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Volumn 4, Issue 1, 2010, Pages 4-16

Proteomic examination of Leishmania chagasi plasma membrane proteins: Contrast between avirulent and virulent (metacyclic) parasite forms

Author keywords

Leishmania; Metacyclic promastigotes; Plasma membrane proteins

Indexed keywords

ACYL CARRIER PROTEIN; ALPHA TUBULIN; AMINOACYLASE; BETA TUBULIN; CALMODULIN; CITRATE SYNTHASE; CYSTEINE PROTEINASE; CYTOCHROME C OXIDASE; CYTOSKELETON PROTEIN; DETERGENT; DYNEIN ADENOSINE TRIPHOSPHATASE; ENOLASE; FRUCTOSE BISPHOSPHATE ALDOLASE; HEAT SHOCK PROTEIN; INITIATION FACTOR; LONG CHAIN FATTY ACID COENZYME A LIGASE; MEMBRANE PROTEIN; METHIONINE TRANSFER RNA LIGASE; NUCLEOSIDE DIPHOSPHATE KINASE; OCTYL GLUCOSIDE; PHOSPHOGLUCONATE DEHYDROGENASE; POLYADENYLIC ACID BINDING PROTEIN; PROTEIN DNAJ; PROTEINASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; RNA HELICASE; STREPTAVIDIN; UBIQUITIN; VIRULENCE FACTOR;

EID: 77951716020     PISSN: 18628346     EISSN: 18628354     Source Type: Journal    
DOI: 10.1002/prca.200900050     Document Type: Article
Times cited : (23)

References (46)
  • 1
    • 34447264232 scopus 로고    scopus 로고
    • Transmission of Leishmania metacyclic promastigotes by phlebotomine sand flies
    • Bates, P.A., Transmission of Leishmania metacyclic promastigotes by phlebotomine sand flies. Int. J. Parasitol. 2007, 37, 1097-1106.
    • (2007) Int. J. Parasitol. , vol.37 , pp. 1097-1106
    • Bates, P.A.1
  • 2
    • 0023616650 scopus 로고
    • Metacyclogenesis is a major determinant of Leishmania promastigote virulence and attenuation
    • da Silva, R., Sacks, D.L., Metacyclogenesis is a major determinant of Leishmania promastigote virulence and attenuation. Infect. Immun. 1987, 55, 2802-2806.
    • (1987) Infect. Immun. , vol.55 , pp. 2802-2806
    • da Silva, R.1    Sacks, D.L.2
  • 3
    • 0024390249 scopus 로고
    • Metacyclogenesis in Leishmania promastigotes
    • Sacks, D.L., Metacyclogenesis in Leishmania promastigotes. Exp. Parasitol. 1989, 69, 100-103.
    • (1989) Exp. Parasitol. , vol.69 , pp. 100-103
    • Sacks, D.L.1
  • 4
    • 0035669096 scopus 로고    scopus 로고
    • A lipophosphoglycan-independent method for isolation of infective Leishmania metacyclic promastigotes by density gradient centrifugation
    • Spath, G.F., Beverley, S.M., A lipophosphoglycan-independent method for isolation of infective Leishmania metacyclic promastigotes by density gradient centrifugation. Exp. Parasitol. 2001, 99, 97-103.
    • (2001) Exp. Parasitol. , vol.99 , pp. 97-103
    • Spath, G.F.1    Beverley, S.M.2
  • 5
    • 31344480960 scopus 로고    scopus 로고
    • Interplay between parasite cysteine proteases and the host kinin system modulates microvascular leakage and macrophage infection by promastigotes of the Leishmania donovani complex
    • Svensjo, E., Batista, P.R., Brodskyn, C.I., Silva, R. et al., Interplay between parasite cysteine proteases and the host kinin system modulates microvascular leakage and macrophage infection by promastigotes of the Leishmania donovani complex. Microbes Infect. 2006, 8, 206-220.
    • (2006) Microbes Infect , vol.8 , pp. 206-220
    • Svensjo, E.1    Batista, P.R.2    Brodskyn, C.I.3    Silva, R.4
  • 6
    • 37349017579 scopus 로고    scopus 로고
    • Leishmania chagasi: homogenous metacyclic promastigotes isolated by buoyant density are highly virulent in a mouse model
    • Yao, C., Chen, Y., Sudan, B., Donelson, J.E., Wilson, M.E., Leishmania chagasi: homogenous metacyclic promastigotes isolated by buoyant density are highly virulent in a mouse model. Exp. Parasitol. 2008, 118, 129-133.
