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Volumn 74, Issue 9, 2011, Pages 1652-1663

2-DE-based proteomic investigation of the saliva of the Amazonian triatomine vectors of Chagas disease: Rhodnius brethesi and Rhodnius robustus

Author keywords

Chagas disease; MALDI MS MS; Phosphorylation; Proteomics; Saliva; Triatomine

Indexed keywords

LIPOCALIN; SALIVA PROTEIN;

EID: 80051673323     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2011.02.022     Document Type: Article
Times cited : (18)

References (45)
  • 2
    • 18144414708 scopus 로고    scopus 로고
    • Testing the sister-group relationship of the Rhodniini and Triatomini (Insecta: Hemiptera: Reduviidae: Triatominae)
    • de Paula A.S., Diotaiuti L., Schofield C.J. Testing the sister-group relationship of the Rhodniini and Triatomini (Insecta: Hemiptera: Reduviidae: Triatominae). Mol Phylogenet Evol 2005, 35:712-718.
    • (2005) Mol Phylogenet Evol , vol.35 , pp. 712-718
    • de Paula, A.S.1    Diotaiuti, L.2    Schofield, C.J.3
  • 4
    • 48249085713 scopus 로고    scopus 로고
    • The elimination of Chagas' disease from Brazil
    • Massad E. The elimination of Chagas' disease from Brazil. Epidemiol Infect 2008, 136:1153-1164.
    • (2008) Epidemiol Infect , vol.136 , pp. 1153-1164
    • Massad, E.1
  • 5
    • 0036637084 scopus 로고    scopus 로고
    • The impact of Chagas disease control in Latin America: a review
    • Dias J.C., Silveira A.C., Schofield C.J. The impact of Chagas disease control in Latin America: a review. Mem Inst Oswaldo Cruz 2002, 97:603-612.
    • (2002) Mem Inst Oswaldo Cruz , vol.97 , pp. 603-612
    • Dias, J.C.1    Silveira, A.C.2    Schofield, C.J.3
  • 6
    • 35748942895 scopus 로고    scopus 로고
    • The saliva proteome of the blood-feeding insect Triatoma infestans is rich in platelet-aggregation inhibitors
    • Charneau S., Junqueira M., Costa C.M., Pires D.L., Fernandes E.S., Bussacos A.C., et al. The saliva proteome of the blood-feeding insect Triatoma infestans is rich in platelet-aggregation inhibitors. Int J Mass Spectrom 2007, 268:265-276.
    • (2007) Int J Mass Spectrom , vol.268 , pp. 265-276
    • Charneau, S.1    Junqueira, M.2    Costa, C.M.3    Pires, D.L.4    Fernandes, E.S.5    Bussacos, A.C.6
  • 9
    • 64449087641 scopus 로고    scopus 로고
    • Classification, evolution, and species groups within the Triatominae
    • Schofield C.J., Galvao C. Classification, evolution, and species groups within the Triatominae. Acta Trop 2009, 110:88-100.
    • (2009) Acta Trop , vol.110 , pp. 88-100
    • Schofield, C.J.1    Galvao, C.2
  • 10
    • 77149137065 scopus 로고    scopus 로고
    • A repertoire of the dominant transcripts from the salivary glands of the blood-sucking bug, Triatoma dimidiata, a vector of Chagas disease
    • Kato H., Jochim R.C., Gomez E.A., Sakoda R., Iwata H., Valenzuela J.G., et al. A repertoire of the dominant transcripts from the salivary glands of the blood-sucking bug, Triatoma dimidiata, a vector of Chagas disease. Infect Genet Evol 2010, 10:184-191.
    • (2010) Infect Genet Evol , vol.10 , pp. 184-191
    • Kato, H.1    Jochim, R.C.2    Gomez, E.A.3    Sakoda, R.4    Iwata, H.5    Valenzuela, J.G.6
  • 12
    • 36348953311 scopus 로고    scopus 로고
    • Biogeography and evolution of Amazonian triatomines (Heteroptera: Reduviidae): implications for Chagas disease surveillance in humid forest ecoregions
    • Abad-Franch F., Monteiro F.A. Biogeography and evolution of Amazonian triatomines (Heteroptera: Reduviidae): implications for Chagas disease surveillance in humid forest ecoregions. Mem Inst Oswaldo Cruz 2007, 102(Suppl 1):57-70.
    • (2007) Mem Inst Oswaldo Cruz , vol.102 , Issue.SUPPL 1 , pp. 57-70
    • Abad-Franch, F.1    Monteiro, F.A.2
  • 15
    • 0034467318 scopus 로고    scopus 로고
    • Phylogeny and molecular taxonomy of the Rhodniini derived from mitochondrial and nuclear DNA sequences
    • Monteiro F.A., Wesson D.M., Dotson E.M., Schofield C.J., Beard C.B. Phylogeny and molecular taxonomy of the Rhodniini derived from mitochondrial and nuclear DNA sequences. Am J Trop Med Hyg 2000, 62:460-465.
