메뉴 건너뛰기




Volumn 26, Issue 5, 2010, Pages 244-254

Production of recombinant proteins from protozoan parasites

Author keywords

[No Author keywords available]

Indexed keywords

RECOMBINANT PROTEIN; RECOMBINANT VACCINE; DIAGNOSTIC AGENT; PROTOZOAL PROTEIN; PROTOZOAL VACCINE;

EID: 77956398026     PISSN: 14714922     EISSN: 14715007     Source Type: Journal    
DOI: 10.1016/j.pt.2010.02.004     Document Type: Review
Times cited : (50)

References (88)
  • 1
    • 65549153047 scopus 로고    scopus 로고
    • Selection of targets for drug development against protozoan parasites
    • de Azevedo W.F., Soares M.B. Selection of targets for drug development against protozoan parasites. Curr. Drug Targets 2009, 10:193-201.
    • (2009) Curr. Drug Targets , vol.10 , pp. 193-201
    • de Azevedo, W.F.1    Soares, M.B.2
  • 2
    • 53649099798 scopus 로고    scopus 로고
    • The sequencing shakeup
    • Coombs A. The sequencing shakeup. Nat. Biotechnol. 2008, 26:1109-1112.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1109-1112
    • Coombs, A.1
  • 3
    • 41849125318 scopus 로고    scopus 로고
    • Malaria: progress, perils, and prospects for eradication
    • Greenwood B.M., et al. Malaria: progress, perils, and prospects for eradication. J. Clin. Invest. 2008, 118:1266-1276.
    • (2008) J. Clin. Invest. , vol.118 , pp. 1266-1276
    • Greenwood, B.M.1
  • 5
    • 51049111849 scopus 로고    scopus 로고
    • Evaluation of Theileria annulata recombinant immunodominant proteins for the development of ELISA
    • Seitzer U., et al. Evaluation of Theileria annulata recombinant immunodominant proteins for the development of ELISA. Transbound. Emerg. Dis. 2008, 55:244-248.
    • (2008) Transbound. Emerg. Dis. , vol.55 , pp. 244-248
    • Seitzer, U.1
  • 6
    • 33747185420 scopus 로고    scopus 로고
    • Effect of sequence variation in Plasmodium falciparum histidine-rich protein 2 on binding of specific monoclonal antibodies: implications for rapid diagnostic tests for malaria
    • Lee N., et al. Effect of sequence variation in Plasmodium falciparum histidine-rich protein 2 on binding of specific monoclonal antibodies: implications for rapid diagnostic tests for malaria. J. Clin. Microbiol. 2006, 44:2773-2778.
    • (2006) J. Clin. Microbiol. , vol.44 , pp. 2773-2778
    • Lee, N.1
  • 7
    • 50149116148 scopus 로고    scopus 로고
    • International meeting: new diagnostic tests are urgently needed to treat patients with Chagas disease
    • Anon.
    • Anon. (2008) International meeting: new diagnostic tests are urgently needed to treat patients with Chagas disease. Rev. Soc. Bras. Med. Trop. 41, 315-319.
    • (2008) Rev. Soc. Bras. Med. Trop. , vol.41 , pp. 315-319
  • 8
    • 48349090695 scopus 로고    scopus 로고
    • Babesiosis: recent insights into an ancient disease
    • Hunfeld K.P., et al. Babesiosis: recent insights into an ancient disease. Int. J. Parasitol. 2008, 38:1219-1237.
    • (2008) Int. J. Parasitol. , vol.38 , pp. 1219-1237
    • Hunfeld, K.P.1
  • 10
    • 34247545662 scopus 로고    scopus 로고
    • Obstacles to the development of a safe and effective attenuated pre-erythrocytic stage malaria vaccine
    • Ripley Ballou W. Obstacles to the development of a safe and effective attenuated pre-erythrocytic stage malaria vaccine. Microbes Infect. 2007, 9:761-766.