    • (2008) Exp. Parasitol. , vol.118 , pp. 129-133
    • Yao, C.1    Chen, Y.2    Sudan, B.3    Donelson, J.E.4    Wilson, M.E.5
  • 8
    • 77951701710 scopus 로고    scopus 로고
    • Myler, P., Fasel, N. (Eds.), Caister Academic Press, Norfolk, UK
    • Sacks, D., Lawyer, P., Kamhawi, S., in: Myler, P., Fasel, N. (Eds.), Leishmania After the Genome, Caister Academic Press, Norfolk, UK 2008, pp. 205-238.
    • (2008) Leishmania After the Genome , pp. 205-238
    • Sacks, D.1    Lawyer, P.2    Kamhawi, S.3
  • 9
    • 0026744781 scopus 로고
    • Developmental modification of lipophosphoglycan during the differentiation of Leishmania major promastigotes to an infectious stage
    • McConville, M.J., Turco, S.J., Ferguson, M.A., Sacks, D.L., Developmental modification of lipophosphoglycan during the differentiation of Leishmania major promastigotes to an infectious stage. EMBO J. 1992, 11, 3593-3600.
    • (1992) EMBO J , vol.11 , pp. 3593-3600
    • McConville, M.J.1    Turco, S.J.2    Ferguson, M.A.3    Sacks, D.L.4
  • 10
    • 0036803115 scopus 로고    scopus 로고
    • Leishmania (Viannia) braziliensis metacyclic promastigotes purified using Bauhinia purpurea lectin are complement resistant and highly infective for macrophages in vitro and hamsters in vivo
    • Pinto-da-Silva, L.H., Camurate, M., Costa, K.A., Oliveira, S.M. et al., Leishmania (Viannia) braziliensis metacyclic promastigotes purified using Bauhinia purpurea lectin are complement resistant and highly infective for macrophages in vitro and hamsters in vivo. Int. J. Parasitol. 2002, 32, 1371-1377.
    • (2002) Int. J. Parasitol. , vol.32 , pp. 1371-1377
    • Pinto-da-Silva, L.H.1    Camurate, M.2    Costa, K.A.3    Oliveira, S.M.4
  • 11
    • 0028963375 scopus 로고
    • Stage-specific binding of Leishmania donovani to the sand fly vector midgut is regulated by conformational changes in the abundant surface lipophosphoglycan
    • Sacks, D.L., Pimenta, P.F., McConville, M.J., Schneider, P., Turco, S.J., Stage-specific binding of Leishmania donovani to the sand fly vector midgut is regulated by conformational changes in the abundant surface lipophosphoglycan. J. Exp. Med. 1995, 181, 685-697.
    • (1995) J. Exp. Med. , vol.181 , pp. 685-697
    • Sacks, D.L.1    Pimenta, P.F.2    McConville, M.J.3    Schneider, P.4    Turco, S.J.5
  • 13
    • 0141888314 scopus 로고    scopus 로고
    • The major surface protease (MSP or GP63) of Leishmania sp. Biosynthesis, regulation of expression, and function
    • Yao, C., Donelson, J.E., Wilson, M.E., The major surface protease (MSP or GP63) of Leishmania sp. Biosynthesis, regulation of expression, and function. Mol. Biochem. Parasitol. 2003, 132, 1-16.
    • (2003) Mol. Biochem. Parasitol. , vol.132 , pp. 1-16
    • Yao, C.1    Donelson, J.E.2    Wilson, M.E.3
  • 14
    • 0023752833 scopus 로고
    • The major concanavalin A-binding surface glycoprotein of Leishmania donovani chagasi promastigotes is involved in attachment to human macrophages
    • Wilson, M.E., Hardin, K.K., The major concanavalin A-binding surface glycoprotein of Leishmania donovani chagasi promastigotes is involved in attachment to human macrophages. J. Immunol. 1988, 141, 265-272.
    • (1988) J. Immunol. , vol.141 , pp. 265-272
    • Wilson, M.E.1    Hardin, K.K.2
  • 15
    • 35348923020 scopus 로고    scopus 로고
    • Internal and surface-localized MSP of Leishmania and their differential release from promastigotes
    • Yao, C., Donelson, J.E., Wilson, M.E., Internal and surface-localized MSP of Leishmania and their differential release from promastigotes. Eukaryot. Cell 2007, 6, 1905-1912.
    • (2007) Eukaryot. Cell. , vol.6 , pp. 1905-1912
    • Yao, C.1    Donelson, J.E.2    Wilson, M.E.3
  • 16
    • 12344252118 scopus 로고    scopus 로고
    • Internal and surface subpopulations of the major surface protease (MSP) of Leishmania chagasi
    • Yao, C., Luo, J., Hsiao, C., Donelson, J.E., Wilson, M.E., Internal and surface subpopulations of the major surface protease (MSP) of Leishmania chagasi. Mol. Biochem. Parasitol. 2005, 139, 173-183.
