메뉴 건너뛰기




Volumn 315, Issue 1-2, 2003, Pages 95-102

Novel sequences encoding venom C-type lectins are conserved in phylogenetically and geographically distinct Echis and Bitis viper species

Author keywords

Bitis arietans; C type lectins; Echis carinatus sochureki; Echis ocellatus; Echis pyramidum leakeyi; Sequence conservation

Indexed keywords

LECTIN; NEUTRALIZING ANTIBODY;

EID: 0141594743     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(03)00716-9     Document Type: Article
Times cited : (30)

References (35)
  • 1
    • 0029816492 scopus 로고    scopus 로고
    • Binding of a novel 50 kDa alboaggregin from Trimeresurus albolabris and related viper venom proteins to the platelet membrane glycoprotein Ib-IX-V complex. Effect on platelet aggregation and glycoprotein Ib-mediated platelet aggregation
    • Andrews R.K., Kroll M.H., Ward C.M., Rose J.W., Scarborough R.M., Smith A.I., Lopez J.A., Berndt M.C. Binding of a novel 50 kDa alboaggregin from Trimeresurus albolabris and related viper venom proteins to the platelet membrane glycoprotein Ib-IX-V complex. Effect on platelet aggregation and glycoprotein Ib-mediated platelet aggregation. Biochemistry. 35:1996;12629-12639.
    • (1996) Biochemistry , vol.35 , pp. 12629-12639
    • Andrews, R.K.1    Kroll, M.H.2    Ward, C.M.3    Rose, J.W.4    Scarborough, R.M.5    Smith, A.I.6    Lopez, J.A.7    Berndt, M.C.8
  • 2
    • 0037032426 scopus 로고    scopus 로고
    • Calcium-binding analysis and molecular modelling reveals echis coagulation factor IX/factor X-binding protein has Ca-binding properties and Ca ion-independent folding of other C-type lectin-like proteins
    • Atoda H., Kaneko H., Mizuno H., Morita T. Calcium-binding analysis and molecular modelling reveals echis coagulation factor IX/factor X-binding protein has Ca-binding properties and Ca ion-independent folding of other C-type lectin-like proteins. FEBS Lett. 531:2002;229-234.
    • (2002) FEBS Lett. , vol.531 , pp. 229-234
    • Atoda, H.1    Kaneko, H.2    Mizuno, H.3    Morita, T.4
  • 4
    • 0028146808 scopus 로고
    • Haemorrhagic metalloproteinases from snake venoms
    • Bjarnason J.B., Fox J.W. Haemorrhagic metalloproteinases from snake venoms. Pharmacol. Ther. 62:1994;345-368.
    • (1994) Pharmacol. Ther. , vol.62 , pp. 345-368
    • Bjarnason, J.B.1    Fox, J.W.2
  • 5
    • 0029913241 scopus 로고    scopus 로고
    • Functional and sequence characterization of coagulation factor IX/factor X binding protein from the venom of Echis leucogaster
    • Chen Y.-H., Tsai I.-H. Functional and sequence characterization of coagulation factor IX/factor X binding protein from the venom of Echis leucogaster. Biochemistry. 35:1996;5264-5271.
    • (1996) Biochemistry , vol.35 , pp. 5264-5271
    • Chen, Y.-H.1    Tsai, I.-H.2
  • 6
    • 0013118110 scopus 로고    scopus 로고
    • The treatment of snake bites: Analysis of requirements and assessment of therapeutic efficacy in tropical Africa
    • A. Menez. Chichester: Wiley
    • Chippaux J.-P. The treatment of snake bites: analysis of requirements and assessment of therapeutic efficacy in tropical Africa. Menez A. Perspectives in Molecular Toxinology. 2002;457-472 Wiley, Chichester.
    • (2002) Perspectives in Molecular Toxinology , pp. 457-472
    • Chippaux, J.-P.1
  • 7