    • (2007) Microbes Infect. , vol.9 , pp. 761-766
    • Ripley Ballou, W.1
  • 11
    • 64549142857 scopus 로고    scopus 로고
    • Estimating novel potential drug targets of Plasmodium falciparum by analysing the metabolic network of knock-out strains in silico
    • Fatumo S., et al. Estimating novel potential drug targets of Plasmodium falciparum by analysing the metabolic network of knock-out strains in silico. Infect. Genet. Evol. 2009, 9:351-358.
    • (2009) Infect. Genet. Evol. , vol.9 , pp. 351-358
    • Fatumo, S.1
  • 12
    • 77951209588 scopus 로고    scopus 로고
    • Homology modeling and atomic level binding study of Leishmania MAPK with inhibitors
    • Awale M., et al. Homology modeling and atomic level binding study of Leishmania MAPK with inhibitors. J. Mol. Model. 2009, 16:475-488.
    • (2009) J. Mol. Model. , vol.16 , pp. 475-488
    • Awale, M.1
  • 13
    • 44349136870 scopus 로고    scopus 로고
    • The plastid-like organelle of apicomplexan parasites as drug target
    • Wiesner J., et al. The plastid-like organelle of apicomplexan parasites as drug target. Curr. Pharm. Des. 2008, 14:855-871.
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 855-871
    • Wiesner, J.1
  • 14
    • 56649090952 scopus 로고    scopus 로고
    • Inhibitors of tubulin assembly identified through screening a compound library
    • Morgan R.E., et al. Inhibitors of tubulin assembly identified through screening a compound library. Chem. Biol. Drug Des. 2008, 72:513-524.
    • (2008) Chem. Biol. Drug Des. , vol.72 , pp. 513-524
    • Morgan, R.E.1
  • 15
    • 33749245660 scopus 로고    scopus 로고
    • Inhibitors of Plasmodium falciparum methionine aminopeptidase 1b possess antimalarial activity
    • Chen X., et al. Inhibitors of Plasmodium falciparum methionine aminopeptidase 1b possess antimalarial activity. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:14548-14553.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 14548-14553
    • Chen, X.1
  • 16
    • 70349901077 scopus 로고    scopus 로고
    • High-throughput crystallography for structural genomics
    • Joachimiak A. High-throughput crystallography for structural genomics. Curr. Opin. Struct. Biol. 2009, 19:573-584.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 573-584
    • Joachimiak, A.1
  • 17
    • 58049219752 scopus 로고    scopus 로고
    • Identification and characterization of small molecule inhibitors of Plasmodium falciparum dihydroorotate dehydrogenase
    • Patel V., et al. Identification and characterization of small molecule inhibitors of Plasmodium falciparum dihydroorotate dehydrogenase. J. Biol. Chem. 2008, 283:35078-35085.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35078-35085
    • Patel, V.1
  • 18
    • 16244415171 scopus 로고    scopus 로고
    • Process development and analysis of liver-stage antigen 1, a preerythrocyte-stage protein-based vaccine for Plasmodium falciparum
    • Hillier C.J., et al. Process development and analysis of liver-stage antigen 1, a preerythrocyte-stage protein-based vaccine for Plasmodium falciparum. Infect. Immun. 2005, 73:2109-2115.
    • (2005) Infect. Immun. , vol.73 , pp. 2109-2115
    • Hillier, C.J.1
  • 19
    • 51649093813 scopus 로고    scopus 로고
    • Comparative testing of six antigen-based malaria vaccine candidates directed toward merozoite-stage Plasmodium falciparum
    • Arnot D.E., et al. Comparative testing of six antigen-based malaria vaccine candidates directed toward merozoite-stage Plasmodium falciparum. Clin. Vaccine Immunol. 2008, 15:1345-1355.
