메뉴 건너뛰기




Volumn 72, Issue 2, 2009, Pages 210-218

Comparative proteomic study of the venom of the piscivorous cone snail Conus consors

Author keywords

Cone snail; Conopeptide; Conotoxin; Conus consors; ESI MS; HPLC; Hydrophobicity; MALDI TOF MS; Mass fingerprint; Mass range; Mass spectrometry; Peptide; Peptidomics; Proteomics; Toxins; Venom; Venomics

Indexed keywords

CONOTOXIN; PROTEOME; SNAIL VENOM;

EID: 60249089640     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2009.01.019     Document Type: Article
Times cited : (74)

References (41)
  • 1
    • 0030729069 scopus 로고    scopus 로고
    • Lecture, 1996. Conus venom peptides, receptor and ion channel targets, and drug design: 50 million years of neuropharmacology
    • B.M. Olivera E.E. Just Lecture, 1996. Conus venom peptides, receptor and ion channel targets, and drug design: 50 million years of neuropharmacology. Mol Biol Cell 1997;8:2101-2109.
    • (1997) Mol Biol Cell , vol.8 , pp. 2101-2109
    • Olivera, B.M.1    Just, E.E.2
  • 2
    • 0242331757 scopus 로고    scopus 로고
    • Therapeutic potential of venom peptides
    • Lewis R.J., and Garcia M.L. Therapeutic potential of venom peptides. Nat Rev Drug Discov 2 (2003) 790-802
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 790-802
    • Lewis, R.J.1    Garcia, M.L.2
  • 3
    • 33644541469 scopus 로고    scopus 로고
    • 'Venomics' or: the venomous systems genome project
    • Menez A., Stocklin R., and Mebs D. 'Venomics' or: the venomous systems genome project. Toxicon 47 (2006) 255-259
    • (2006) Toxicon , vol.47 , pp. 255-259
    • Menez, A.1    Stocklin, R.2    Mebs, D.3
  • 4
    • 33745484291 scopus 로고    scopus 로고
    • Mass spectrometry strategies for venom mapping and peptide sequencing from crude venoms: case applications with single arthropod specimen
    • Favreau P., Menin L., Michalet S., Perret F., Cheneval O., Stocklin M., et al. Mass spectrometry strategies for venom mapping and peptide sequencing from crude venoms: case applications with single arthropod specimen. Toxicon 47 (2006) 676-687
    • (2006) Toxicon , vol.47 , pp. 676-687
    • Favreau, P.1    Menin, L.2    Michalet, S.3    Perret, F.4    Cheneval, O.5    Stocklin, M.6
  • 5
    • 0013458375 scopus 로고    scopus 로고
    • Proteomics of venom peptides
    • Menez A. (Ed), John Wiley & Sons Ltd, Chichester, UK
    • Stocklin R., and Favreau P. Proteomics of venom peptides. In: Menez A. (Ed). Perspectives in molecular toxinology (2002), John Wiley & Sons Ltd, Chichester, UK 107-123
    • (2002) Perspectives in molecular toxinology , pp. 107-123
    • Stocklin, R.1    Favreau, P.2
  • 6
    • 43849090011 scopus 로고    scopus 로고
    • Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis
    • Sanz L., Escolano J., Ferretti M., Biscoglio M.J., Rivera E., Crescenti E.J., et al. Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis. J Proteomics 71 (2008) 46-60
    • (2008) J Proteomics , vol.71 , pp. 46-60
    • Sanz, L.1    Escolano, J.2    Ferretti, M.3    Biscoglio, M.J.4    Rivera, E.5    Crescenti, E.J.6
  • 7
    • 33646133193 scopus 로고    scopus 로고
    • Venom landscapes: mining the complexity of spider venoms via a combined cDNA and mass spectrometric approach
    • Escoubas P., Sollod B., and King G.F. Venom landscapes: mining the complexity of spider venoms via a combined cDNA and mass spectrometric approach. Toxicon 47 (2006) 650-663