    • 0033527341 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of Aggretin, a collagen-like platelet aggregator
    • Chung C.-H., Au L.-C., Huang T.-F. Molecular cloning and sequence analysis of Aggretin, a collagen-like platelet aggregator. Biochem. Biophys. Res. Commun. 263:1999;723-727.
    • (1999) Biochem. Biophys. Res. Commun. , vol.263 , pp. 723-727
    • Chung, C.-H.1    Au, L.-C.2    Huang, T.-F.3
  • 9
    • 0023710284 scopus 로고
    • Two distinct classes of carbohydrate-recognition domains in animal lectins
    • Drickamer K. Two distinct classes of carbohydrate-recognition domains in animal lectins. J. Biol. Chem. 263(20):1988;9557-9560.
    • (1988) J. Biol. Chem. , vol.263 , Issue.20 , pp. 9557-9560
    • Drickamer, K.1
  • 10
    • 0030568869 scopus 로고    scopus 로고
    • Purification and characterization of bitiscetin, a novel von Willebrand factor modulator protein from Bitis arietans venom
    • Hamako J., Matsui T., Suzuki M., Ito M., Makita K., Fujimura Y., Ozeki Y., Titani K. Purification and characterization of bitiscetin, a novel von Willebrand factor modulator protein from Bitis arietans venom. Biochem. Biophys. Res. Commun. 226:1996;273-279.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 273-279
    • Hamako, J.1    Matsui, T.2    Suzuki, M.3    Ito, M.4    Makita, K.5    Fujimura, Y.6    Ozeki, Y.7    Titani, K.8
  • 11
    • 0033842555 scopus 로고    scopus 로고
    • Antibody from mice immunised with DNA encoding the carboxyl-disintegrin and cysteine rich domain (JD9) of the haemorrhagic metalloprotease, Jararhagin, inhibits the main lethal component of viper venom
    • Harrison R.A., Moura-da-Silva A.M., Laing G.D., Wu Y., Richards A., Broadhead A., Bianco A.E., Theakston R.D.G. Antibody from mice immunised with DNA encoding the carboxyl-disintegrin and cysteine rich domain (JD9) of the haemorrhagic metalloprotease, Jararhagin, inhibits the main lethal component of viper venom. J. Clin. Exp. Immunol. 121:2000;358-363.
    • (2000) J. Clin. Exp. Immunol. , vol.121 , pp. 358-363
    • Harrison, R.A.1    Moura-da-Silva, A.M.2    Laing, G.D.3    Wu, Y.4    Richards, A.5    Broadhead, A.6    Bianco, A.E.7    Theakston, R.D.G.8
  • 12
    • 0037086695 scopus 로고    scopus 로고
    • Simultaneous GeneGun immunisation with plasmids encoding antigen and GM-CSF: Significant enhancement of murine antivenom IgG1 titres
    • Harrison R.A., Richards A., Laing G.D., Theakston R.D.G. Simultaneous GeneGun immunisation with plasmids encoding antigen and GM-CSF: significant enhancement of murine antivenom IgG1 titres. Vaccine. 20:2002;1702-1706.
    • (2002) Vaccine , vol.20 , pp. 1702-1706
    • Harrison, R.A.1    Richards, A.2    Laing, G.D.3    Theakston, R.D.G.4
  • 13
    • 0037376318 scopus 로고    scopus 로고
    • The conserved structure of snake venom toxins confers extensive immunological cross-reactivity to toxin-specific antibody
    • Harrison R.A., Wüster W., Theakston R.D.G. The conserved structure of snake venom toxins confers extensive immunological cross-reactivity to toxin-specific antibody. Toxicon. 41:2003;441-449.
    • (2003) Toxicon , vol.41 , pp. 441-449
    • Harrison, R.A.1    Wüster, W.2    Theakston, R.D.G.3
  • 14
    • 0027244625 scopus 로고
    • Action of snake venom components on the haemostatic system
    • Hutton R.A., Warrell D.A. Action of snake venom components on the haemostatic system. Blood Rev. 7:1993;176-189.