    • (2008) Clin. Vaccine Immunol. , vol.15 , pp. 1345-1355
    • Arnot, D.E.1
  • 20
    • 34247220229 scopus 로고    scopus 로고
    • Conjugating recombinant proteins to Pseudomonas aeruginosa ExoProtein A: a strategy for enhancing immunogenicity of malaria vaccine candidates
    • Qian F., et al. Conjugating recombinant proteins to Pseudomonas aeruginosa ExoProtein A: a strategy for enhancing immunogenicity of malaria vaccine candidates. Vaccine 2007, 25:3923-3933.
    • (2007) Vaccine , vol.25 , pp. 3923-3933
    • Qian, F.1
  • 21
    • 34250177601 scopus 로고    scopus 로고
    • Immunogenicity and in vitro protective efficacy of a polyepitope Plasmodium falciparum candidate vaccine constructed by epitope shuffling
    • Cai Q., et al. Immunogenicity and in vitro protective efficacy of a polyepitope Plasmodium falciparum candidate vaccine constructed by epitope shuffling. Vaccine 2007, 25:5155-5165.
    • (2007) Vaccine , vol.25 , pp. 5155-5165
    • Cai, Q.1
  • 22
    • 44249090614 scopus 로고    scopus 로고
    • Toxoplasma gondii: serological characterization and immunogenicity of recombinant surface antigen 2 (SAG2) expressed in the yeast Pichia pastoris
    • Lau Y.L., Fong M.Y. Toxoplasma gondii: serological characterization and immunogenicity of recombinant surface antigen 2 (SAG2) expressed in the yeast Pichia pastoris. Exp. Parasitol. 2008, 119:373-378.
    • (2008) Exp. Parasitol. , vol.119 , pp. 373-378
    • Lau, Y.L.1    Fong, M.Y.2
  • 23
    • 38049174734 scopus 로고    scopus 로고
    • N-linked glycosylation of proteins in the protozoan parasite Toxoplasma gondii
    • Luk F.C., et al. N-linked glycosylation of proteins in the protozoan parasite Toxoplasma gondii. Mol. Biochem. Parasitol. 2008, 157:169-178.
    • (2008) Mol. Biochem. Parasitol. , vol.157 , pp. 169-178
    • Luk, F.C.1
  • 24
    • 51249123730 scopus 로고    scopus 로고
    • Expression and purification of non-glycosylated Trypanosoma brucei transferrin receptor in insect cells
    • Maier A., Steverding D. Expression and purification of non-glycosylated Trypanosoma brucei transferrin receptor in insect cells. Exp. Parasitol. 2008, 120:205-207.
    • (2008) Exp. Parasitol. , vol.120 , pp. 205-207
    • Maier, A.1    Steverding, D.2
  • 25
    • 33644656442 scopus 로고    scopus 로고
    • The malaria parasite Plasmodium falciparum histones: organization, expression, and acetylation
    • Miao J., et al. The malaria parasite Plasmodium falciparum histones: organization, expression, and acetylation. Gene 2006, 369:53-65.
    • (2006) Gene , vol.369 , pp. 53-65
    • Miao, J.1
  • 26
    • 27944481176 scopus 로고    scopus 로고
    • Histone-modifying complexes regulate gene expression pertinent to the differentiation of the protozoan parasite Toxoplasma gondii
    • Saksouk N., et al. Histone-modifying complexes regulate gene expression pertinent to the differentiation of the protozoan parasite Toxoplasma gondii. Mol. Cell. Biol. 2005, 25:10301-10314.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10301-10314
    • Saksouk, N.1
  • 27
    • 53949087361 scopus 로고    scopus 로고
    • Heterologous expression of plasmodial proteins for structural studies and functional annotation
    • Birkholtz L.M., et al. Heterologous expression of plasmodial proteins for structural studies and functional annotation. Malar. J. 2008, 7:197.
    • (2008) Malar. J. , vol.7 , pp. 197
    • Birkholtz, L.M.1
  • 28
    • 33747666218 scopus 로고    scopus 로고
    • Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems
    • Terpe K. Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol. 2006, 72:211-222.