    • (2005) Mol. Biochem. Parasitol. , vol.139 , pp. 173-183
    • Yao, C.1    Luo, J.2    Hsiao, C.3    Donelson, J.E.4    Wilson, M.E.5
  • 17
    • 1942542161 scopus 로고    scopus 로고
    • Multiple products of the Leishmania chagasi major surface protease (MSP or GP63) gene family
    • Yao, C., Luo, J., Storlie, P., Donelson, J.E., Wilson, M.E., Multiple products of the Leishmania chagasi major surface protease (MSP or GP63) gene family. Mol. Biochem. Parasitol. 2004, 135, 171-183.
    • (2004) Mol. Biochem. Parasitol. , vol.135 , pp. 171-183
    • Yao, C.1    Luo, J.2    Storlie, P.3    Donelson, J.E.4    Wilson, M.E.5
  • 18
    • 0022652645 scopus 로고
    • The involvement of the major surface glycoprotein (gp63) of Leishmania promastigotes in attachment to macrophages
    • Russell, D.G., Wilhelm, H., The involvement of the major surface glycoprotein (gp63) of Leishmania promastigotes in attachment to macrophages. J. Immunol. 1986, 136, 2613-2620.
    • (1986) J. Immunol. , vol.136 , pp. 2613-2620
    • Russell, D.G.1    Wilhelm, H.2
  • 19
    • 0024395616 scopus 로고
    • Expression of the major surface glycoprotein of Leishmania donovani chagasi in virulent and attenuated promastigotes
    • Wilson, M.E., Hardin, K.K., Donelson, J.E., Expression of the major surface glycoprotein of Leishmania donovani chagasi in virulent and attenuated promastigotes. J. Immunol. 1989, 143, 678-684.
    • (1989) J. Immunol. , vol.143 , pp. 678-684
    • Wilson, M.E.1    Hardin, K.K.2    Donelson, J.E.3
  • 20
    • 0027975364 scopus 로고
    • Identification by extrachromosomal amplification and overexpression of a zeta-crystallin/NADPH-oxidoreductase homologue constitutively expressed in Leishmania spp
    • Liu, X., Chang, K.P., Identification by extrachromosomal amplification and overexpression of a zeta-crystallin/NADPH-oxidoreductase homologue constitutively expressed in Leishmania spp. Mol. Biochem. Parasitol. 1994, 66, 201-210.
    • (1994) Mol. Biochem. Parasitol. , vol.66 , pp. 201-210
    • Liu, X.1    Chang, K.P.2
  • 21
    • 22244441812 scopus 로고    scopus 로고
    • The genome of the African trypanosome Trypanosoma brucei
    • Berriman, M., Ghedin, E., Hertz-Fowler, C., Blandin, G. et al., The genome of the African trypanosome Trypanosoma brucei. Science 2005, 309, 416-422.
    • (2005) Science , vol.309 , pp. 416-422
    • Berriman, M.1    Ghedin, E.2    Hertz-Fowler, C.3    Blandin, G.4
  • 22
    • 22244453726 scopus 로고    scopus 로고
    • The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas disease
    • El-Sayed, N.M., Myler, P.J., Bartholomeu, D.C., Nilsson, D. et al., The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas disease. Science 2005, 309, 409-415.
    • (2005) Science , vol.309 , pp. 409-415
    • El-Sayed, N.M.1    Myler, P.J.2    Bartholomeu, D.C.3    Nilsson, D.4
  • 23
    • 22244437571 scopus 로고    scopus 로고
    • The genome of the kinetoplastid parasite, Leishmania major
    • Ivens, A.C., Peacock, C.S., Worthey, E.A., Murphy, L. et al., The genome of the kinetoplastid parasite, Leishmania major. Science 2005, 309, 436-442.
    • (2005) Science , vol.309 , pp. 436-442
    • Ivens, A.C.1    Peacock, C.S.2    Worthey, E.A.3    Murphy, L.4
  • 24
    • 34347339518 scopus 로고    scopus 로고
    • Comparative genomic analysis of three Leishmania species that cause diverse human disease
    • Peacock, C.S., Seeger, K., Harris, D., Murphy, L. et al., Comparative genomic analysis of three Leishmania species that cause diverse human disease. Nat. Genet. 2007, 39, 839-847.