    • (1993) Blood Rev. , vol.7 , pp. 176-189
    • Hutton, R.A.1    Warrell, D.A.2
  • 15
    • 0023984742 scopus 로고
    • The antigenic index: A novel algorithm for predicting antigenic determinants
    • Jameson B.A., Wolf H. The antigenic index: a novel algorithm for predicting antigenic determinants. Comput. Appl. Biosci. 4(1):1988;181-186.
    • (1988) Comput. Appl. Biosci. , vol.4 , Issue.1 , pp. 181-186
    • Jameson, B.A.1    Wolf, H.2
  • 16
    • 0030175550 scopus 로고    scopus 로고
    • Insights into the mechanism of haemorrhage caused by snake venom metalloproteases
    • Kamiguti A.S., Hay C.R.M., Theakston R.D.G., Zuzel M. Insights into the mechanism of haemorrhage caused by snake venom metalloproteases. Toxicon. 34:1996;627-642.
    • (1996) Toxicon , vol.34 , pp. 627-642
    • Kamiguti, A.S.1    Hay, C.R.M.2    Theakston, R.D.G.3    Zuzel, M.4
  • 17
    • 0030293016 scopus 로고    scopus 로고
    • Are C-type lectin-related proteins derived by proteolysis of metalloproteinase/disintegrin precursor proteins?
    • Kini R.M. Are C-type lectin-related proteins derived by proteolysis of metalloproteinase/disintegrin precursor proteins? Toxicon. 34(11/12):1996; 1287-1294.
    • (1996) Toxicon , vol.34 , Issue.11-12 , pp. 1287-1294
    • Kini, R.M.1
  • 19
    • 0032528246 scopus 로고    scopus 로고
    • Cloning of subunits of convulxin, a collagen-like platelet-aggregating protein from beta Crotalus durissus terrificus venom
    • Leduc M., Bon C. Cloning of subunits of convulxin, a collagen-like platelet-aggregating protein from beta Crotalus durissus terrificus venom. Biochem. J. 333:1998;389-393.
    • (1998) Biochem. J. , vol.333 , pp. 389-393
    • Leduc, M.1    Bon, C.2
  • 20
    • 0034782555 scopus 로고    scopus 로고
    • Evolutionary relationships among the true vipers (Reptilia: Viperidae) inferred from mitochondrial DNA sequences
    • Lenk P., Kalayabina S., Winl M., Joger U. Evolutionary relationships among the true vipers (Reptilia: Viperidae) inferred from mitochondrial DNA sequences. Mol. Phylogen. Evol. 19:2001;94-104.
    • (2001) Mol. Phylogen. Evol. , vol.19 , pp. 94-104
    • Lenk, P.1    Kalayabina, S.2    Winl, M.3    Joger, U.4
  • 22
    • 0032402107 scopus 로고    scopus 로고
    • Snake venoms and the haemostatic system
    • Markland F.S. Snake venoms and the haemostatic system. Toxicon. 36(12):1998;1749-1800.
    • (1998) Toxicon , vol.36 , Issue.12 , pp. 1749-1800
    • Markland, F.S.1
  • 25
    • 0030979409 scopus 로고    scopus 로고
    • Structure of coagulation factors IX/X-binding protein, a heterodimer of C-type lectin domains
    • Mizuno H., Fujimoto Z., Koizumi M., Kano H., Atoda H., Morita T. Structure of coagulation factors IX/X-binding protein, a heterodimer of C-type lectin domains. Nat. Struct. Biol. 4:1997;438-441.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 438-441
    • Mizuno, H.1    Fujimoto, Z.2    Koizumi, M.3    Kano, H.4    Atoda, H.5    Morita, T.6
  • 27
    • 0027964650 scopus 로고
    • Cloning of metalloprotease genes in the carpet viper (Echis pyramidum leakeyi). Further members of the metalloprotease/disintegrin gene family
    • Paine M.J., Moura-da-Silva A.M., Theakston R.D.G., Crampton J.M. Cloning of metalloprotease genes in the carpet viper (Echis pyramidum leakeyi). Further members of the metalloprotease/disintegrin gene family. Eur. J. Biochem. 224:1994;483-488.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 483-488