    • (2000) Am J Trop Med Hyg , vol.62 , pp. 460-465
    • Monteiro, F.A.1    Wesson, D.M.2    Dotson, E.M.3    Schofield, C.J.4    Beard, C.B.5
  • 16
    • 0036010091 scopus 로고    scopus 로고
    • Allozyme relationships among ten species of Rhodniini, showing paraphyly of Rhodnius including Psammolestes
    • Monteiro F.A., Lazoski C., Noireau F., Sole-Cava A.M. Allozyme relationships among ten species of Rhodniini, showing paraphyly of Rhodnius including Psammolestes. Med Vet Entomol 2002, 16:83-90.
    • (2002) Med Vet Entomol , vol.16 , pp. 83-90
    • Monteiro, F.A.1    Lazoski, C.2    Noireau, F.3    Sole-Cava, A.M.4
  • 17
    • 0031733968 scopus 로고    scopus 로고
    • Salivary heme proteins distinguish Rhodnius prolixus from Rhodnius robustus (Hemiptera: Reduviidae: Triatominae)
    • Soares R.P., Gontijo N.F., Romanha A.J., Diotaiuti L., Pereira M.H. Salivary heme proteins distinguish Rhodnius prolixus from Rhodnius robustus (Hemiptera: Reduviidae: Triatominae). Acta Trop 1998, 71:285-291.
    • (1998) Acta Trop , vol.71 , pp. 285-291
    • Soares, R.P.1    Gontijo, N.F.2    Romanha, A.J.3    Diotaiuti, L.4    Pereira, M.H.5
  • 19
    • 84988074679 scopus 로고
    • Improved silver staining of plant-proteins, RNA and DNA in polyacrylamide gels
    • Blum H., Beier H., Gross H.J. Improved silver staining of plant-proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 1987, 8:93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 20
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 1996, 68:850-858.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 21
    • 0032961627 scopus 로고    scopus 로고
    • Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: a method for the removal of silver ions to enhance sensitivity
    • Gharahdaghi F., Weinberg C.R., Meagher D.A., Imai B.S., Mische S.M. Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: a method for the removal of silver ions to enhance sensitivity. Electrophoresis 1999, 20:601-605.
    • (1999) Electrophoresis , vol.20 , pp. 601-605
    • Gharahdaghi, F.1    Weinberg, C.R.2    Meagher, D.A.3    Imai, B.S.4    Mische, S.M.5
  • 22
    • 40649122246 scopus 로고    scopus 로고
    • On-target sample preparation of 4-sulfophenyl isothiocyanate-derivatized peptides using AnchorChip Targets
    • Zhang X., Rogowska-Wrzesinska A., Roepstorff P. On-target sample preparation of 4-sulfophenyl isothiocyanate-derivatized peptides using AnchorChip Targets. J Mass Spectrom 2008, 43:346-359.
    • (2008) J Mass Spectrom , vol.43 , pp. 346-359
    • Zhang, X.1    Rogowska-Wrzesinska, A.2    Roepstorff, P.3
  • 23
    • 0033057707 scopus 로고    scopus 로고
    • Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry
    • Gobom J., Nordhoff E., Mirgorodskaya E., Ekman R., Roepstorff P. Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry. J Mass Spectrom 1999, 34:105-116.
    • (1999) J Mass Spectrom , vol.34 , pp. 105-116
    • Gobom, J.1    Nordhoff, E.2    Mirgorodskaya, E.3    Ekman, R.4    Roepstorff, P.5
  • 24
    • 0035326344 scopus 로고    scopus 로고
    • Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching
    • Shevchenko A., Sunyaev S., Loboda A., Bork P., Ens W., Standing K.G. Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching. Anal Chem 2001, 73:1917-1926.
    • (2001) Anal Chem , vol.73 , pp. 1917-1926
    • Shevchenko, A.1    Sunyaev, S.2    Loboda, A.3    Bork, P.4    Ens, W.5    Standing, K.G.6
  • 25
    • 63349100700 scopus 로고    scopus 로고
    • Changes in the 2-DE protein profile during zygotic embryogenesis in the Brazilian Pine (Araucaria angustifolia)
    • Balbuena T.S., Silveira V., Junqueira M., Dias L.L., Santa-Catarina C., Shevchenko A., et al. Changes in the 2-DE protein profile during zygotic embryogenesis in the Brazilian Pine (Araucaria angustifolia). J Proteomics 2009, 72:337-352.
    • (2009) J Proteomics , vol.72 , pp. 337-352
    • Balbuena, T.S.1    Silveira, V.2    Junqueira, M.3    Dias, L.L.4    Santa-Catarina, C.5    Shevchenko, A.6
  • 26