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 211-222
    • Terpe, K.1
  • 29
    • 33845482665 scopus 로고    scopus 로고
    • Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms
    • Vedadi M., et al. Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms. Mol. Biochem. Parasitol. 2007, 151:100-110.
    • (2007) Mol. Biochem. Parasitol. , vol.151 , pp. 100-110
    • Vedadi, M.1
  • 30
    • 33745666810 scopus 로고    scopus 로고
    • Heterologous expression of proteins from Plasmodium falciparum: results from 1000 genes
    • Mehlin C., et al. Heterologous expression of proteins from Plasmodium falciparum: results from 1000 genes. Mol. Biochem. Parasitol. 2006, 148:144-160.
    • (2006) Mol. Biochem. Parasitol. , vol.148 , pp. 144-160
    • Mehlin, C.1
  • 31
    • 7444220614 scopus 로고    scopus 로고
    • High-throughput generation of Plasmodium falciparum functional molecules by recombinational cloning
    • Aguiar J.C., et al. High-throughput generation of Plasmodium falciparum functional molecules by recombinational cloning. Genome Res. 2004, 14:2076-2082.
    • (2004) Genome Res. , vol.14 , pp. 2076-2082
    • Aguiar, J.C.1
  • 32
    • 38749142906 scopus 로고    scopus 로고
    • Protein production and purification
    • Graslund S., et al. Protein production and purification. Nat. Methods 2008, 5:135-146.
    • (2008) Nat. Methods , vol.5 , pp. 135-146
    • Graslund, S.1
  • 33
    • 58249087221 scopus 로고    scopus 로고
    • The effect of heating rate on Escherichia coli metabolism, physiological stress, transcriptional response, and production of temperature-induced recombinant protein: a scale-down study
    • Caspeta L., et al. The effect of heating rate on Escherichia coli metabolism, physiological stress, transcriptional response, and production of temperature-induced recombinant protein: a scale-down study. Biotechnol. Bioeng. 2009, 102:468-482.
    • (2009) Biotechnol. Bioeng. , vol.102 , pp. 468-482
    • Caspeta, L.1
  • 34
    • 67651042924 scopus 로고    scopus 로고
    • Buffer optimization of thermal melt assays of Plasmodium proteins for detection of small-molecule ligands
    • Crowther G.J., et al. Buffer optimization of thermal melt assays of Plasmodium proteins for detection of small-molecule ligands. J. Biomol. Screen. 2009, 14:700-707.
    • (2009) J. Biomol. Screen. , vol.14 , pp. 700-707
    • Crowther, G.J.1
  • 35
    • 38549143777 scopus 로고    scopus 로고
    • Production of active eukaryotic proteins through bacterial expression systems: a review of the existing biotechnology strategies
    • Sahdev S., et al. Production of active eukaryotic proteins through bacterial expression systems: a review of the existing biotechnology strategies. Mol. Cell. Biochem. 2008, 307:249-264.
    • (2008) Mol. Cell. Biochem. , vol.307 , pp. 249-264
    • Sahdev, S.1
  • 36
    • 0033999271 scopus 로고    scopus 로고
    • Overcoming codon bias: a method for high-level overexpression of Plasmodium and other AT-rich parasite genes in Escherichia coli
    • Baca A.M., Hol W.G. Overcoming codon bias: a method for high-level overexpression of Plasmodium and other AT-rich parasite genes in Escherichia coli. Int. J. Parasitol. 2000, 30:113-118.
    • (2000) Int. J. Parasitol. , vol.30 , pp. 113-118
    • Baca, A.M.1    Hol, W.G.2
  • 37
    • 39449112551 scopus 로고    scopus 로고
    • Complete chemical synthesis, assembly, and cloning of a Mycoplasma genitalium genome
    • Gibson D.G., et al. Complete chemical synthesis, assembly, and cloning of a Mycoplasma genitalium genome. Science 2008, 319:1215-1220.
