Cytolysin

From Proteopedia

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spinqualitylabelsall models Cytolysin complex with N-acetyl-D-galactosamine and glycerol (PDB code 4owk). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Cytolysins are (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]. Structural highlights [10].

3D structures of Cytolysin

Updated on 29-May-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. ↑ 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