    • 0028947447 scopus 로고
    • Purification, partial characterization, and cloning of nitric oxide-carrying heme proteins (nitrophorins) from salivary glands of the blood-sucking insect Rhodnius prolixus
    • Champagne D.E., Nussenzveig R.H., Ribeiro J.M. Purification, partial characterization, and cloning of nitric oxide-carrying heme proteins (nitrophorins) from salivary glands of the blood-sucking insect Rhodnius prolixus. J Biol Chem 1995, 270:8691-8695.
    • (1995) J Biol Chem , vol.270 , pp. 8691-8695
    • Champagne, D.E.1    Nussenzveig, R.H.2    Ribeiro, J.M.3
  • 27
    • 9244254265 scopus 로고    scopus 로고
    • Purification, characterization and cDNA cloning of a novel anticoagulant of the intrinsic pathway, (prolixin-S) from salivary glands of the blood sucking bug, Rhodnius prolixus
    • Sun J., Yamaguchi M., Yuda M., Miura K., Takeya H., Hirai M., et al. Purification, characterization and cDNA cloning of a novel anticoagulant of the intrinsic pathway, (prolixin-S) from salivary glands of the blood sucking bug, Rhodnius prolixus. Thromb Haemost 1996, 75:573-577.
    • (1996) Thromb Haemost , vol.75 , pp. 573-577
    • Sun, J.1    Yamaguchi, M.2    Yuda, M.3    Miura, K.4    Takeya, H.5    Hirai, M.6
  • 28
    • 0032029865 scopus 로고    scopus 로고
    • Characterization and cDNA cloning of a hemoprotein in the salivary glands of the blood-sucking insect, Rhodnius prolixus
    • Sun J., Yuda M., Miura K., Chinzei Y. Characterization and cDNA cloning of a hemoprotein in the salivary glands of the blood-sucking insect, Rhodnius prolixus. Insect Biochem Mol Biol 1998, 28:191-200.
    • (1998) Insect Biochem Mol Biol , vol.28 , pp. 191-200
    • Sun, J.1    Yuda, M.2    Miura, K.3    Chinzei, Y.4
  • 29
    • 0037849950 scopus 로고    scopus 로고
    • Inhibition of hemostasis by a high affinity biogenic amine-binding protein from the saliva of a blood-feeding insect
    • Andersen J.F., Francischetti I.M., Valenzuela J.G., Schuck P., Ribeiro J.M. Inhibition of hemostasis by a high affinity biogenic amine-binding protein from the saliva of a blood-feeding insect. J Biol Chem 2003, 278:4611-4617.
    • (2003) J Biol Chem , vol.278 , pp. 4611-4617
    • Andersen, J.F.1    Francischetti, I.M.2    Valenzuela, J.G.3    Schuck, P.4    Ribeiro, J.M.5
  • 30
    • 0034724672 scopus 로고    scopus 로고
    • Purification, cloning, expression, and mechanism of action of a novel platelet aggregation inhibitor from the salivary gland of the blood-sucking bug, Rhodnius prolixus
    • Francischetti I.M., Ribeiro J.M., Champagne D., Andersen J. Purification, cloning, expression, and mechanism of action of a novel platelet aggregation inhibitor from the salivary gland of the blood-sucking bug, Rhodnius prolixus. J Biol Chem 2000, 275:12639-12650.
    • (2000) J Biol Chem , vol.275 , pp. 12639-12650
    • Francischetti, I.M.1    Ribeiro, J.M.2    Champagne, D.3    Andersen, J.4
  • 31
    • 0027213409 scopus 로고
    • Reversible binding of nitric oxide by a salivary heme protein from a bloodsucking insect
    • Ribeiro J.M., Hazzard J.M., Nussenzveig R.H., Champagne D.E., Walker F.A. Reversible binding of nitric oxide by a salivary heme protein from a bloodsucking insect. Science 1993, 260:539-541.
    • (1993) Science , vol.260 , pp. 539-541
    • Ribeiro, J.M.1    Hazzard, J.M.2    Nussenzveig, R.H.3    Champagne, D.E.4    Walker, F.A.5
  • 32
    • 0028029463 scopus 로고
    • High affinity histamine-binding and antihistaminic activity of the salivary nitric oxide-carrying heme protein (nitrophorin) of Rhodnius prolixus
    • Ribeiro J.M., Walker F.A. High affinity histamine-binding and antihistaminic activity of the salivary nitric oxide-carrying heme protein (nitrophorin) of Rhodnius prolixus. J Exp Med 1994, 180:2251-2257.
    • (1994) J Exp Med , vol.180 , pp. 2251-2257
    • Ribeiro, J.M.1    Walker, F.A.2
  • 33
    • 0034702817 scopus 로고    scopus 로고
    • Kinetics and equilibria in ligand binding by nitrophorins 1-4: evidence for stabilization of a nitric oxide-ferriheme complex through a ligand-induced conformational trap