    • (2006) Toxicon , vol.47 , pp. 650-663
    • Escoubas, P.1    Sollod, B.2    King, G.F.3
  • 8
    • 46849122906 scopus 로고    scopus 로고
    • Probing peptide libraries from Conus achatinus using mass spectrometry and cDNA sequencing: identification of delta and omega-conotoxins
    • Gowd K.H., Dewan K.K., Iengar P., Krishnan K.S., and Balaram P. Probing peptide libraries from Conus achatinus using mass spectrometry and cDNA sequencing: identification of delta and omega-conotoxins. J Mass Spectrom 43 (2008) 791-805
    • (2008) J Mass Spectrom , vol.43 , pp. 791-805
    • Gowd, K.H.1    Dewan, K.K.2    Iengar, P.3    Krishnan, K.S.4    Balaram, P.5
  • 9
    • 0037372230 scopus 로고    scopus 로고
    • Genetic and ecological correlates of intraspecific variation in pitviper venom composition detected using matrix-assisted laser desorption time-of-flight mass spectrometry (MALDI-TOF-MS) and isoelectric focusing
    • Creer S., Malhotra A., Thorpe R.S., Stocklin R.S., Favreau P.S., and Hao Chou W.S. Genetic and ecological correlates of intraspecific variation in pitviper venom composition detected using matrix-assisted laser desorption time-of-flight mass spectrometry (MALDI-TOF-MS) and isoelectric focusing. J Mol Evol 56 (2003) 317-329
    • (2003) J Mol Evol , vol.56 , pp. 317-329
    • Creer, S.1    Malhotra, A.2    Thorpe, R.S.3    Stocklin, R.S.4    Favreau, P.S.5    Hao Chou, W.S.6
  • 10
    • 34547144755 scopus 로고    scopus 로고
    • Snake venomics of Bitis species reveals large intragenus venom toxin composition variation: application to taxonomy of congeneric taxa
    • Calvete J.J., Escolano J., and Sanz L. Snake venomics of Bitis species reveals large intragenus venom toxin composition variation: application to taxonomy of congeneric taxa. J Proteome Res 6 (2007) 2732-2745
    • (2007) J Proteome Res , vol.6 , pp. 2732-2745
    • Calvete, J.J.1    Escolano, J.2    Sanz, L.3
  • 11
    • 58149512850 scopus 로고    scopus 로고
    • Intersexual variations in the pharmacological properties of Coremiocnemis tropix (Araneae, Theraphosidae) spider venom
    • Herzig V., and Hodgson W.C. Intersexual variations in the pharmacological properties of Coremiocnemis tropix (Araneae, Theraphosidae) spider venom. Toxicon 53 (2008) 196-205
    • (2008) Toxicon , vol.53 , pp. 196-205
    • Herzig, V.1    Hodgson, W.C.2
  • 12
    • 0030725532 scopus 로고    scopus 로고
    • High-performance liquid chromatography matrix-assisted laser desorption/ionization time-of-flight mass spectrometry peptide fingerprinting of tarantula venoms in the genus Brachypelma: chemotaxonomic and biochemical applications
    • Escoubas P., Celerier M.L., and Nakajima T. High-performance liquid chromatography matrix-assisted laser desorption/ionization time-of-flight mass spectrometry peptide fingerprinting of tarantula venoms in the genus Brachypelma: chemotaxonomic and biochemical applications. Rapid Commun Mass Spectrom 11 (1997) 1891-1899
    • (1997) Rapid Commun Mass Spectrom , vol.11 , pp. 1891-1899
    • Escoubas, P.1    Celerier, M.L.2    Nakajima, T.3
  • 13
    • 0034856719 scopus 로고    scopus 로고
    • Moving pieces in a proteomic puzzle: mass fingerprinting of toxic fractions from the venom of Tityus serrulatus (Scorpiones, Buthidae)
    • Pimenta A.M., Stocklin R., Favreau P., Bougis P.E., and Martin-Eauclaire M.F. Moving pieces in a proteomic puzzle: mass fingerprinting of toxic fractions from the venom of Tityus serrulatus (Scorpiones, Buthidae). Rapid Commun Mass Spectrom 15 (2001) 1562-1572
