메뉴 건너뛰기




Volumn 82, Issue , 2013, Pages 52-63

The trypanosoma rangeli trypomastigote surfaceome reveals novel proteins and targets for specific diagnosis

Author keywords

Antigens; GPI anchored proteins; Proteomic; Surface proteins; Trypanosoma rangeli

Indexed keywords

CALCIUM BINDING PROTEIN; MEMBRANE PROTEIN;

EID: 84875761938     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.02.011     Document Type: Article
Times cited : (15)

References (74)
  • 1
    • 0000886795 scopus 로고
    • Biology of Trypanosoma (Herpetosoma) rangeli Tejera
    • London Academic, London, W.H.R. Lumsden, D.A. Evans (Eds.)
    • D'Alessandro A. Biology of Trypanosoma (Herpetosoma) rangeli Tejera. Biology of the Kinetoplastida 1976, 327-403. London Academic, London. W.H.R. Lumsden, D.A. Evans (Eds.).
    • (1976) Biology of the Kinetoplastida , pp. 327-403
    • D'Alessandro, A.1
  • 3
    • 77950940030 scopus 로고    scopus 로고
    • Human trypanosomiasis in the eastern region of the Panama Province: new endemic areas for Chagas disease
    • Calzada J.E., Pineda V., Garisto J.D., Samudio F., Santamaria A.M., Saldana A. Human trypanosomiasis in the eastern region of the Panama Province: new endemic areas for Chagas disease. Am J Trop Med Hyg 2010, 82:580-582.
    • (2010) Am J Trop Med Hyg , vol.82 , pp. 580-582
    • Calzada, J.E.1    Pineda, V.2    Garisto, J.D.3    Samudio, F.4    Santamaria, A.M.5    Saldana, A.6
  • 4
    • 84855770578 scopus 로고    scopus 로고
    • WHO, Fact Sheet No 340, World Health Organization
    • WHO Chagas disease (American trypanosomiasis) 2012, Fact Sheet No 340, World Health Organization.
    • (2012) Chagas disease (American trypanosomiasis)
  • 5
    • 31544451278 scopus 로고    scopus 로고
    • Predominance of Trypanosoma rangeli infection in children from a Chagas disease endemic area in the west-shore of the Panama canal
    • Saldana A., Samudio F., Miranda A., Herrera L.M., Saavedra S.P., Caceres L., et al. Predominance of Trypanosoma rangeli infection in children from a Chagas disease endemic area in the west-shore of the Panama canal. Mem Inst Oswaldo Cruz 2005, 100:729-731.
    • (2005) Mem Inst Oswaldo Cruz , vol.100 , pp. 729-731
    • Saldana, A.1    Samudio, F.2    Miranda, A.3    Herrera, L.M.4    Saavedra, S.P.5    Caceres, L.6
  • 6
    • 46749130415 scopus 로고    scopus 로고
    • Trypanosoma rangeli Tejera, 1920, in chronic Chagas' disease patients under ambulatory care at the Evandro Chagas Clinical Research Institute (IPEC-Fiocruz, Brazil)
    • de Sousa M.A., da Silva Fonseca T., Dos Santos B.N., Dos Santos Pereira S.M., Carvalhal C., Hasslocher Moreno A.M. Trypanosoma rangeli Tejera, 1920, in chronic Chagas' disease patients under ambulatory care at the Evandro Chagas Clinical Research Institute (IPEC-Fiocruz, Brazil). Parasitol Res 2008, 103:697-703.
    • (2008) Parasitol Res , vol.103 , pp. 697-703
    • de Sousa, M.A.1    da Silva Fonseca, T.2    Dos Santos, B.N.3    Dos Santos Pereira, S.M.4    Carvalhal, C.5    Hasslocher Moreno, A.M.6
  • 8
    • 0032946031 scopus 로고    scopus 로고
    • Mini-exon gene sequence polymorphism among Trypanosoma rangeli strains isolated from distinct geographical regions
    • Grisard E.C., Campbell D.A., Romanha A.J. Mini-exon gene sequence polymorphism among Trypanosoma rangeli strains isolated from distinct geographical regions. Parasitology 1999, 118(Pt 4):375-382.