    • (2007) Nat. Genet. , vol.39 , pp. 839-847
    • Peacock, C.S.1    Seeger, K.2    Harris, D.3    Murphy, L.4
  • 26
    • 34447580876 scopus 로고    scopus 로고
    • Subcellular proteomics of cell differentiation: quantitative analysis of the plasma membrane proteome of Caco-2 cells
    • Pshezhetsky, A.V., Fedjaev, M., Ashmarina, L., Mazur, A. et al., Subcellular proteomics of cell differentiation: quantitative analysis of the plasma membrane proteome of Caco-2 cells. Proteomics 2007, 7, 2201-2215.
    • (2007) Proteomics , vol.7 , pp. 2201-2215
    • Pshezhetsky, A.V.1    Fedjaev, M.2    Ashmarina, L.3    Mazur, A.4
  • 28
    • 34247255381 scopus 로고    scopus 로고
    • Identifying the membrane proteome of HIV-1 latently infected cells
    • Berro, R., de la Fuente, C., Klase, Z., Kehn, K. et al., Identifying the membrane proteome of HIV-1 latently infected cells. J. Biol. Chem. 2007, 282, 8207-8218.
    • (2007) J. Biol. Chem. , vol.282 , pp. 8207-8218
    • Berro, R.1    de la Fuente, C.2    Klase, Z.3    Kehn, K.4
  • 29
    • 33748760583 scopus 로고    scopus 로고
    • Proteomic profiling and identification of immunodominant spore antigens of Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis
    • Delvecchio, V.G., Connolly, J.P., Alefantis, T.G., Walz, A. et al., Proteomic profiling and identification of immunodominant spore antigens of Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis. Appl. Environ. Microbiol. 2006, 72, 6355-6363.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 6355-6363
    • Delvecchio, V.G.1    Connolly, J.P.2    Alefantis, T.G.3    Walz, A.4
  • 30
    • 23044451178 scopus 로고    scopus 로고
    • A twodimensional electrophoretic map of human mitochondrial proteins from immortalized lymphoblastoid cell lines: A prerequisite to study mitochondrial disorders in patients
    • Xie, J., Techritz, S., Haebel, S., Horn, A. et al., A twodimensional electrophoretic map of human mitochondrial proteins from immortalized lymphoblastoid cell lines: A prerequisite to study mitochondrial disorders in patients. Proteomics 2005, 5, 2981-2999.
    • (2005) Proteomics , vol.5 , pp. 2981-2999
    • Xie, J.1    Techritz, S.2    Haebel, S.3    Horn, A.4
  • 32
    • 0142244518 scopus 로고    scopus 로고
    • Profiling of the cell surface proteome
    • Jang, J.H., Hanash, S., Profiling of the cell surface proteome. Proteomics 2003, 3, 1947-1954.
    • (2003) Proteomics , vol.3 , pp. 1947-1954
    • Jang, J.H.1    Hanash, S.2
  • 33
    • 0037008715 scopus 로고    scopus 로고
    • Identification of surface proteins of Helicobacter pylori by selective biotinylation, affinity purification, and two-dimensional gel electrophoresis
    • Sabarth, N., Lamer, S., Zimny-Arndt, U., Jungblut, P.R. et al., Identification of surface proteins of Helicobacter pylori by selective biotinylation, affinity purification, and two-dimensional gel electrophoresis. J. Biol. Chem. 2002, 277, 27896-27902.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27896-27902
    • Sabarth, N.1    Lamer, S.2    Zimny-Arndt, U.3    Jungblut, P.R.4
  • 34
    • 0037470247 scopus 로고    scopus 로고
    • Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function
    • Shin, B.K., Wang, H., Yim, A.M., Le Naour, F. et al., Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function. J. Biol. Chem. 2003, 278, 7607-7616.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7607-7616
    • Shin, B.K.1    Wang, H.2    Yim, A.M.3    Le Naour, F.4
  • 35
    • 0347134596 scopus 로고    scopus 로고
    • Affinity enrichment of plasma membrane for proteomics analysis
    • Zhang, W., Zhou, G., Zhao, Y., White, M.A., Affinity enrichment of plasma membrane for proteomics analysis. Electrophoresis 2003, 24, 2855-2863.
    • (2003) Electrophoresis , vol.24 , pp. 2855-2863
    • Zhang, W.1    Zhou, G.2    Zhao, Y.3    White, M.A.4
  • 36
    • 1842529218 scopus 로고    scopus 로고
    • Proteomic analysis of integral plasmamembrane proteins
    • Zhao, Y., Zhang, W., Kho, Y., Proteomic analysis of integral plasmamembrane proteins. Anal. Chem. 2004, 76, 1817-1823.
