Purification and characterization of Ophiophagus hannah cytotoxin-like proteins

Toxicon

Volumn 48, Issue 4, 2006, Pages 429-436

  Chang, Long Sen ^a   Chen, Ku Chung ^a   Lin, Shinne Ren ^b   Huang, Hsien Bin ^c  

^a NATIONAL SUN YAT SEN UNIVERSITY   (Taiwan)

^b KAOHSIUNG MEDICAL UNIVERSITY   (Taiwan)

^c NATIONAL CHUNG CHENG UNIVERSITY   (Taiwan)

Author keywords

Cytotoxin like proteins; Functional residues; Lytic activity; Ophiophagus hannah; Primary structure

Indexed keywords

AMINO ACID; CARDIOTOXIN; CYTOTOXIN; PROTEIN; SNAKE VENOM;

AMINO ACID SEQUENCE; APOPTOSIS; ARTICLE; CELL DEATH; CELL VIABILITY; CIRCULAR DICHROISM; CYTOLYSIS; HUMAN; HUMAN CELL; ION EXCHANGE CHROMATOGRAPHY; NONHUMAN; NUCLEOTIDE SEQUENCE; OPHIOPHAGUS HANNAH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SNAKE; TOXIN ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CELL SURVIVAL; CIRCULAR DICHROISM; COBRA VENOMS; CYTOTOXINS; DIRECT LYTIC FACTORS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEINS;

NAJA ATRA; OPHIOPHAGUS HANNAH;

EID: 33747756552     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2006.06.012     Document Type: Article

References (30)

