3zxd

Structural highlights

Function

[TXL_EISFO] Pore-forming toxin that specifically binds sphingomyelin in the plasma membrane of various cells. Has hemolytic activity. Is also cytotoxic to spermatozoa of some species of invertebrates and many species of vertebrates and to amphibian larvae, guinea pig polymorphonuclear leukocytes, chicken fibroblasts, normal spleen cells and various tumor cells. Is lethal for various species of reptiles, amphibian, birds and mammals. Induces smooth muscle contraction. It binds sphingomyelin and induces hemolysis in the same manner as lysenin-related protein 2, and is 10 times more effective than lysenin-related protein 1.^{[1] [2] [3] [4] [5] [6]}

See Also

• Cytolysin 3D structures

References

1. ↑ Kobayashi H, Sekizawa Y, Aizu M, Umeda M. Lethal and non-lethal responses of spermatozoa from a wide variety of vertebrates and invertebrates to lysenin, a protein from the coelomic fluid of the earthworm Eisenia foetida. J Exp Zool. 2000 Apr 1;286(5):538-49. PMID:10684578
2. ↑ Yamaji-Hasegawa A, Makino A, Baba T, Senoh Y, Kimura-Suda H, Sato SB, Terada N, Ohno S, Kiyokawa E, Umeda M, Kobayashi T. Oligomerization and pore formation of a sphingomyelin-specific toxin, lysenin. J Biol Chem. 2003 Jun 20;278(25):22762-70. Epub 2003 Apr 3. PMID:12676961 doi:http://dx.doi.org/10.1074/jbc.M213209200
3. ↑ Kiyokawa E, Makino A, Ishii K, Otsuka N, Yamaji-Hasegawa A, Kobayashi T. Recognition of sphingomyelin by lysenin and lysenin-related proteins. Biochemistry. 2004 Aug 3;43(30):9766-73. PMID:15274631 doi:http://dx.doi.org/10.1021/bi049561j
4. ↑ Kobayashi H, Suzuki H, Ohta N. Exfoliation of the epidermal cells and defecation by amphibian larvae in response to coelomic fluid and lysenin from the earthworm Eisenia foetida. Biomed Res. 2006 Aug;27(4):169-81. PMID:16971770
5. ↑ Sekizawa Y, Kubo T, Kobayashi H, Nakajima T, Natori S. Molecular cloning of cDNA for lysenin, a novel protein in the earthworm Eisenia foetida that causes contraction of rat vascular smooth muscle. Gene. 1997 May 20;191(1):97-102. PMID:9210594
6. ↑ Yamaji A, Sekizawa Y, Emoto K, Sakuraba H, Inoue K, Kobayashi H, Umeda M. Lysenin, a novel sphingomyelin-specific binding protein. J Biol Chem. 1998 Feb 27;273(9):5300-6. PMID:9478988
7. ↑ De Colibus L, Sonnen AF, Morris KJ, Siebert CA, Abrusci P, Plitzko J, Hodnik V, Leippe M, Volpi E, Anderluh G, Gilbert RJ. Structures of lysenin reveal a shared evolutionary origin for pore-forming proteins and its mode of sphingomyelin recognition. Structure. 2012 Sep 5;20(9):1498-507. Epub 2012 Jul 19. PMID:22819216 doi:http://dx.doi.org/10.1016/j.str.2012.06.011