    • (2004) Anal. Chem. , vol.76 , pp. 1817-1823
    • Zhao, Y.1    Zhang, W.2    Kho, Y.3
  • 37
    • 38149099329 scopus 로고    scopus 로고
    • Characterisation of the plasma membrane subproteome of bloodstream form Trypanosoma brucei
    • Bridges, D.J., Pitt, A.R., Hanrahan, O., Brennan, K. et al., Characterisation of the plasma membrane subproteome of bloodstream form Trypanosoma brucei. Proteomics 2008, 8, 83-99.
    • (2008) Proteomics , vol.8 , pp. 83-99
    • Bridges, D.J.1    Pitt, A.R.2    Hanrahan, O.3    Brennan, K.4
  • 38
    • 34247870811 scopus 로고    scopus 로고
    • Genetic and proteomic evidences support the localization of yeast enolase in the cell surface
    • Lopez-Villar, E., Monteoliva, L., Larsen, M.R., Sachon, E. et al., Genetic and proteomic evidences support the localization of yeast enolase in the cell surface. Proteomics 2006, 6, S107-S118.
    • (2006) Proteomics , vol.6
    • Lopez-Villar, E.1    Monteoliva, L.2    Larsen, M.R.3    Sachon, E.4
  • 39
    • 0025819231 scopus 로고
    • Role of cell-surface lysines in plasminogen binding to cells: identification of alpha-enolase as a candidate plasminogen receptor
    • Miles, L.A., Dahlberg, C.M., Plescia, J., Felez, J. et al., Role of cell-surface lysines in plasminogen binding to cells: identification of alpha-enolase as a candidate plasminogen receptor. Biochemistry 1991, 30, 1682-1691.
    • (1991) Biochemistry , vol.30 , pp. 1682-1691
    • Miles, L.A.1    Dahlberg, C.M.2    Plescia, J.3    Felez, J.4
  • 40
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional alpha-enolase: its role in diseases
    • Pancholi, V., Multifunctional alpha-enolase: its role in diseases. Cell. Mol. Life Sci. 2001, 58, 902-920.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 902-920
    • Pancholi, V.1
  • 41
    • 0032486286 scopus 로고    scopus 로고
    • alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • Pancholi, V., Fischetti, V.A., alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J. Biol. Chem. 1998, 273, 14503-14515.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 42
    • 34248212625 scopus 로고    scopus 로고
    • Leishmania mexicana: molecular cloning and characterization of enolase
    • Quinones, W., Pena, P., Domingo-Sananes, M., Caceres, A. et al., Leishmania mexicana: molecular cloning and characterization of enolase. Exp. Parasitol. 2007, 116, 241-251.
    • (2007) Exp. Parasitol. , vol.116 , pp. 241-251
    • Quinones, W.1    Pena, P.2    Domingo-Sananes, M.3    Caceres, A.4
  • 43
    • 0026738957 scopus 로고
    • Stereo views and immunogold labeling of the pellicular microtubules at the inner surface of the plasma membrane of Leishmania as revealed by fracture-flip
    • Hou, W.Y., Pimenta, P.F., Shen, R.L., Da Silva, P.P., Stereo views and immunogold labeling of the pellicular microtubules at the inner surface of the plasma membrane of Leishmania as revealed by fracture-flip. J. Histochem. Cytochem. 1992, 40, 1309-1318.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 1309-1318
    • Hou, W.Y.1    Pimenta, P.F.2    Shen, R.L.3    Da Silva, P.P.4
  • 44
    • 0023872337 scopus 로고
    • A 60-kDa cytoskeletal protein from Trypanosoma brucei brucei can interact with membranes and with microtubules
    • Seebeck, T., Kung, V., Wyler, T., Muller, M., A 60-kDa cytoskeletal protein from Trypanosoma brucei brucei can interact with membranes and with microtubules. Proc. Natl. Acad. Sci. USA 1988, 85, 1101-1104.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1101-1104
    • Seebeck, T.1    Kung, V.2    Wyler, T.3    Muller, M.4
  • 45
    • 0034895593 scopus 로고    scopus 로고
    • CAP5.5, a life-cycleregulated, cytoskeleton-associated protein is a member of a novel family of calpain-related proteins in Trypanosoma brucei
    • Hertz-Fowler, C., Ersfeld, K., Gull, K., CAP5.5, a life-cycleregulated, cytoskeleton-associated protein is a member of a novel family of calpain-related proteins in Trypanosoma brucei. Mol. Biochem. Parasitol. 2001, 116, 25-34.
    • (2001) Mol. Biochem. Parasitol. , vol.116 , pp. 25-34
    • Hertz-Fowler, C.1    Ersfeld, K.2    Gull, K.3


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