    • (2008) Science , vol.319 , pp. 1215-1220
    • Gibson, D.G.1
  • 38
    • 70349199628 scopus 로고    scopus 로고
    • Design parameters to control synthetic gene expression in Escherichia coli
    • Welch M., et al. Design parameters to control synthetic gene expression in Escherichia coli. PLoS One 2009, 4:e7002.
    • (2009) PLoS One , vol.4
    • Welch, M.1
  • 39
    • 59449096626 scopus 로고    scopus 로고
    • Cryptopain-1, a cysteine protease of Cryptosporidium parvum, does not require the pro-domain for folding
    • Na B.K., et al. Cryptopain-1, a cysteine protease of Cryptosporidium parvum, does not require the pro-domain for folding. Parasitology 2009, 136:149-157.
    • (2009) Parasitology , vol.136 , pp. 149-157
    • Na, B.K.1
  • 40
    • 84954358339 scopus 로고    scopus 로고
    • Purification, refolding and autoactivation of the recombinant cysteine proteinase EhCP112 from Entamoeba histolytica
    • Quintas-Granados L.I., et al. Purification, refolding and autoactivation of the recombinant cysteine proteinase EhCP112 from Entamoeba histolytica. Protein Expr. Purif. 2009, 63:26-32.
    • (2009) Protein Expr. Purif. , vol.63 , pp. 26-32
    • Quintas-Granados, L.I.1
  • 41
    • 55849120501 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of Babesia gibsoni dihydrofolate reductase-thymidylate synthase: inhibitory effect of antifolates on its catalytic activity and parasite proliferation
    • Aboge G.O., et al. Cloning, expression, and characterization of Babesia gibsoni dihydrofolate reductase-thymidylate synthase: inhibitory effect of antifolates on its catalytic activity and parasite proliferation. Antimicrob. Agents Chemother. 2008, 52:4072-4080.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 4072-4080
    • Aboge, G.O.1
  • 42
    • 70349772921 scopus 로고    scopus 로고
    • CD8 T cell immunity to Plasmodium permits generation of protective antibodies after repeated sporozoite challenge
    • Schmidt N.W., et al. CD8 T cell immunity to Plasmodium permits generation of protective antibodies after repeated sporozoite challenge. Vaccine 2009, 27:6103-6106.
    • (2009) Vaccine , vol.27 , pp. 6103-6106
    • Schmidt, N.W.1
  • 43
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides S.C. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 1996, 60:512-538.
    • (1996) Microbiol. Rev. , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 44
    • 27644484749 scopus 로고    scopus 로고
    • A protein interaction network of the malaria parasite Plasmodium falciparum
    • LaCount D.J., et al. A protein interaction network of the malaria parasite Plasmodium falciparum. Nature 2005, 438:103-107.
    • (2005) Nature , vol.438 , pp. 103-107
    • LaCount, D.J.1
  • 45
    • 84934439701 scopus 로고    scopus 로고
    • Baculovirus expression vector system: an emerging host for high-throughput eukaryotic protein expression
    • Shrestha B., et al. Baculovirus expression vector system: an emerging host for high-throughput eukaryotic protein expression. Methods Mol. Biol. 2008, 439:269-289.
    • (2008) Methods Mol. Biol. , vol.439 , pp. 269-289
    • Shrestha, B.1
  • 46
    • 38349157756 scopus 로고    scopus 로고
    • Expression, purification and characterization of recombinant mitochondrial topoisomerase II of kinetoplastid Crithidia fasciculata in high-five insect cells
    • Wang Y., et al. Expression, purification and characterization of recombinant mitochondrial topoisomerase II of kinetoplastid Crithidia fasciculata in high-five insect cells. Protein Expr. Purif. 2008, 58:122-131.