    • (1999) Parasitology , vol.118 , Issue.PART 4 , pp. 375-382
    • Grisard, E.C.1    Campbell, D.A.2    Romanha, A.J.3
  • 9
    • 77549088297 scopus 로고    scopus 로고
    • Immunodiagnosis of Chagas disease: synthesis of three latex-protein complexes containing different antigens of Trypanosoma cruzi
    • Gonzalez V.D., Garcia V.S., Vega J.R., Marcipar I.S., Meira G.R., Gugliotta L.M. Immunodiagnosis of Chagas disease: synthesis of three latex-protein complexes containing different antigens of Trypanosoma cruzi. Colloids Surf B Biointerfaces 2010, 77:12-17.
    • (2010) Colloids Surf B Biointerfaces , vol.77 , pp. 12-17
    • Gonzalez, V.D.1    Garcia, V.S.2    Vega, J.R.3    Marcipar, I.S.4    Meira, G.R.5    Gugliotta, L.M.6
  • 10
    • 71949119401 scopus 로고    scopus 로고
    • Characterising the KMP-11 and HSP-70 recombinant antigens' humoral immune response profile in chagasic patients
    • Flechas I.D., Cuellar A., Cucunuba Z.M., Rosas F., Velasco V., Steindel M., et al. Characterising the KMP-11 and HSP-70 recombinant antigens' humoral immune response profile in chagasic patients. BMC Infect Dis 2009, 9:186.
    • (2009) BMC Infect Dis , vol.9 , pp. 186
    • Flechas, I.D.1    Cuellar, A.2    Cucunuba, Z.M.3    Rosas, F.4    Velasco, V.5    Steindel, M.6
  • 11
    • 0018627250 scopus 로고
    • Antigenic make-up of Trypanosoma cruzi culture forms: identification of a specific component
    • Afchain D., Le Ray D., Fruit J., Capron A. Antigenic make-up of Trypanosoma cruzi culture forms: identification of a specific component. J Parasitol 1979, 65:507-514.
    • (1979) J Parasitol , vol.65 , pp. 507-514
    • Afchain, D.1    Le Ray, D.2    Fruit, J.3    Capron, A.4
  • 12
    • 0029930605 scopus 로고    scopus 로고
    • Trypanosoma rangeli: epimastigote immunogenicity and cross-reaction with Trypanosoma cruzi
    • Saldana A., Sousa O.E. Trypanosoma rangeli: epimastigote immunogenicity and cross-reaction with Trypanosoma cruzi. J Parasitol 1996, 82:363-366.
    • (1996) J Parasitol , vol.82 , pp. 363-366
    • Saldana, A.1    Sousa, O.E.2
  • 13
    • 77954726282 scopus 로고    scopus 로고
    • Trypanosoma rangeli in a blood donor at the Valencian Blood Transfusion Centre
    • Parada C., Villalba J., Alvarez M., Puig N., Planelles D., Ramada C., et al. Trypanosoma rangeli in a blood donor at the Valencian Blood Transfusion Centre. Vox Sang 2010, 99:193-194.
    • (2010) Vox Sang , vol.99 , pp. 193-194
    • Parada, C.1    Villalba, J.2    Alvarez, M.3    Puig, N.4    Planelles, D.5    Ramada, C.6
  • 14
    • 64949191444 scopus 로고    scopus 로고
    • Different serological cross-reactivity of Trypanosoma rangeli forms in Trypanosoma cruzi-infected patients sera
    • de Moraes M.H., Guarneri A.A., Girardi F.P., Rodrigues J.B., Eger I., Tyler K.M., et al. Different serological cross-reactivity of Trypanosoma rangeli forms in Trypanosoma cruzi-infected patients sera. Parasites and Vectors 2008, 1:20.
    • (2008) Parasites and Vectors , vol.1 , pp. 20
    • de Moraes, M.H.1    Guarneri, A.A.2    Girardi, F.P.3    Rodrigues, J.B.4    Eger, I.5    Tyler, K.M.6
  • 15
    • 0036661949 scopus 로고    scopus 로고
    • Molecular characterization and diagnosis of trypanosoma cruzi and T. rangeli
    • Guhl F., Jaramillo C., Carranza J.C., Vallejo G.A. Molecular characterization and diagnosis of trypanosoma cruzi and T. rangeli. Arch Med Res 2002, 33:362-370.
    • (2002) Arch Med Res , vol.33 , pp. 362-370
    • Guhl, F.1    Jaramillo, C.2    Carranza, J.C.3    Vallejo, G.A.4
  • 16
    • 77956260301 scopus 로고    scopus 로고
    • Molecular mechanisms of host cell invasion by Trypanosoma cruzi
    • Epting C.L., Coates B.M., Engman D.M. Molecular mechanisms of host cell invasion by Trypanosoma cruzi. Exp Parasitol 2010, 126:283-291.
