Cytolysin

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*'''Perfringolysin O''' is a pore-forming, cholesterol-dependent cytolysin secreted by ''Clostridium perfringens''<ref>PMID:16701509</ref>.<br />
*'''Perfringolysin O''' is a pore-forming, cholesterol-dependent cytolysin secreted by ''Clostridium perfringens''<ref>PMID:16701509</ref>.<br />
*'''Pneumolysin''' is a virulence factor which augments intrapulmonary growth and dissemination during the early infection ''Streptococcus pneumonia''<ref>PMID:9452123</ref>.<br />
*'''Pneumolysin''' is a virulence factor which augments intrapulmonary growth and dissemination during the early infection ''Streptococcus pneumonia''<ref>PMID:9452123</ref>.<br />
 +
*'''Sticholysin''' is a pore-forming toxin secreted by sea anemone<ref>PMID:19268489</ref>.<br />
 +
*'''Stonustoxin''' is a lethal factor secreted by stonefish<ref>PMID:9271089</ref>.<br />
 +
*'''Streptolysin O''' is a thin-activated membrane-damaging protein which is produced by β-hemolytic group A streptococci<ref>PMID:3880730</ref>.<br />
 +
== Relevance ==
 +
 +
Steptolysin O has the potential to establish a new class of suicide gene therapeutic reagents<ref>PMID:16818521</ref> as well as reversibly permeabilize adherent and non-adherent cells allowing the delivery of molecules with up to 100 kDa mass to the cytosol<ref>PMID:11248053</ref>.
== Structural highlights ==
== Structural highlights ==
<scene name='46/462210/Cv/3'>Cytolysin β-trefoil lectin binds a disaccharide</scene><ref>PMID:24862282</ref>.
<scene name='46/462210/Cv/3'>Cytolysin β-trefoil lectin binds a disaccharide</scene><ref>PMID:24862282</ref>.
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 +
==3D structures of Cytolysin==
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[[Cytolysin 3D structures]]
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</StructureSection>
</StructureSection>
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* Equinatoxin II
* Equinatoxin II
-
**[[1kd6]] – Equx – ''Actinia equina'' - NMR<br />
+
**[[1iaz]] – AeEqux – ''Actinia equina'' <br />
 +
**[[1kd6]] – AeEqux - NMR<br />
 +
**[[1tzq]] – AeEqux (mutant)<br />
* Fragaceatoxin C
* Fragaceatoxin C
-
**[[3w9p]] – FraC – strawberry anemone<br />
+
**[[3w9p]], [[5bpg]], [[4tsy]], [[4tsq]], [[4tsp]], [[4tso]], [[4tsn]], [[4tsl]], [[3zwj]], [[3zwg]], [[3vwi]], [[3lim]] – saFraC – strawberry anemone<br />
 +
**[[4wdc]] – saFraC (mutant)<br />
* Hemolysin see [[Hemolysin]]
* Hemolysin see [[Hemolysin]]
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* Intermedilysin
* Intermedilysin
-
**[[5imt]] – IntL – ''Streptococcus intermedius''<br />
+
**[[5imt]], [[5imw]], [[1s3r]] – SiIntL – ''Streptococcus intermedicus''<br />
 +
**[[4bik]] – SiIntL + CD59<br />
* Listeriolysin O
* Listeriolysin O
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* Lysenin
* Lysenin
-
**[[5ec5]] – Lys – red wiggler worm<br />
+
**[[5ec5]] – rwwLys – red wiggler worm<br />
 +
**[[5gaq]] – rwwLys – Cryo EM<br />
 +
**[[3zxd]] – cbwLys – common brandling worm<br />
 +
**[[3zx7]] – cbwLys + phosphocholine <br />
 +
**[[3zxg]] – cbwLys + sphingomyelin <br />
* Perforin-1
* Perforin-1
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**[[4y1s]], [[4y1t]] – mPrf1 C2 domain – mouse<br />
**[[4y1s]], [[4y1t]] – mPrf1 C2 domain – mouse<br />
**[[3nsj]] – mPrf1 (mutant)<br />
**[[3nsj]] – mPrf1 (mutant)<br />
 +
**[[5ug6]], [[5ug7]] – mPrf1 C2 domain (mutant)<br />
* Perfringolysin O
* Perfringolysin O
**[[5dhl]], [[5dim]] – CpPerL (mutant) – ''Clostridium perfringens''<br />
**[[5dhl]], [[5dim]] – CpPerL (mutant) – ''Clostridium perfringens''<br />
-
**[[1pfo]] – CpPerL <br />
+
**[[1pfo]], [[1m3i]], [[1m3j]] – CpPerL <br />
* Pneumolysin
* Pneumolysin
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**[[5cr8]] – SpPneL membrane-binding domain<br />
**[[5cr8]] – SpPneL membrane-binding domain<br />
**[[4qqq]] – SpPneL + mannose<br />
**[[4qqq]] – SpPneL + mannose<br />
-
**[[2bk1]], [[2bk2]] – SpPneL - CryoEM<br />
+
**[[2bk1]], [[2bk2]], [[5ly6]] – SpPneL - CryoEM<br />
* Sticholysin
* Sticholysin

Revision as of 08:26, 2 June 2019

Cytolysin complex with N-acetyl-D-galactosamine and glycerol (PDB code 4owk).