    • (2008) Protein Expr. Purif. , vol.58 , pp. 122-131
    • Wang, Y.1
  • 47
    • 0036892173 scopus 로고    scopus 로고
    • A modified hepatitis B virus core particle containing multiple epitopes of the Plasmodium falciparum circumsporozoite protein provides a highly immunogenic malaria vaccine in preclinical analyses in rodent and primate hosts
    • Birkett A., et al. A modified hepatitis B virus core particle containing multiple epitopes of the Plasmodium falciparum circumsporozoite protein provides a highly immunogenic malaria vaccine in preclinical analyses in rodent and primate hosts. Infect. Immun. 2002, 70:6860-6870.
    • (2002) Infect. Immun. , vol.70 , pp. 6860-6870
    • Birkett, A.1
  • 48
    • 33646353667 scopus 로고    scopus 로고
    • Safety, immunogenicity, and efficacy of prime-boost immunization with recombinant poxvirus FP9 and modified vaccinia virus Ankara encoding the full-length Plasmodium falciparum circumsporozoite protein
    • Walther M., et al. Safety, immunogenicity, and efficacy of prime-boost immunization with recombinant poxvirus FP9 and modified vaccinia virus Ankara encoding the full-length Plasmodium falciparum circumsporozoite protein. Infect. Immun. 2006, 74:2706-2716.
    • (2006) Infect. Immun. , vol.74 , pp. 2706-2716
    • Walther, M.1
  • 49
    • 0036304601 scopus 로고    scopus 로고
    • Surface expression of an immunodominant malaria protein B cell epitope by yellow fever virus
    • Bonaldo M.C., et al. Surface expression of an immunodominant malaria protein B cell epitope by yellow fever virus. J. Mol. Biol. 2002, 315:873-885.
    • (2002) J. Mol. Biol. , vol.315 , pp. 873-885
    • Bonaldo, M.C.1
  • 50
    • 0036263432 scopus 로고    scopus 로고
    • In vivo expression and immunological studies of the 42-kilodalton carboxyl-terminal processing fragment of Plasmodium falciparum merozoite surface protein 1 in the baculovirus-silkworm system
    • Pang A.L., et al. In vivo expression and immunological studies of the 42-kilodalton carboxyl-terminal processing fragment of Plasmodium falciparum merozoite surface protein 1 in the baculovirus-silkworm system. Infect. Immun. 2002, 70:2772-2779.
    • (2002) Infect. Immun. , vol.70 , pp. 2772-2779
    • Pang, A.L.1
  • 51
    • 58249090958 scopus 로고    scopus 로고
    • Recombinant viral vaccines expressing merozoite surface protein-1 induce antibody- and T cell-mediated multistage protection against malaria
    • Draper S.J., et al. Recombinant viral vaccines expressing merozoite surface protein-1 induce antibody- and T cell-mediated multistage protection against malaria. Cell Host Microbe 2009, 5:95-105.
    • (2009) Cell Host Microbe , vol.5 , pp. 95-105
    • Draper, S.J.1
  • 52
    • 33645943034 scopus 로고    scopus 로고
    • Vaccination with replication-deficient recombinant adenoviruses encoding the main surface antigens of Toxoplasma gondii induces immune response and protection against infection in mice
    • Caetano B.C., et al. Vaccination with replication-deficient recombinant adenoviruses encoding the main surface antigens of Toxoplasma gondii induces immune response and protection against infection in mice. Hum. Gene Ther. 2006, 17:415-426.
    • (2006) Hum. Gene Ther. , vol.17 , pp. 415-426
    • Caetano, B.C.1
  • 53
    • 2442492088 scopus 로고    scopus 로고
    • MVA ROP2 vaccinia virus recombinant as a vaccine candidate for toxoplasmosis
    • Roque-Resendiz J.L., et al. MVA ROP2 vaccinia virus recombinant as a vaccine candidate for toxoplasmosis. Parasitology 2004, 128:397-405.