    • (2010) Exp Parasitol , vol.126 , pp. 283-291
    • Epting, C.L.1    Coates, B.M.2    Engman, D.M.3
  • 17
    • 84855558173 scopus 로고    scopus 로고
    • Improved proteomic approach for the discovery of potential vaccine targets in Trypanosoma cruzi
    • Nakayasu E.S., Sobreira T.J., Torres R., Ganiko L., Oliveira P.S., Marques A.F., et al. Improved proteomic approach for the discovery of potential vaccine targets in Trypanosoma cruzi. J Proteome Res 2012, 11:237-246.
    • (2012) J Proteome Res , vol.11 , pp. 237-246
    • Nakayasu, E.S.1    Sobreira, T.J.2    Torres, R.3    Ganiko, L.4    Oliveira, P.S.5    Marques, A.F.6
  • 18
    • 0034793409 scopus 로고    scopus 로고
    • Proinflammatory activity of glycosylphosphatidylinositol anchors derived from Trypanosoma cruzi: structural and functional analyses
    • Almeida I.C., Gazzinelli R.T. Proinflammatory activity of glycosylphosphatidylinositol anchors derived from Trypanosoma cruzi: structural and functional analyses. J Leukoc Biol 2001, 70:467-477.
    • (2001) J Leukoc Biol , vol.70 , pp. 467-477
    • Almeida, I.C.1    Gazzinelli, R.T.2
  • 21
    • 0034234658 scopus 로고    scopus 로고
    • Functional diversity in the trans-sialidase and mucin families in Trypanosoma cruzi
    • Frasch A.C. Functional diversity in the trans-sialidase and mucin families in Trypanosoma cruzi. Parasitol Today 2000, 16:282-286.
    • (2000) Parasitol Today , vol.16 , pp. 282-286
    • Frasch, A.C.1
  • 22
    • 38349186616 scopus 로고    scopus 로고
    • Isolation, purification, characterization and antigenic evaluation of GPI-anchored membrane proteins from Leishmania (Viannia) braziliensis
    • Rojas A., Garcia-Lugo P., Crisante G., Anez-Rojas N., Anez N. Isolation, purification, characterization and antigenic evaluation of GPI-anchored membrane proteins from Leishmania (Viannia) braziliensis. Acta Trop 2008, 105:139-144.
    • (2008) Acta Trop , vol.105 , pp. 139-144
    • Rojas, A.1    Garcia-Lugo, P.2    Crisante, G.3    Anez-Rojas, N.4    Anez, N.5
  • 23
    • 0031590269 scopus 로고    scopus 로고
    • The surface glycoconjugates of trypanosomatid parasites
    • Ferguson M.A. The surface glycoconjugates of trypanosomatid parasites. Philos Trans R Soc Lond B Biol Sci 1997, 352:1295-1302.
    • (1997) Philos Trans R Soc Lond B Biol Sci , vol.352 , pp. 1295-1302
    • Ferguson, M.A.1
  • 24
    • 0029046678 scopus 로고
    • Role of the Leishmania surface protease gp63 in complement fixation, cell adhesion, and resistance to complement-mediated lysis
    • Brittingham A., Morrison C.J., McMaster W.R., McGwire B.S., Chang K.P., Mosser D.M. Role of the Leishmania surface protease gp63 in complement fixation, cell adhesion, and resistance to complement-mediated lysis. J Immunol 1995, 155:3102-3111.
    • (1995) J Immunol , vol.155 , pp. 3102-3111
    • Brittingham, A.1    Morrison, C.J.2    McMaster, W.R.3    McGwire, B.S.4    Chang, K.P.5    Mosser, D.M.6
  • 26
    • 67249163230 scopus 로고    scopus 로고
    • Genomic organization and expression profile of the mucin-associated surface protein (masp) family of the human pathogen Trypanosoma cruzi
    • Bartholomeu D.C., Cerqueira G.C., Leao A.C., daRocha W.D., Pais F.S., Macedo C., et al. Genomic organization and expression profile of the mucin-associated surface protein (masp) family of the human pathogen Trypanosoma cruzi. Nucleic Acids Res 2009, 37:3407-3417.