    • Andersen J.F., Ding X.D., Balfour C., Shokhireva T.K., Champagne D.E., Walker F.A., et al. Kinetics and equilibria in ligand binding by nitrophorins 1-4: evidence for stabilization of a nitric oxide-ferriheme complex through a ligand-induced conformational trap. Biochemistry 2000, 39:10118-10131.
    • (2000) Biochemistry , vol.39 , pp. 10118-10131
    • Andersen, J.F.1    Ding, X.D.2    Balfour, C.3    Shokhireva, T.K.4    Champagne, D.E.5    Walker, F.A.6
  • 34
    • 0029044597 scopus 로고
    • Purification and characterization of prolixin S (nitrophorin 2), the salivary anticoagulant of the blood-sucking bug Rhodnius prolixus
    • Ribeiro J.M., Schneider M., Guimaraes J.A. Purification and characterization of prolixin S (nitrophorin 2), the salivary anticoagulant of the blood-sucking bug Rhodnius prolixus. Biochem J 1995, 308(Pt 1):243-249.
    • (1995) Biochem J , vol.308 , Issue.PART 1 , pp. 243-249
    • Ribeiro, J.M.1    Schneider, M.2    Guimaraes, J.A.3
  • 35
    • 0032575297 scopus 로고    scopus 로고
    • Nitrophorin-2: a novel mixed-type reversible specific inhibitor of the intrinsic factor-X activating complex
    • Zhang Y., Ribeiro J.M., Guimaraes J.A., Walsh P.N. Nitrophorin-2: a novel mixed-type reversible specific inhibitor of the intrinsic factor-X activating complex. Biochemistry 1998, 37:10681-10690.
    • (1998) Biochemistry , vol.37 , pp. 10681-10690
    • Zhang, Y.1    Ribeiro, J.M.2    Guimaraes, J.A.3    Walsh, P.N.4
  • 36
    • 0037133520 scopus 로고    scopus 로고
    • Biochemical and functional characterization of recombinant Rhodnius prolixus platelet aggregation inhibitor 1 as a novel lipocalin with high affinity for adenosine diphosphate and other adenine nucleotides
    • Francischetti I.M., Andersen J.F., Ribeiro J.M. Biochemical and functional characterization of recombinant Rhodnius prolixus platelet aggregation inhibitor 1 as a novel lipocalin with high affinity for adenosine diphosphate and other adenine nucleotides. Biochemistry 2002, 41:3810-3818.
    • (2002) Biochemistry , vol.41 , pp. 3810-3818
    • Francischetti, I.M.1    Andersen, J.F.2    Ribeiro, J.M.3
  • 38
    • 0030666566 scopus 로고    scopus 로고
    • Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug
    • Fuentes-Prior P., Noeske-Jungblut C., Donner P., Schleuning W.D., Huber R., Bode W. Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug. Proc Natl Acad Sci USA 1997, 94:11845-11850.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11845-11850
    • Fuentes-Prior, P.1    Noeske-Jungblut, C.2    Donner, P.3    Schleuning, W.D.4    Huber, R.5    Bode, W.6
  • 40
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen M.R., Thingholm T.E., Jensen O.N., Roepstorff P., Jorgensen T.J. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol Cell Proteomics 2005, 4:873-886.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jorgensen, T.J.5
  • 41
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • Blom N., Gammeltoft S., Brunak S. Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 1999, 294:1351-1362.
    • (1999) J Mol Biol , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 42
    • 29144471957 scopus 로고    scopus 로고
    • Characterization of human tear proteome using multiple proteomic analysis techniques
    • Li N., Wang N., Zheng J., Liu X.M., Lever O.W., Erickson P.M., et al. Characterization of human tear proteome using multiple proteomic analysis techniques. J Proteome Res 2005, 4:2052-2061.
    • (2005) J Proteome Res , vol.4 , pp. 2052-2061
    • Li, N.1    Wang, N.2    Zheng, J.3    Liu, X.M.4    Lever, O.W.5    Erickson, P.M.6
  • 44
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome
    • Mann M., Ong S.E., Gronborg M., Steen H., Jensen O.N., Pandey A. Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trends Biotechnol 2002, 20:261-268.
    • (2002) Trends Biotechnol , vol.20 , pp. 261-268
    • Mann, M.1    Ong, S.E.2    Gronborg, M.3    Steen, H.4    Jensen, O.N.5    Pandey, A.6


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