    • (2001) Rapid Commun Mass Spectrom , vol.15 , pp. 1562-1572
    • Pimenta, A.M.1    Stocklin, R.2    Favreau, P.3    Bougis, P.E.4    Martin-Eauclaire, M.F.5
  • 14
    • 33646799127 scopus 로고    scopus 로고
    • The potential of Bothrops moojeni venom in the field of hemostasis. Established use and new insights
    • Perchuc A.M., Menin L., Stocklin R., Buhler B., and Schoni R. The potential of Bothrops moojeni venom in the field of hemostasis. Established use and new insights. Pathophysiol Haemost Thromb 34 (2005) 241-245
    • (2005) Pathophysiol Haemost Thromb , vol.34 , pp. 241-245
    • Perchuc, A.M.1    Menin, L.2    Stocklin, R.3    Buhler, B.4    Schoni, R.5
  • 16
    • 0033545910 scopus 로고    scopus 로고
    • Biochemical characterization and nuclear magnetic resonance structure of novel alpha-conotoxins isolated from the venom of Conus consors
    • Favreau P., Krimm I., Le G.F., Bobenrieth M.J., Lamthanh H., Bouet F., et al. Biochemical characterization and nuclear magnetic resonance structure of novel alpha-conotoxins isolated from the venom of Conus consors. Biochemistry 38 (1999) 6317-6326
    • (1999) Biochemistry , vol.38 , pp. 6317-6326
    • Favreau, P.1    Krimm, I.2    Le, G.F.3    Bobenrieth, M.J.4    Lamthanh, H.5    Bouet, F.6
  • 18
    • 0035253337 scopus 로고    scopus 로고
    • Alpha-cyano-4-hydroxycinnamic acid affinity sample preparation. A protocol for MALDI-MS peptide analysis in proteomics
    • Gobom J., Schuerenberg M., Mueller M., Theiss D., Lehrach H., and Nordhoff E. Alpha-cyano-4-hydroxycinnamic acid affinity sample preparation. A protocol for MALDI-MS peptide analysis in proteomics. Anal Chem 73 (2001) 434-438
    • (2001) Anal Chem , vol.73 , pp. 434-438
    • Gobom, J.1    Schuerenberg, M.2    Mueller, M.3    Theiss, D.4    Lehrach, H.5    Nordhoff, E.6
  • 21
    • 26444450533 scopus 로고    scopus 로고
    • The effect of the mobile phase additives on sensitivity in the analysis of peptides and proteins by high-performance liquid chromatography-electrospray mass spectrometry
    • Garcia M.C. The effect of the mobile phase additives on sensitivity in the analysis of peptides and proteins by high-performance liquid chromatography-electrospray mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci 825 (2005) 111-123
    • (2005) J Chromatogr B Analyt Technol Biomed Life Sci , vol.825 , pp. 111-123
    • Garcia, M.C.1
  • 22
    • 51249106671 scopus 로고    scopus 로고
    • Improved peptide mass fingerprinting matches via optimized sample preparation in MALDI mass spectrometry
    • Padliya N.D., and Wood T.D. Improved peptide mass fingerprinting matches via optimized sample preparation in MALDI mass spectrometry. Anal Chim Acta 627 (2008) 162-168
    • (2008) Anal Chim Acta , vol.627 , pp. 162-168
    • Padliya, N.D.1    Wood, T.D.2
  • 23
    • 0028883956 scopus 로고
    • Enhanced sensitivity for peptide mapping with electrospray liquid chromatography-mass spectrometry in the presence of signal suppression due to trifluoroacetic acid-containing mobile phases
    • Apffel A., Fischer S., Goldberg G., Goodley P.C., and Kuhlmann F.E. Enhanced sensitivity for peptide mapping with electrospray liquid chromatography-mass spectrometry in the presence of signal suppression due to trifluoroacetic acid-containing mobile phases. J Chromatogr A 712 (1995) 177-190