    • (2009) Nucleic Acids Res , vol.37 , pp. 3407-3417
    • Bartholomeu, D.C.1    Cerqueira, G.C.2    Leao, A.C.3    daRocha, W.D.4    Pais, F.S.5    Macedo, C.6
  • 29
    • 84866314328 scopus 로고    scopus 로고
    • Trypanosoma cruzi trans-sialidase as a multifunctional enzyme in Chagas' disease
    • Dc-Rubin S.S., Schenkman S. Trypanosoma cruzi trans-sialidase as a multifunctional enzyme in Chagas' disease. Cell Microbiol 2012, 14:1522-1530.
    • (2012) Cell Microbiol , vol.14 , pp. 1522-1530
    • Dc-Rubin, S.S.1    Schenkman, S.2
  • 30
    • 0028958148 scopus 로고
    • Structural characterization of the major glycosylphosphatidylinositol membrane-anchored glycoprotein from epimastigote forms of Trypanosoma cruzi Y-strain
    • Previato J.O., Jones C., Xavier M.T., Wait R., Travassos L.R., Parodi A.J., et al. Structural characterization of the major glycosylphosphatidylinositol membrane-anchored glycoprotein from epimastigote forms of Trypanosoma cruzi Y-strain. J Biol Chem 1995, 270:7241-7250.
    • (1995) J Biol Chem , vol.270 , pp. 7241-7250
    • Previato, J.O.1    Jones, C.2    Xavier, M.T.3    Wait, R.4    Travassos, L.R.5    Parodi, A.J.6
  • 32
    • 78649363018 scopus 로고    scopus 로고
    • Genome survey sequence analysis and identification of homologs of major surface protease (gp63) genes in Trypanosoma rangeli
    • Ferreira K.A., Ruiz J.C., Dias F.C., Lages-Silva E., Tosi L.R., Ramirez L.E., et al. Genome survey sequence analysis and identification of homologs of major surface protease (gp63) genes in Trypanosoma rangeli. Vector Borne Zoonotic Dis 2010, 10:847-853.
    • (2010) Vector Borne Zoonotic Dis , vol.10 , pp. 847-853
    • Ferreira, K.A.1    Ruiz, J.C.2    Dias, F.C.3    Lages-Silva, E.4    Tosi, L.R.5    Ramirez, L.E.6
  • 33
    • 23944472139 scopus 로고    scopus 로고
    • A mucin like gene different from the previously reported members of the mucin like gene families is transcribed in Trypanosoma cruzi but not in Trypanosoma rangeli
    • Abate T., Rincon M., Diaz-Bello Z., Spencer L., Rodriguez-Acosta A. A mucin like gene different from the previously reported members of the mucin like gene families is transcribed in Trypanosoma cruzi but not in Trypanosoma rangeli. Mem Inst Oswaldo Cruz 2005, 100:391-395.
    • (2005) Mem Inst Oswaldo Cruz , vol.100 , pp. 391-395
    • Abate, T.1    Rincon, M.2    Diaz-Bello, Z.3    Spencer, L.4    Rodriguez-Acosta, A.5
  • 34
    • 0007340430 scopus 로고    scopus 로고
    • Trypanosoma rangeli sialidase: kinetics of release and antigenic characterization
    • Saldana A., Sousa O.E., Orn A., Harris R.A. Trypanosoma rangeli sialidase: kinetics of release and antigenic characterization. Acta Trop 1998, 70:87-99.
    • (1998) Acta Trop , vol.70 , pp. 87-99
    • Saldana, A.1    Sousa, O.E.2    Orn, A.3    Harris, R.A.4
  • 36
    • 30644463471 scopus 로고    scopus 로고
    • Isolation, purification and characterization of GPI-anchored membrane proteins from Trypanosoma rangeli and Trypanosoma cruzi
    • Anezrojas N., Garcialugo P., Crisante G., Rojas A., Anez N. Isolation, purification and characterization of GPI-anchored membrane proteins from Trypanosoma rangeli and Trypanosoma cruzi. Acta Trop 2006, 97:140-145.
    • (2006) Acta Trop , vol.97 , pp. 140-145
    • Anezrojas, N.1    Garcialugo, P.2    Crisante, G.3    Rojas, A.4    Anez, N.5
  • 37
    • 67650578607 scopus 로고    scopus 로고
    • Molecular analysis of surface glycoprotein multigene family TrGP expressed on the plasma membrane of Trypanosoma rangeli epimastigotes forms
    • Pena C.P., Lander N., Rodriguez E., Crisante G., Anez N., Ramirez J.L., et al. Molecular analysis of surface glycoprotein multigene family TrGP expressed on the plasma membrane of Trypanosoma rangeli epimastigotes forms. Acta Trop 2009, 111:255-262.
