Bacillus cereus sphingomyelinase recognizes ganglioside GM3

Biochemical and Biophysical Research Communications

Volumn 431, Issue 2, 2013, Pages 164-168

  Oda, Masataka ^a   Fujita, Aoi ^a   Okui, Kensuke ^a   Miyamoto, Kazuaki ^a   Shibutani, Masahiro ^a   Takagishi, Teruhisa ^a   Nagahama, Masahiro ^a  

^a TOKUSHIMA BUNRI UNIVERSITY   (Japan)

Author keywords

Hairpin; Bacillus cereus; GM3; Sphingomyelinase; Tethering

Indexed keywords

GANGLIOSIDE GM3; LIPOSOME; SPHINGOMYELIN PHOSPHODIESTERASE;

AMINO ACID SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BACILLUS CEREUS; BINDING SITE; CONCENTRATION RESPONSE; CONTROLLED STUDY; ENZYME BINDING; MALE; MEMBRANE BINDING; MOUSE; NONHUMAN; PERITONEUM MACROPHAGE; PRIORITY JOURNAL; SURFACE PLASMON RESONANCE; WILD TYPE;

AMINO ACID SEQUENCE; ANIMALS; BACILLUS CEREUS; G(M3) GANGLIOSIDE; LIPOSOMES; MACROPHAGES; MICE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, SECONDARY; SPHINGOMYELIN PHOSPHODIESTERASE; SURFACE PLASMON RESONANCE;

BACILLUS CEREUS;

EID: 84873438808     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.01.002     Document Type: Article

References (31)