    • (2004) Parasitology , vol.128 , pp. 397-405
    • Roque-Resendiz, J.L.1
  • 54
    • 0032914633 scopus 로고    scopus 로고
    • Surface display of a parasite antigen in the ciliate Tetrahymena thermophila
    • Gaertig J., et al. Surface display of a parasite antigen in the ciliate Tetrahymena thermophila. Nat. Biotechnol. 1999, 17:462-465.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 462-465
    • Gaertig, J.1
  • 55
    • 0035005160 scopus 로고    scopus 로고
    • The I-antigens of Ichthyophthirius multifiliis are GPI-anchored proteins
    • Clark T.G., et al. The I-antigens of Ichthyophthirius multifiliis are GPI-anchored proteins. J. Eukaryot. Microbiol. 2001, 48:332-337.
    • (2001) J. Eukaryot. Microbiol. , vol.48 , pp. 332-337
    • Clark, T.G.1
  • 56
    • 0036064561 scopus 로고    scopus 로고
    • The circumsporozoite protein of Plasmodium falciparum is expressed and localized to the cell surface in the free-living ciliate Tetrahymena thermophila
    • Peterson D.S., et al. The circumsporozoite protein of Plasmodium falciparum is expressed and localized to the cell surface in the free-living ciliate Tetrahymena thermophila. Mol. Biochem. Parasitol. 2002, 122:119-126.
    • (2002) Mol. Biochem. Parasitol. , vol.122 , pp. 119-126
    • Peterson, D.S.1
  • 57
    • 34047175251 scopus 로고    scopus 로고
    • A recombinase system facilitates cloning of expression cassettes in the ciliate Tetrahymena thermophila
    • Weide T., et al. A recombinase system facilitates cloning of expression cassettes in the ciliate Tetrahymena thermophila. BMC Microbiol. 2007, 7:12.
    • (2007) BMC Microbiol. , vol.7 , pp. 12
    • Weide, T.1
  • 58
    • 33748598232 scopus 로고    scopus 로고
    • Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a model eukaryote
    • Eisen J.A., et al. Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a model eukaryote. PLoS Biol. 2006, 4:e286.
    • (2006) PLoS Biol. , vol.4
    • Eisen, J.A.1
  • 59
    • 33748420540 scopus 로고    scopus 로고
    • From cell-cell adhesion and cellular oscillations to spectacular views inside the cell - 50 years of research with Dictyostelium
    • Muller-Taubenberger A., Bozzaro S. From cell-cell adhesion and cellular oscillations to spectacular views inside the cell - 50 years of research with Dictyostelium. Eur. J. Cell Biol. 2006, 85:851-858.
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 851-858
    • Muller-Taubenberger, A.1    Bozzaro, S.2
  • 60
    • 57349106051 scopus 로고    scopus 로고
    • Dictyostelium discoideum - a promising expression system for the production of eukaryotic proteins
    • Arya R., et al. Dictyostelium discoideum - a promising expression system for the production of eukaryotic proteins. FASEB J. 2008, 22:4055-4066.
    • (2008) FASEB J. , vol.22 , pp. 4055-4066
    • Arya, R.1
  • 61
    • 0029049736 scopus 로고
    • Anchoring of an immunogenic Plasmodium falciparum circumsporozoite protein on the surface of Dictyostelium discoideum
    • Reymond C.D., et al. Anchoring of an immunogenic Plasmodium falciparum circumsporozoite protein on the surface of Dictyostelium discoideum. J. Biol. Chem. 1995, 270:12941-12947.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12941-12947
    • Reymond, C.D.1
  • 62
    • 0026587156 scopus 로고
    • Dictyostelium discoideum as an expression host for the circumsporozoite protein of Plasmodium falciparum
    • Fasel N., et al. Dictyostelium discoideum as an expression host for the circumsporozoite protein of Plasmodium falciparum. Gene 1992, 111:157-163.
    • (1992) Gene , vol.111 , pp. 157-163
    • Fasel, N.1
  • 63
    • 18344395923 scopus 로고    scopus 로고
    • The genome of the social amoeba Dictyostelium discoideum
    • Eichinger L., et al. The genome of the social amoeba Dictyostelium discoideum. Nature 2005, 435:43-57.
