spans the cytosolic membrane of the virulent host cell. Once ESAT-6/CFP-10 is next to the membrane of the virulent host cell, the CFP-10 C-terminal attaches and binds itself to the cells surface. The ESAT-6/CFP-10 complex’s secretion and attachment to the virulent host cell shows its contribution to the pathogenicity of Mycobacterium tuberculosis. [4]. StructureThe 10-kDa culture filtrate protein (CFP-10) and 6kDaA early secreted antigen target (ESAT-6) complex is a 100 amino-acid sequence protein. ESAT-6/CFP-10 has a hydrophobic nature as well as a high content of α-helical structures. Resonance structure analysis of the complex reveals two similar helix-turn-helix hairpin structures formed by the individual proteins, which lie anti-parallel to each other and forms a four-helix bundle. Its long flexible arm projecting off the four-helix bundle, formed by the seven amino-acid C-terminal of CFP-10, is essential for binding and attaching to the surface of host white blood cells; such as macrophages and monocytes. If this C-terminus is cleaved off, the complex shows greatly reduced attachment ability. See also
References1. ^{{PDB|1WA8}}; {{cite journal | vauthors = Renshaw PS, Lightbody KL, Veverka V, Muskett FW, Kelly G, Frenkiel TA, Gordon SV, Hewinson RG, Burke B, Norman J, Williamson RA, Carr MD | title = Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6 | journal = EMBO J. | volume = 24 | issue = 14 | pages = 2491–8 |date=July 2005 | pmid = 15973432 | pmc = 1176459 | doi = 10.1038/sj.emboj.7600732 }} 2. ^{{cite web|url=https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=886194&itool=EntrezSystem2.PEntrez.Gene.Gene_ResultsPanel.Gene_RVDocSum|title=Entrez gene}} 3. ^{{cite journal |vauthors=Meher AK, Bal NC, Chary KV, Arora A |title=Mycobacterium tuberculosis H37Rv ESAT-6-CFP-10 compleand biochemical stability |journal=FEBS J. |volume=273 |issue=7 |pages=1445–62 |date=Apr 2006 |pmid=16689931 |doi=10.1111/j.1742-4658.2006.05166.x }} Further reading{{refbegin}}
1 : Tuberculosis |
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