    • (1995) J Chromatogr A , vol.712 , pp. 177-190
    • Apffel, A.1    Fischer, S.2    Goldberg, G.3    Goodley, P.C.4    Kuhlmann, F.E.5
  • 24
    • 35649011512 scopus 로고    scopus 로고
    • Mass fingerprinting of toxic fractions from the venom of the Indian red scorpion, Mesobuthus tamulus: biotope-specific variation in the expression of venom peptides
    • Newton K.A., Clench M.R., Deshmukh R., Jeyaseelan K., and Strong P.N. Mass fingerprinting of toxic fractions from the venom of the Indian red scorpion, Mesobuthus tamulus: biotope-specific variation in the expression of venom peptides. Rapid Commun Mass Spectrom 21 (2007) 3467-3476
    • (2007) Rapid Commun Mass Spectrom , vol.21 , pp. 3467-3476
    • Newton, K.A.1    Clench, M.R.2    Deshmukh, R.3    Jeyaseelan, K.4    Strong, P.N.5
  • 25
    • 44949130553 scopus 로고    scopus 로고
    • Mass spectrometry analysis, amino acid sequence and biological activity of venom components from the Brazilian scorpion Opisthacanthus cayaporum
    • Schwartz E.F., Camargos T.S., Zamudio F.Z., Silva L.P., Bloch Jr. C., Caixeta F., et al. Mass spectrometry analysis, amino acid sequence and biological activity of venom components from the Brazilian scorpion Opisthacanthus cayaporum. Toxicon 51 (2008) 1499-1508
    • (2008) Toxicon , vol.51 , pp. 1499-1508
    • Schwartz, E.F.1    Camargos, T.S.2    Zamudio, F.Z.3    Silva, L.P.4    Bloch Jr., C.5    Caixeta, F.6
  • 26
    • 0012123168 scopus 로고    scopus 로고
    • Conus venom peptides (conopeptides): inter-species, intra-species and within individual variation revealed by ionspray mass spectrometry
    • Lazarovici E., Spira M.E., and Zlotkin E. (Eds), Alaken, Fort Collins
    • Bingham J.P., Jones A., Lewis R.J., Andrew P.R., and Alewood D. Conus venom peptides (conopeptides): inter-species, intra-species and within individual variation revealed by ionspray mass spectrometry. In: Lazarovici E., Spira M.E., and Zlotkin E. (Eds). Biomedical Aspects of Marine Pharmacology (1996), Alaken, Fort Collins 13-27
    • (1996) Biomedical Aspects of Marine Pharmacology , pp. 13-27
    • Bingham, J.P.1    Jones, A.2    Lewis, R.J.3    Andrew, P.R.4    Alewood, D.5
  • 27
    • 0029080121 scopus 로고
    • A new family of Conus peptides targeted to the nicotinic acetylcholine receptor
    • Hopkins C., Grilley M., Miller C., Shon K.J., Cruz L.J., Gray W.R., et al. A new family of Conus peptides targeted to the nicotinic acetylcholine receptor. J Biol Chem 270 (1995) 22361-22367
    • (1995) J Biol Chem , vol.270 , pp. 22361-22367
    • Hopkins, C.1    Grilley, M.2    Miller, C.3    Shon, K.J.4    Cruz, L.J.5    Gray, W.R.6
  • 28
    • 0028973580 scopus 로고
    • alpha-Conotoxin EI, a new nicotinic acetylcholine receptor antagonist with novel selectivity
    • Martinez J.S., Olivera B.M., Gray W.R., Craig A.G., Groebe D.R., Abramson S.N., et al. alpha-Conotoxin EI, a new nicotinic acetylcholine receptor antagonist with novel selectivity. Biochemistry 34 (1995) 14519-14526
    • (1995) Biochemistry , vol.34 , pp. 14519-14526
    • Martinez, J.S.1    Olivera, B.M.2    Gray, W.R.3    Craig, A.G.4    Groebe, D.R.5    Abramson, S.N.6
  • 29
    • 3042759058 scopus 로고    scopus 로고
    • AlphaA-Conotoxin OIVA defines a new alphaA-conotoxin subfamily of nicotinic acetylcholine receptor inhibitors