    • (2009) Acta Trop , vol.111 , pp. 255-262
    • Pena, C.P.1    Lander, N.2    Rodriguez, E.3    Crisante, G.4    Anez, N.5    Ramirez, J.L.6
  • 38
    • 0036136392 scopus 로고    scopus 로고
    • Differentiation of Trypanosoma rangeli: high production of infective Trypomastigote forms in vitro
    • Koerich L.B., Emmanuelle-Machado P., Santos K., Grisard E.C., Steindel M. Differentiation of Trypanosoma rangeli: high production of infective Trypomastigote forms in vitro. Parasitol Res 2002, 88:21-25.
    • (2002) Parasitol Res , vol.88 , pp. 21-25
    • Koerich, L.B.1    Emmanuelle-Machado, P.2    Santos, K.3    Grisard, E.C.4    Steindel, M.5
  • 39
    • 0022647936 scopus 로고
    • Stage-specific surface antigens of metacyclic trypomastigotes of Trypanosoma cruzi identified by monoclonal antibodies
    • Teixeira M.M., Yoshida N. Stage-specific surface antigens of metacyclic trypomastigotes of Trypanosoma cruzi identified by monoclonal antibodies. Mol Biochem Parasitol 1986, 18:271-282.
    • (1986) Mol Biochem Parasitol , vol.18 , pp. 271-282
    • Teixeira, M.M.1    Yoshida, N.2
  • 40
    • 67650367143 scopus 로고    scopus 로고
    • Proteomic analysis of detergent-solubilized membrane proteins from insect-developmental forms of Trypanosoma cruzi
    • Cordero E.M., Nakayasu E.S., Gentil L.G., Yoshida N., Almeida I.C., da Silveira J.F. Proteomic analysis of detergent-solubilized membrane proteins from insect-developmental forms of Trypanosoma cruzi. J Proteome Res 2009, 8:3642-3652.
    • (2009) J Proteome Res , vol.8 , pp. 3642-3652
    • Cordero, E.M.1    Nakayasu, E.S.2    Gentil, L.G.3    Yoshida, N.4    Almeida, I.C.5    da Silveira, J.F.6
  • 42
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Emanuelsson O., Brunak S., von Heijne G., Nielsen H. Locating proteins in the cell using TargetP, SignalP and related tools. Nat Protoc 2007, 2:953-971.
    • (2007) Nat Protoc , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 43
    • 34548713371 scopus 로고    scopus 로고
    • FragAnchor: a large-scale predictor of glycosylphosphatidylinositol anchors in eukaryote protein sequences by qualitative scoring
    • Poisson G., Chauve C., Chen X., Bergeron A. FragAnchor: a large-scale predictor of glycosylphosphatidylinositol anchors in eukaryote protein sequences by qualitative scoring. Genomics Proteomics Bioinformatics 2007, 5:121-130.
    • (2007) Genomics Proteomics Bioinformatics , vol.5 , pp. 121-130
    • Poisson, G.1    Chauve, C.2    Chen, X.3    Bergeron, A.4
  • 44
    • 2942564436 scopus 로고    scopus 로고
    • N-terminal myristoylation predictions by ensembles of neural networks
    • Bologna G., Yvon C., Duvaud S., Veuthey A.L. N-terminal myristoylation predictions by ensembles of neural networks. Proteomics 2004, 4:1626-1632.
    • (2004) Proteomics , vol.4 , pp. 1626-1632
    • Bologna, G.1    Yvon, C.2    Duvaud, S.3    Veuthey, A.L.4
  • 45
    • 54249148026 scopus 로고    scopus 로고
    • CSS-Palm 2.0: an updated software for palmitoylation sites prediction
    • Ren J., Wen L., Gao X., Jin C., Xue Y., Yao X. CSS-Palm 2.0: an updated software for palmitoylation sites prediction. Protein Eng Des Sel 2008, 21:639-644.