1. Schuchman E.H., Suchi M., Takahashi T., Sandhoff K., Desnick R.J. Human acid sphingomyelinase. Isolation, nucleotide sequence and expression of the full-length and alternatively spliced cDNAs. J. Biol. Chem. 1991, 266:8531-8539.
2. Duan R.D., Nyberg L., Nilsson A. Alkaline sphingomyelinase activity in rat gastrointestinal tract: distribution and characteristics. Biochim. Biophys. Acta 1995, 1259:49-55.
3. Tomiuk S., Hofmann K., Nix M., Zumbansen M., Stoffel W. Cloned mammalian neutral sphingomyelinase: functions in sphingolipid signaling?. Proc. Natl. Acad. Sci. USA 1998, 95:3638-3643.
4. 2+-dependent neutral sphingomyelinase. Proc. Natl. Acad. Sci. USA 2000, 97:5895-5900.
5. Geoffroy C., Raveneau J., Beretti J.L., Lecroisey A., Vazquez-Boland J.A., Alouf J.E., Berche P. Purification and characterization of an extracellular 29-kilodalton phospholipase C from Listeria monocytogenes. Infect. Immun. 1991, 59:2382-2388.
6. Titball R.W., Fearn A.M., Williamson E.D. Biochemical and immunological properties of the C-terminal domain of the alpha-toxin of Clostridium perfringens. FEMS Microbiol. Lett. 1993, 110:45-50.
7. Projan S.J., Kornblum J., Kreiswirth B., Moghazeh S.L., Eisner W., Novick R.P. Nucleotide sequence: the beta-hemolysin gene of Staphylococcus aureus. Nucleic Acids Res. 1989, 17:3305.
8. Huseby M., Shi K., Brown C.K., Digre J., Mengistu F., Seo K.S., Bohach G.A., Schlievert P.M., Ohlendorf D.H., Earhart C.A. Structure and biological activities of beta toxin from Staphylococcus aureus. J. Bacteriol. 2007, 189:8719-8726.
9. Yamada A., Tsukagoshi N., Udaka S., Sasaki T., Makino S., Nakamura S., Little C., Tomita M., Ikezawa H. Nucleotide sequence and expression in Escherichia coli of the gene coding for sphingomyelinase of Bacillus cereus. Eur. J. Biochem. 1988, 175:213-220.
10. Segers R.P., van der Drift A., de Nijs A., Corcione P., van der Zeijst B.A., Gaastra W. Molecular analysis of a sphingomyelinase C gene from Leptospira interrogans serovar hardjo. Infect. Immun. 1990, 58:2177-2185.
11. Gonzalez-Zorn B., Dominguez-Bernal G., Suarez M., Ripio M.T., Vega Y., Novella S., Vazquez-Boland J.A. The smcL gene of Listeria ivanovii encodes a sphingomyelinase C that mediates bacterial escape from the phagocytic vacuole. Mol. Microbiol. 1999, 33:510-523.
12. Openshaw A.E., Race P.R., Monzo H.J., Vazquez-Boland J.A., Banfield M.J. Crystal structure of SmcL, a bacterial neutral sphingomyelinase C from Listeria. J. Biol. Chem. 2005, 280:35011-35017.
13. Rodrigues-Lima F., Fensome A.C., Josephs M., Evans J., Veldman R.J., Katan M. Structural requirements for catalysis and membrane targeting of mammalian enzymes with neutral sphingomyelinase and lysophospholipid phospholipase C activities. Analysis by chemical modification and site-directed mutagenesis. J. Biol. Chem. 2000, 275:28316-28325.
14. Goni F.M., Alonso A. Sphingomyelinases: enzymology and membrane activity. FEBS Lett. 2002, 531:38-46.
15. Weston S.A., Lahm A., Suck D. X-ray structure of the DNase I-d(GGTATACC)2 complex at 2.3 A resolution. J. Mol. Biol. 1992, 226:1237-1256.
16. Oefner C., Suck D. Crystallographic refinement and structure of DNase I at 2 A resolution. J. Mol. Biol. 1986, 192:605-632.
17. Murzin A.G., Brenner S.E., Hubbard T., Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 1995, 247:536-540.
18. Ago H., Oda M., Takahashi M., Tsuge H., Ochi S., Katunuma N., Miyano M., Sakurai J. Structural basis of the sphingomyelin phosphodiesterase activity in neutral sphingomyelinase from Bacillus cereus. J. Biol. Chem. 2006, 281:16157-16167.
19. 2+ essential for catalytic activity. J. Biochem. 2003, 133:279-286.
20. Obama T., Fujii S., Ikezawa H., Ikeda K., Imagawa M., Tsukamoto K. His151 and His296 are the acid-base catalytic residues of Bacillus cereus sphingomyelinase in sphingomyelin hydrolysis. Biol. Pharm. Bull. 2003, 26:920-926.
21. Matsuo Y., Yamada A., Tsukamoto K., Tamura H., Ikezawa H., Nakamura H., Nishikawa K. A distant evolutionary relationship between bacterial sphingomyelinase and mammalian DNase I. Protein Sci. 1996, 5:2459-2467.
22. Oda M., Takahashi M., Tsuge H., Nagahama M., Sakurai J. Role of side-edge site of sphingomyelinase from Bacillus cereus. Biochem. Biophys. Res. Commun. 2012, 422:128-132.
23. Chai Q., Arndt J.W., Dong M., Tepp W.H., Johnson E.A., Chapman E.R., Stevens R.C. Structural basis of cell surface receptor recognition by botulinum neurotoxin B. Nature 2006, 444:1096-1100.
24. Tsukamoto K., Kozai Y., Ihara H., Kohda T., Mukamoto M., Tsuji T., Kozaki S. Identification of the receptor-binding sites in the carboxyl-terminal half of the heavy chain of botulinum neurotoxin types C and D. Microb. Pathog. 2008, 44:484-493.
25. Eidels L., Proia R.L., Hart D.A. Membrane receptors for bacterial toxins. Microbiol. Rev. 1983, 47:596-620.
26. Oda M., Kabura M., Takagishi T., Suzue A., Tominaga K., Urano S., Nagahama M., Kobayashi K., Furukawa K., Sakurai J. Clostridium perfringens alpha-toxin recognizes the GM1a-TrkA complex. J. Biol. Chem. 2012, 287:33070-33079.
27. Oda M., Hashimoto M., Takahashi M., Ohmae Y., Seike S., Kato R., Fujita A., Tsuge H., Nagahama M., Ochi S., Sasahara T., Hayashi S., Hirai Y., Sakurai J. Role of sphingomyelinase in infectious diseases caused by Bacillus cereus. PLoS One 2012, 7:e38054.
28. Finnegan C.M., Rawat S.S., Puri A., Wang J.M., Ruscetti F.W., Blumenthal R. Ceramide, a target for antiretroviral therapy. Proc. Natl. Acad. Sci. USA 2004, 101:15452-15457.
29. Coll O., Morales A., Fernandez-Checa J.C., Garcia-Ruiz C. Neutral sphingomyelinase-induced ceramide triggers germinal vesicle breakdown and oxidant-dependent apoptosis in Xenopus laevis oocytes. J. Lipid Res. 2007, 48:1924-1935.
30. Finnegan C.M., Rawat S.S., Cho E.H., Guiffre D.L., Lockett S., Merrill A.H., Blumenthal R. Sphingomyelinase restricts the lateral diffusion of CD4 and inhibits human immunodeficiency virus fusion. J. Virol. 2007, 81:5294-5304.
31. Notredame C., Higgins D.G., Heringa J. T-Coffee: a novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 2000, 302:205-217.