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Function
Cytolysins are β-barrel (Alpha Helices, Beta Strands , Loops , Turns) pore-forming toxins secreted by a variety of organisms and causing cell lysis.
- Anthrolysin O is a pore-forming, cholesterol-dependent cytolysin secreted by Bacillus anthracis[1].
- Equinatoxin is an α-helical pore-forming toxin that pirate cellular membranes by the use of α-helices [2].
- Fragaceaatoxin is a sea anemone toxin [3].
- Intermedilysin is human-specific toxin found in liver abscesses [4].
- Listerolysin O is a pore-forming, cholesterol-dependent cytolysis secreted by Listeria monocytogenes[5].
- Lysenin is small β-pore-forming toxin secreted by an earthworm[6].
- Perforin is produced by killer lymphocytes and released by cytoplasmic granules[7].
- Perfringolysin O is a pore-forming, cholesterol-dependent cytolysin secreted by Clostridium perfringens[8].
- Pneumolysin is a virulence factor which augments intrapulmonary growth and dissemination during the early infection Streptococcus pneumonia[9].
- Sticholysin is a pore-forming toxin secreted by sea anemone[10].
- Stonustoxin is a lethal factor secreted by stonefish[11].
- Streptolysin O is a thin-activated membrane-damaging protein which is produced by β-hemolytic group A streptococci[12].
See also Cytolysin A.
Relevance
Steptolysin O has the potential to establish a new class of suicide gene therapeutic reagents[13] as well as reversibly permeabilize adherent and non-adherent cells allowing the delivery of molecules with up to 100 kDa mass to the cytosol[14].
Structural highlights
Cytolysin β-trefoil lectin binds a disaccharide[15].
3D structures of Cytolysin
Cytolysin 3D structures
- ↑ 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:https://dx.doi.org/10.1016/j.jmb.2014.05.021
- ↑ 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:https://dx.doi.org/10.1074/jbc.M113.481572
- ↑ 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
- ↑ 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
- ↑ 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:https://dx.doi.org/10.1016/j.micinf.2007.05.005
- ↑ 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:https://dx.doi.org/10.1038/ncomms11293
- ↑ Liu CC, Walsh CM, Young JD. Perforin: structure and function. Immunol Today. 1995 Apr;16(4):194-201. PMID:7734048
- ↑ 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:https://dx.doi.org/10.1016/j.anaerobe.2003.09.003
- ↑ Rubins JB, Janoff EN. Pneumolysin: a multifunctional pneumococcal virulence factor. J Lab Clin Med. 1998 Jan;131(1):21-7. PMID:9452123
- ↑ 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:https://dx.doi.org/10.1016/j.toxicon.2009.02.022
- ↑ 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
- ↑ Bhakdi S, Tranum-Jensen J, Sziegoleit A. Mechanism of membrane damage by streptolysin-O. Infect Immun. 1985 Jan;47(1):52-60. PMID:3880730
- ↑ 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:https://dx.doi.org/10.1158/1535-7163.MCT-05-0515
- ↑ 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:https://dx.doi.org/10.1073/pnas.051429498
- ↑ 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:https://dx.doi.org/10.1016/j.jmb.2014.05.021
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