    • (2008) Protein Eng Des Sel , vol.21 , pp. 639-644
    • Ren, J.1    Wen, L.2    Gao, X.3    Jin, C.4    Xue, Y.5    Yao, X.6
  • 46
    • 0031809552 scopus 로고    scopus 로고
    • NetOglyc: prediction of mucin type O-glycosylation sites based on sequence context and surface accessibility
    • Hansen J.E., Lund O., Tolstrup N., Gooley A.A., Williams K.L., Brunak S. NetOglyc: prediction of mucin type O-glycosylation sites based on sequence context and surface accessibility. Glycoconj J 1998, 15:115-130.
    • (1998) Glycoconj J , vol.15 , pp. 115-130
    • Hansen, J.E.1    Lund, O.2    Tolstrup, N.3    Gooley, A.A.4    Williams, K.L.5    Brunak, S.6
  • 47
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnady G.E., Simon I. The HMMTOP transmembrane topology prediction server. Bioinformatics 2001, 17:849-850.
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 48
    • 25444479978 scopus 로고    scopus 로고
    • Improved profile HMM performance by assessment of critical algorithmic features in SAM and HMMER
    • Wistrand M., Sonnhammer E.L. Improved profile HMM performance by assessment of critical algorithmic features in SAM and HMMER. BMC Bioinformatics 2005, 6:99.
    • (2005) BMC Bioinformatics , vol.6 , pp. 99
    • Wistrand, M.1    Sonnhammer, E.L.2
  • 52
    • 0028869863 scopus 로고
    • Purification of glycosylphosphatidylinositol-anchored proteins by modified triton X-114 partitioning and preparative gel electrophoresis
    • Ko Y.G., Thompson G.A. Purification of glycosylphosphatidylinositol-anchored proteins by modified triton X-114 partitioning and preparative gel electrophoresis. Anal Biochem 1995, 224:166-172.
    • (1995) Anal Biochem , vol.224 , pp. 166-172
    • Ko, Y.G.1    Thompson, G.A.2
  • 54
    • 80054790079 scopus 로고    scopus 로고
    • Genomic analyses, gene expression and antigenic profile of the trans-sialidase superfamily of Trypanosoma cruzi reveal an undetected level of complexity
    • Freitas L.M., dos Santos S.L., Rodrigues-Luiz G.F., Mendes T.A., Rodrigues T.S., Gazzinelli R.T., et al. Genomic analyses, gene expression and antigenic profile of the trans-sialidase superfamily of Trypanosoma cruzi reveal an undetected level of complexity. PLoS One 2011, 6:e25914.
    • (2011) PLoS One , vol.6
    • Freitas, L.M.1    dos Santos, S.L.2    Rodrigues-Luiz, G.F.3    Mendes, T.A.4    Rodrigues, T.S.5    Gazzinelli, R.T.6
  • 56
    • 0141780967 scopus 로고    scopus 로고
    • Gp63 homologues in Trypanosoma cruzi: surface antigens with metalloprotease activity and a possible role in host cell infection. Infection and
    • Cuevas I.C., Cazzulo J.J., Sanchez D.O. gp63 homologues in Trypanosoma cruzi: surface antigens with metalloprotease activity and a possible role in host cell infection. Infection and. Immunity 2003, 71:5739-5749.
    • (2003) Immunity , vol.71 , pp. 5739-5749
    • Cuevas, I.C.1    Cazzulo, J.J.2    Sanchez, D.O.3
  • 57
    • 0022689973 scopus 로고
    • The major surface protein of Leishmania promastigotes is anchored in the membrane by a myristic acid-labeled phospholipid
    • Etges R., Bouvier J., Bordier C. The major surface protein of Leishmania promastigotes is anchored in the membrane by a myristic acid-labeled phospholipid. EMBO J 1986, 5:597-601.
    • (1986) EMBO J , vol.5 , pp. 597-601
    • Etges, R.1    Bouvier, J.2    Bordier, C.3
  • 58
    • 85027926400 scopus 로고    scopus 로고
    • An evolutionary analysis of trypanosomatid GP63 proteases
    • Ma L., Chen K., Meng Q., Liu Q., Tang P., Hu S., et al. An evolutionary analysis of trypanosomatid GP63 proteases. Parasitol Res 2011, 109:1075-1084.