    • Teichert R.W., Rivier J., Dykert J., Cervini L., Gulyas J., Bulaj G., et al. AlphaA-Conotoxin OIVA defines a new alphaA-conotoxin subfamily of nicotinic acetylcholine receptor inhibitors. Toxicon 44 (2004) 207-214
    • (2004) Toxicon , vol.44 , pp. 207-214
    • Teichert, R.W.1    Rivier, J.2    Dykert, J.3    Cervini, L.4    Gulyas, J.5    Bulaj, G.6
  • 30
    • 33645237703 scopus 로고    scopus 로고
    • Structural and functional diversities among mu-conotoxins targeting TTX-resistant sodium channels
    • Zhang M.M., Fiedler B., Green B.R., Catlin P., Watkins M., Garrett J.E., et al. Structural and functional diversities among mu-conotoxins targeting TTX-resistant sodium channels. Biochemistry 45 (2006) 3723-3732
    • (2006) Biochemistry , vol.45 , pp. 3723-3732
    • Zhang, M.M.1    Fiedler, B.2    Green, B.R.3    Catlin, P.4    Watkins, M.5    Garrett, J.E.6
  • 31
    • 0032844209 scopus 로고    scopus 로고
    • A new conotoxin isolated from Conus consors venom acting selectively on axons and motor nerve terminals through a Na+-dependent mechanism
    • Le Gall F., Favreau P., Benoit E., Mattei C., Bouet F., Menou J.L., et al. A new conotoxin isolated from Conus consors venom acting selectively on axons and motor nerve terminals through a Na+-dependent mechanism. Eur J Neurosci 11 (1999) 3134-3142
    • (1999) Eur J Neurosci , vol.11 , pp. 3134-3142
    • Le Gall, F.1    Favreau, P.2    Benoit, E.3    Mattei, C.4    Bouet, F.5    Menou, J.L.6
  • 35
  • 36
  • 37
    • 52049126211 scopus 로고    scopus 로고
    • Neuronally selective mu-conotoxins from Conus striatus utilise an alpha-helical motif to target mammalian sodium channels
    • Schroeder C.I., Ekberg J., Nielsen K.J., Adams D., Loughnan M.L., Thomas L., et al. Neuronally selective mu-conotoxins from Conus striatus utilise an alpha-helical motif to target mammalian sodium channels. J Biol Chem 283 (2008) 21621-21628
    • (2008) J Biol Chem , vol.283 , pp. 21621-21628
    • Schroeder, C.I.1    Ekberg, J.2    Nielsen, K.J.3    Adams, D.4    Loughnan, M.L.5    Thomas, L.6
  • 38
    • 47849085599 scopus 로고    scopus 로고
    • Alpha-conopeptides specifically expressed in the salivary gland of Conus pulicarius
    • Biggs J.S., Olivera B.M., and Kantor Y.I. Alpha-conopeptides specifically expressed in the salivary gland of Conus pulicarius. Toxicon 52 (2008) 101-105
    • (2008) Toxicon , vol.52 , pp. 101-105
    • Biggs, J.S.1    Olivera, B.M.2    Kantor, Y.I.3
  • 39
    • 33646470012 scopus 로고    scopus 로고
    • Fourier transform mass spectrometry: a powerful tool for toxin analysis
    • Quinton L., Le Caer J.P., Vinh J., Gilles N., and Chamot-Rooke J. Fourier transform mass spectrometry: a powerful tool for toxin analysis. Toxicon 47 (2006) 715-726
    • (2006) Toxicon , vol.47 , pp. 715-726
    • Quinton, L.1    Le Caer, J.P.2    Vinh, J.3    Gilles, N.4    Chamot-Rooke, J.5
  • 41
    • 0035807854 scopus 로고    scopus 로고
    • A new omega-conotoxin that targets N-type voltage-sensitive calcium channels with unusual specificity
    • Favreau P., Gilles N., Lamthanh H., Bournaud R., Shimahara T., Bouet F., et al. A new omega-conotoxin that targets N-type voltage-sensitive calcium channels with unusual specificity. Biochemistry 40 (2001) 14567-14575
    • (2001) Biochemistry , vol.40 , pp. 14567-14575
    • Favreau, P.1    Gilles, N.2    Lamthanh, H.3    Bournaud, R.4    Shimahara, T.5    Bouet, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.