1. Bhaskaran R., Huang C.C., Chang D.K., and Yu C. Cardiotoxin III from Taiwan cobra (Naja naja atra). Determination of structure in solution and comparison with short neurotoxins. J. Mol. Biol. 235 (1994) 1291-1301
2. Chang L.S., Lin J., and Wu P.F. cDNA sequence analysis and expression of cardiotoxin V and a new cardiotoxin VII from Naja naja atra (Taiwan cobra). Biochim. Biophys. Acta 1295 (1996) 1-4
3. Chang L.S., Huang H.B., and Lin S.R. The multiplicity of cardiotoxins from Naja naja atra (Taiwan cobra) venom. Toxicon 38 (2000) 1065-1076
4. Chang L.S., Liou J.C., Lin S.R., and Huang H.B. Purification and characterization of a neurotoxin from the venom of Ophiophagus hannah (King cobra). Biochem. Biophys. Res. Commun. 294 (2002) 574-578
5. Chang L.S., Lin S.K., and Chung C. Molecular cloning and evolution of the genes encoding the precursors of Taiwan cobra cardiotoxin and cardiotoxin-like basic protein. Biochem. Genet. 42 (2004) 429-439
6. Chen T.S., Chung F.Y., Tjong S.C., Goh K.S., Huang W.N., Chien K.Y., Wu P.L., Lin H.C., Chen C.J., and Wu W.G. Structural difference between group I and group II cobra cardiotoxins: X-ray, NMR, and CD analysis of the effect of cis-proline conformation on three-fingered toxins. Biochemistry 44 (2005) 7414-7426
7. Chien K.Y., Huang W.N., Jean J.H., and Wu W.G. Fusion of sphingomyelin vesicles induced by proteins from Taiwan cobra (Naja naja atra) venom. Interaction of zwitterionic phospholipids with cardiotoxin analogues. J. Biol. Chem. 266 (1991) 3252-3259
8. 2 from king cobra (Ophiophagus hannah) venom. J. Protein Chem. 14 (1995) 451-456
9. Erdreich-Epstein A., Shimada H., Groshen S., Liu M., Metelitsa L.S., Kim K.S., Stins M.F., Seeger R.C., and Durden D.L. Integrins αvβ3 and αvβ5 are expressed by endothelium of high-risk neuroblastoma and their inhibition is associated with increased endogenous ceramide. Cancer Res. 60 (2000) 712-721
10. Erdreich-Epsteins A., Tran L.B., Cox O.T., Huang E.Y., Laug W.E., Shimada H., and Millard M. Endothelial apoptosis induced by inhibition of integrins αvβ3 and αvβ5 involves ceramide metabolic pathway. Blood 105 (2005) 4353-4361
11. Forouhar F., Huang W.N., Liu J.H., Chien K.Y., Wu W.G., and Hsiao C.D. Structural basis of membrane-induced cardiotoxins A3 oligomerization. J. Biol. Chem. 278 (2003) 21980-21988
12. Gatineau E., Toma F., Montenay-Garestier T., Takechu M., Fromageot P., and Menez A. Role of tyrosine and tryptophan residues in the structure-activity relationship of a cardiotoxin from Naja nigricollis venom. Biochemistry 26 (1987) 8046-8055
13. 2 from Ophiophagus hannah snake venom. Life Sci. 61 (1997) 2211-2217
14. Kozlova N., Morozevich G.E., Chubukina A., and Berman A.E. Integrin αvβ3 promotes anchorage-dependent apoptosis in human intestinal carcinoma cells. Oncogene 20 (2001) 4710-4717
15. Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105-132
16. Lee C.S., Kumar T.K.S., Lian L.Y., Chang J.W., and Yu C. Main-chain dynamics of cardiotoxin II from Taiwan cobra (Naja naja atra) as studied by carbon-13 NMR at neutral abundance: delineation of the role of functionally important residues. Biochemistry 37 (1998) 155-164
17. Lin S.R., Chang K.L., and Chang C.C. Chemical modification of amino groups in cardiotoxin III from Taiwan cobra (Naja naja atra) venom. Biochem. Mol. Biol. Int. 31 (1993) 175-184
18. Lin S.R., Chi S.H., Chang L.S., Kuo K.W., and Chang C.C. Chemical modification of cationic groups of a novel α-neurotoxin (Oh-4) from king cobra (Ophiophagus hannah) venom. J. Biochem. 118 (1995) 297-301
19. Lin S.R., Chang L.S., and Chang K.L. Separation and structure-function studies of Taiwan cobra cardiotoxins. J. Protein Chem. 21 (2002) 81-86
20. Menez A., Gatineau F., Roumestand C., Harvey A.L., Mouaward L., Gilquin B., and Toma F. Do cardiotoxins possess a functional site? Structural and chemical modification studies reveal the functional site of the cardiotoxin from Naja nigricollis. Biochimie 72 (1990) 575-588
21. Mesner Jr. P.W., and Kaufmann S.H. The role of proteases in neuronal apoptosis. In: Hannun Y.A., and Boustany R.M. (Eds). Apoptosis in Neurobiology (1999), CRC Press, New York 73-104
22. Sivaraman T., Kumar T.K.S., Yamg P.W., and Yu C. Cardiotoxin-like basic protein (CLBP) from Naja naja atra is not a cardiotoxin. Toxicon 35 (1997) 1367-1371
23. Stevens-Truss R., and Hinman C.L. Chemical modification of methionines in a cobra venom cytotoxin differentiates between lytic and binding domains. Toxicol. Appl. Pharmacol. 139 (1996) 234-242
24. Sun Y.J., Wu W.G., Chiang C.M., Hsin A.Y., and Hsiao C.D. Crystal structure of cardiotoxin V from Taiwan cobra venom: pH-dependent conformational change and a novel membrane-binding motif identified in the three-finger loops of P-type cardiotoxins. Biochemistry 36 (1997) 2403-2413
25. Wang C.H., and Wu W.G. Amphiphilic β-sheet cobra cardiotoxin targets mitochondria and disrupts its network. FEBS Lett. 579 (2005) 3169-3174
26. Wang C.H., Monette R., Lee S.C., Morley P., and Wu W.G. Cobra cardiotoxin-induced cell death in fetal rat cardiomyocytes and cortical neurons: different pathway but similar cell surface target. Toxicon 46 (2005) 430-440
27. Wang C.H., Liu J.H., Lee S.C., Hsiao C.D., and Wu W.G. Glycosphingolipid- facilitated membrane insertion and internalization of cobra cardiotoxin. The sulfatide-cardiotoxin complex structure in a membrane-like environment suggests a lipid-dependent cell-penetrating mechanism for membrane binding polypeptides. J. Biol. Chem. 281 (2006) 656-667
28. Wu P.L., Lee S.C., Chuang C.C., Mori S., Akakura N., Wu W.G., and Takada Y. O1_MRKO1_MRKNon-cytotoxic cobra cardiotoxin A5 binds to integrin αvβ3 and inhibits bone resorption: identification of cardiotoxins as non-RGD integrin-binding proteins of the Ly-6 family. J. Biol. Chem. 281 (2006) 7937-7945
29. 2 from Ophiophagus hannah with the "pancreatic loop". J. Struct. Biol. 138 (2002) 207-215
30. Zhou X., Murphy F.R., Gehdu N., Zhang J., Iredale J.P., and Benyon R.C. Engagement of αvβ3 integrin regulates proliferation and apoptosis of hepatic stellate cells. J. Biol. Chem. 279 (2004) 23996-24006