    • (2011) Parasitol Res , vol.109 , pp. 1075-1084
    • Ma, L.1    Chen, K.2    Meng, Q.3    Liu, Q.4    Tang, P.5    Hu, S.6
  • 59
    • 0028818843 scopus 로고
    • The lipid structure of the glycosylphosphatidylinositol-anchored mucin-like sialic acid acceptors of Trypanosoma cruzi changes during parasite differentiation from epimastigotes to infective metacyclic trypomastigote forms
    • Serrano A.A., Schenkman S., Yoshida N., Mehlert A., Richardson J.M., Ferguson M.A. The lipid structure of the glycosylphosphatidylinositol-anchored mucin-like sialic acid acceptors of Trypanosoma cruzi changes during parasite differentiation from epimastigotes to infective metacyclic trypomastigote forms. J Biol Chem 1995, 270:27244-27253.
    • (1995) J Biol Chem , vol.270 , pp. 27244-27253
    • Serrano, A.A.1    Schenkman, S.2    Yoshida, N.3    Mehlert, A.4    Richardson, J.M.5    Ferguson, M.A.6
  • 60
    • 0028670563 scopus 로고
    • Lytic anti-alpha-galactosyl antibodies from patients with chronic Chagas' disease recognize novel O-linked oligosaccharides on mucin-like glycosyl-phosphatidylinositol-anchored glycoproteins of Trypanosoma cruzi
    • Almeida I.C., Ferguson M.A., Schenkman S., Travassos L.R. Lytic anti-alpha-galactosyl antibodies from patients with chronic Chagas' disease recognize novel O-linked oligosaccharides on mucin-like glycosyl-phosphatidylinositol-anchored glycoproteins of Trypanosoma cruzi. Biochem J 1994, 304(Pt 3):793-802.
    • (1994) Biochem J , vol.304 , Issue.PART 3 , pp. 793-802
    • Almeida, I.C.1    Ferguson, M.A.2    Schenkman, S.3    Travassos, L.R.4
  • 62
    • 0032079885 scopus 로고    scopus 로고
    • The Trypanosoma cruzi mucin family is transcribed from hundreds of genes having hypervariable regions
    • Di Noia J.M., D'Orso I., Aslund L., Sanchez D.O., Frasch A.C. The Trypanosoma cruzi mucin family is transcribed from hundreds of genes having hypervariable regions. J Biol Chem 1998, 273:10843-10850.
    • (1998) J Biol Chem , vol.273 , pp. 10843-10850
    • Di Noia, J.M.1    D'Orso, I.2    Aslund, L.3    Sanchez, D.O.4    Frasch, A.C.5
  • 63
    • 80051677176 scopus 로고    scopus 로고
    • Molecular diversity of the Trypanosoma cruzi TcSMUG family of mucin genes and proteins
    • Urban I., Santurio L.B., Chidichimo A., Yu H., Chen X., Mucci J., et al. Molecular diversity of the Trypanosoma cruzi TcSMUG family of mucin genes and proteins. Biochem J 2011, 438:303-313.
    • (2011) Biochem J , vol.438 , pp. 303-313
    • Urban, I.1    Santurio, L.B.2    Chidichimo, A.3    Yu, H.4    Chen, X.5    Mucci, J.6
  • 64
    • 0032774770 scopus 로고    scopus 로고
    • Immunization of mice with a TolA-like surface protein of Trypanosoma cruzi generates CD4(+) T-cell-dependent parasiticidal activity
    • Quanquin N.M., Galaviz C., Fouts D.L., Wrightsman R.A., Manning J.E. Immunization of mice with a TolA-like surface protein of Trypanosoma cruzi generates CD4(+) T-cell-dependent parasiticidal activity. Infect Immun 1999, 67:4603-4612.
    • (1999) Infect Immun , vol.67 , pp. 4603-4612
    • Quanquin, N.M.1    Galaviz, C.2    Fouts, D.L.3    Wrightsman, R.A.4    Manning, J.E.5
  • 65
    • 47749140011 scopus 로고    scopus 로고
    • Vaccination with epimastigotes of different strains of Trypanosoma rangeli protects mice against Trypanosoma cruzi infection
    • Basso B., Moretti E., Fretes R. Vaccination with epimastigotes of different strains of Trypanosoma rangeli protects mice against Trypanosoma cruzi infection. Mem Inst Oswaldo Cruz 2008, 103:370-374.
    • (2008) Mem Inst Oswaldo Cruz , vol.103 , pp. 370-374
    • Basso, B.1    Moretti, E.2    Fretes, R.3
  • 66
    • 0027158311 scopus 로고
    • Deletion of an immunodominant Trypanosoma cruzi surface glycoprotein disrupts flagellum-cell adhesion
    • Cooper R., de Jesus A.R., Cross G.A. Deletion of an immunodominant Trypanosoma cruzi surface glycoprotein disrupts flagellum-cell adhesion. J Cell Biol 1993, 122:149-156.