    • Paine, M.J.1    Moura-da-Silva, A.M.2    Theakston, R.D.G.3    Crampton, J.M.4
  • 28
    • 85087537765 scopus 로고
    • Isolation, characterization and amino acid sequence of echicetin beta subunit, a specific inhibitor of von Willebrand factor and thrombin interaction with glycoprotein Ib
    • Peng M., Holt J.C., Niewiarowski S. Isolation, characterization and amino acid sequence of echicetin beta subunit, a specific inhibitor of von Willebrand factor and thrombin interaction with glycoprotein Ib. Thromb. Haemost. 67:1994;702-707.
    • (1994) Thromb. Haemost. , vol.67 , pp. 702-707
    • Peng, M.1    Holt, J.C.2    Niewiarowski, S.3
  • 29
    • 0025753137 scopus 로고
    • Thrombin-like venom enzymes: Structure and function
    • Pirkle H., Theodor I. Thrombin-like venom enzymes: structure and function. Adv. Exp. Med. Biol. 281:1990;165-175.
    • (1990) Adv. Exp. Med. Biol. , vol.281 , pp. 165-175
    • Pirkle, H.1    Theodor, I.2
  • 30
    • 0023375195 scopus 로고
    • The neighbour-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The neighbour-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:1987;406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 31
    • 0034209699 scopus 로고    scopus 로고
    • Molecular cloning of glycoprotein Ib-binding protein, Flavocetin-A, which inhibits platelet aggregation
    • Shin Y., Okuyama I., Hasegawa J., Morita T. Molecular cloning of glycoprotein Ib-binding protein, Flavocetin-A, which inhibits platelet aggregation. Thromb. Res. 99:2000;239-247.
    • (2000) Thromb. Res. , vol.99 , pp. 239-247
    • Shin, Y.1    Okuyama, I.2    Hasegawa, J.3    Morita, T.4
  • 32
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.J., Cibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.J.2    Cibson, T.J.3
  • 33
    • 0002414874 scopus 로고    scopus 로고
    • Clinical features of envenoming from snake bites
    • C. Bon, & M. Goyffon. Lyon: Foundation Marcel Merieux
    • Warrell D.A. Clinical features of envenoming from snake bites. Bon C., Goyffon M. Envenomings and their Treatments. 1996;63-76 Foundation Marcel Merieux, Lyon.
    • (1996) Envenomings and their Treatments , pp. 63-76
    • Warrell, D.A.1
  • 34
    • 0141449769 scopus 로고    scopus 로고
    • C-type lectins from snake venoms: New tools for research in thrombosis and haemostasis
    • A. Menez. Chichester: Wiley
    • Wisner A., Leduc M., Bon C. C-type lectins from snake venoms: new tools for research in thrombosis and haemostasis. Menez A. Perspectives in Molecular Toxinology. 2002;357-376 Wiley, Chichester.
    • (2002) Perspectives in Molecular Toxinology , pp. 357-376
    • Wisner, A.1    Leduc, M.2    Bon, C.3
  • 35
    • 0029939421 scopus 로고    scopus 로고
    • Isolation and characterization of carinactivase, a novel prothrombin activator in Echis carinatus venom with a unique catalytic mechanism
    • Yamada D., Sekiya F., Morita T. Isolation and characterization of carinactivase, a novel prothrombin activator in Echis carinatus venom with a unique catalytic mechanism. J. Biol. Chem. 271:1996;5200-5207.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5200-5207
    • Yamada, D.1    Sekiya, F.2    Morita, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.