Drag the structure with the mouse to rotate

3D structures of Cytolysin

Updated on 02-June-2019

References

  1. ↑ Kaus K, Lary JW, Cole JL, Olson R. Glycan Specificity of the Vibrio vulnificus Hemolysin Lectin Outlines Evolutionary History of Membrane Targeting by a Toxin Family. J Mol Biol. 2014 Jul 29;426(15):2800-12. doi: 10.1016/j.jmb.2014.05.021. Epub, 2014 May 24. PMID:24862282 doi:http://dx.doi.org/10.1016/j.jmb.2014.05.021
  2. ↑ Rojko N, Kristan KC, Viero G, Zerovnik E, Macek P, Dalla Serra M, Anderluh G. Membrane damage by an alpha-helical pore-forming protein, Equinatoxin II, proceeds through a succession of ordered steps. J Biol Chem. 2013 Aug 16;288(33):23704-15. doi: 10.1074/jbc.M113.481572. Epub, 2013 Jun 26. PMID:23803608 doi:http://dx.doi.org/10.1074/jbc.M113.481572
  3. ↑ Bellomio A, Morante K, Barlic A, Gutierrez-Aguirre I, Viguera AR, Gonzalez-Manas JM. Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea. Toxicon. 2009 Nov;54(6):869-80. doi: 10.1016/j.toxicon.2009.06.022. Epub 2009 Jun, 27. PMID:19563820 doi:10.1016/j.toxicon.2009.06.022
  4. ↑ Nagamune H, Ohnishi C, Katsuura A, Fushitani K, Whiley RA, Tsuji A, Matsuda Y. Intermedilysin, a novel cytotoxin specific for human cells secreted by Streptococcus intermedius UNS46 isolated from a human liver abscess. Infect Immun. 1996 Aug;64(8):3093-100. PMID:8757839
  5. ↑ Schnupf P, Portnoy DA. Listeriolysin O: a phagosome-specific lysin. Microbes Infect. 2007 Aug;9(10):1176-87. doi: 10.1016/j.micinf.2007.05.005. Epub , 2007 May 7. PMID:17720603 doi:http://dx.doi.org/10.1016/j.micinf.2007.05.005
  6. ↑ Bokori-Brown M, Martin TG, Naylor CE, Basak AK, Titball RW, Savva CG. Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein. Nat Commun. 2016 Apr 6;7:11293. doi: 10.1038/ncomms11293. PMID:27048994 doi:http://dx.doi.org/10.1038/ncomms11293
  7. ↑ Liu CC, Walsh CM, Young JD. Perforin: structure and function. Immunol Today. 1995 Apr;16(4):194-201. PMID:7734048
  8. ↑ Ohno-Iwashita Y, Shimada Y, Waheed AA, Hayashi M, Inomata M, Nakamura M, Maruya M, Iwashita S. Perfringolysin O, a cholesterol-binding cytolysin, as a probe for lipid rafts. Anaerobe. 2004 Apr;10(2):125-34. doi: 10.1016/j.anaerobe.2003.09.003. PMID:16701509 doi:http://dx.doi.org/10.1016/j.anaerobe.2003.09.003
  9. ↑ Rubins JB, Janoff EN. Pneumolysin: a multifunctional pneumococcal virulence factor. J Lab Clin Med. 1998 Jan;131(1):21-7. PMID:9452123
  10. ↑ Alvarez C, Mancheno JM, Martinez D, Tejuca M, Pazos F, Lanio ME. Sticholysins, two pore-forming toxins produced by the Caribbean Sea anemone Stichodactyla helianthus: their interaction with membranes. Toxicon. 2009 Dec 15;54(8):1135-47. doi: 10.1016/j.toxicon.2009.02.022. Epub 2009, Mar 4. PMID:19268489 doi:http://dx.doi.org/10.1016/j.toxicon.2009.02.022
  11. ↑ Chen D, Kini RM, Yuen R, Khoo HE. Haemolytic activity of stonustoxin from stonefish (Synanceja horrida) venom: pore formation and the role of cationic amino acid residues. Biochem J. 1997 Aug 1;325 ( Pt 3):685-91. PMID:9271089
  12. ↑ Bhakdi S, Tranum-Jensen J, Sziegoleit A. Mechanism of membrane damage by streptolysin-O. Infect Immun. 1985 Jan;47(1):52-60. PMID:3880730
  13. ↑ Yang WS, Park SO, Yoon AR, Yoo JY, Kim MK, Yun CO, Kim CW. Suicide cancer gene therapy using pore-forming toxin, streptolysin O. Mol Cancer Ther. 2006 Jun;5(6):1610-9. doi: 10.1158/1535-7163.MCT-05-0515. PMID:16818521 doi:http://dx.doi.org/10.1158/1535-7163.MCT-05-0515
  14. ↑ Walev I, Bhakdi SC, Hofmann F, Djonder N, Valeva A, Aktories K, Bhakdi S. Delivery of proteins into living cells by reversible membrane permeabilization with streptolysin-O. Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):3185-90. doi: 10.1073/pnas.051429498., Epub 2001 Mar 6. PMID:11248053 doi:http://dx.doi.org/10.1073/pnas.051429498
  15. ↑ Kaus K, Lary JW, Cole JL, Olson R. Glycan Specificity of the Vibrio vulnificus Hemolysin Lectin Outlines Evolutionary History of Membrane Targeting by a Toxin Family. J Mol Biol. 2014 Jul 29;426(15):2800-12. doi: 10.1016/j.jmb.2014.05.021. Epub, 2014 May 24. PMID:24862282 doi:http://dx.doi.org/10.1016/j.jmb.2014.05.021

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