    • (1993) J Cell Biol , vol.122 , pp. 149-156
    • Cooper, R.1    de Jesus, A.R.2    Cross, G.A.3
  • 67
    • 0030602236 scopus 로고    scopus 로고
    • Characterization of the Trypanosoma brucei homologue of a Trypanosoma cruzi flagellum-adhesion glycoprotein
    • Nozaki T., Haynes P.A., Cross G.A. Characterization of the Trypanosoma brucei homologue of a Trypanosoma cruzi flagellum-adhesion glycoprotein. Mol Biochem Parasitol 1996, 82:245-255.
    • (1996) Mol Biochem Parasitol , vol.82 , pp. 245-255
    • Nozaki, T.1    Haynes, P.A.2    Cross, G.A.3
  • 68
    • 0037124117 scopus 로고    scopus 로고
    • Trypanosoma brucei FLA1 is required for flagellum attachment and cytokinesis
    • LaCount D.J., Barrett B., Donelson J.E. Trypanosoma brucei FLA1 is required for flagellum attachment and cytokinesis. J Biol Chem 2002, 277:17580-17588.
    • (2002) J Biol Chem , vol.277 , pp. 17580-17588
    • LaCount, D.J.1    Barrett, B.2    Donelson, J.E.3
  • 69
    • 0030561125 scopus 로고    scopus 로고
    • Trypanosoma rangeli and Trypanosoma cruzi: molecular characterization of genes encoding putative calcium-binding proteins, highly conserved in trypanosomatids
    • Porcel B.M., Bontempi E.J., Henriksson J., Rydaker M., Aslund L., Segura E.L., et al. Trypanosoma rangeli and Trypanosoma cruzi: molecular characterization of genes encoding putative calcium-binding proteins, highly conserved in trypanosomatids. Exp Parasitol 1996, 84:387-399.
    • (1996) Exp Parasitol , vol.84 , pp. 387-399
    • Porcel, B.M.1    Bontempi, E.J.2    Henriksson, J.3    Rydaker, M.4    Aslund, L.5    Segura, E.L.6
  • 70
    • 0033560770 scopus 로고    scopus 로고
    • Flagellar protein localization mediated by a calcium-myristoyl/palmitoyl switch mechanism
    • Godsel L.M., Engman D.M. Flagellar protein localization mediated by a calcium-myristoyl/palmitoyl switch mechanism. EMBO J 1999, 18:2057-2065.
    • (1999) EMBO J , vol.18 , pp. 2057-2065
    • Godsel, L.M.1    Engman, D.M.2
  • 71
    • 0028290129 scopus 로고
    • T-cell responses to the trypanosome variant surface glycoprotein: a new paradigm?
    • Mansfield J.M. T-cell responses to the trypanosome variant surface glycoprotein: a new paradigm?. Parasitol Today 1994, 10:267-270.
    • (1994) Parasitol Today , vol.10 , pp. 267-270
    • Mansfield, J.M.1
  • 72
    • 0025296687 scopus 로고
    • T-cell-independent and T-cell-dependent B-cell responses to exposed variant surface glycoprotein epitopes in trypanosome-infected mice
    • Reinitz D.M., Mansfield J.M. T-cell-independent and T-cell-dependent B-cell responses to exposed variant surface glycoprotein epitopes in trypanosome-infected mice. Infect Immun 1990, 58:2337-2342.
    • (1990) Infect Immun , vol.58 , pp. 2337-2342
    • Reinitz, D.M.1    Mansfield, J.M.2
  • 73
    • 0034834670 scopus 로고    scopus 로고
    • Excretory-secretory antigens of Trypanosoma cruzi are potentially useful for serodiagnosis of chronic Chagas' disease
    • Nakazawa M., Rosa D.S., Pereira V.R., Moura M.O., Furtado V.C., Souza W.V., et al. Excretory-secretory antigens of Trypanosoma cruzi are potentially useful for serodiagnosis of chronic Chagas' disease. Clin Diagn Lab Immunol 2001, 8:1024-1027.
    • (2001) Clin Diagn Lab Immunol , vol.8 , pp. 1024-1027
    • Nakazawa, M.1    Rosa, D.S.2    Pereira, V.R.3    Moura, M.O.4    Furtado, V.C.5    Souza, W.V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.