    • (2005) Nature , vol.435 , pp. 43-57
    • Eichinger, L.1
  • 64
    • 57049139865 scopus 로고    scopus 로고
    • Plasmodium falciparum: chemically defined medium for continuous intraerythrocytic growth using lipids and recombinant albumin
    • Asahi H. Plasmodium falciparum: chemically defined medium for continuous intraerythrocytic growth using lipids and recombinant albumin. Exp. Parasitol. 2009, 121:22-28.
    • (2009) Exp. Parasitol. , vol.121 , pp. 22-28
    • Asahi, H.1
  • 65
    • 0029656031 scopus 로고    scopus 로고
    • Comparative evaluation of several techniques for purification of Cryptosporidium parvum oocysts from rat feces
    • Suresh P., Rehg J.E. Comparative evaluation of several techniques for purification of Cryptosporidium parvum oocysts from rat feces. J. Clin. Microbiol. 1996, 34:38-40.
    • (1996) J. Clin. Microbiol. , vol.34 , pp. 38-40
    • Suresh, P.1    Rehg, J.E.2
  • 66
    • 0030946239 scopus 로고    scopus 로고
    • Expression of Toxoplasma gondii genes in the closely-related apicomplexan parasite Neospora caninum
    • Howe D.K., et al. Expression of Toxoplasma gondii genes in the closely-related apicomplexan parasite Neospora caninum. Mol. Biochem. Parasitol. 1997, 86:29-36.
    • (1997) Mol. Biochem. Parasitol. , vol.86 , pp. 29-36
    • Howe, D.K.1
  • 67
    • 0035851346 scopus 로고    scopus 로고
    • Attenuated Toxoplasma gondii ts-4 mutants engineered to express the Leishmania antigen KMP-11 elicit a specific immune response in BALB/c mice
    • Ramirez J.R., et al. Attenuated Toxoplasma gondii ts-4 mutants engineered to express the Leishmania antigen KMP-11 elicit a specific immune response in BALB/c mice. Vaccine 2001, 20:455-461.
    • (2001) Vaccine , vol.20 , pp. 455-461
    • Ramirez, J.R.1
  • 68
    • 25444509858 scopus 로고    scopus 로고
    • Heterologous expression in Tritrichomonas foetus of functional Trichomonas vaginalis AP65 adhesin
    • Kucknoor A.S., et al. Heterologous expression in Tritrichomonas foetus of functional Trichomonas vaginalis AP65 adhesin. BMC Mol. Biol. 2005, 6:5.
    • (2005) BMC Mol. Biol. , vol.6 , pp. 5
    • Kucknoor, A.S.1
  • 69
    • 33750617911 scopus 로고    scopus 로고
    • Expression and function of pvcrt-o, a Plasmodium vivax ortholog of pfcrt, in Plasmodium falciparum and Dictyostelium discoideum
    • Sa J.M., et al. Expression and function of pvcrt-o, a Plasmodium vivax ortholog of pfcrt, in Plasmodium falciparum and Dictyostelium discoideum. Mol. Biochem. Parasitol. 2006, 150:219-228.
    • (2006) Mol. Biochem. Parasitol. , vol.150 , pp. 219-228
    • Sa, J.M.1
  • 70
    • 35448955196 scopus 로고    scopus 로고
    • Trypanosoma cruzi as a model system to study the expression of exogenous genes coding for polyamine biosynthetic enzymes. Induction of DFMO resistance in transgenic parasites
    • Carrillo C., et al. Trypanosoma cruzi as a model system to study the expression of exogenous genes coding for polyamine biosynthetic enzymes. Induction of DFMO resistance in transgenic parasites. Biochim. Biophys. Acta 2007, 1770:1605-1611.
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 1605-1611
    • Carrillo, C.1
  • 71
    • 33845995108 scopus 로고    scopus 로고
    • Cell-free production of functional Plasmodium falciparum dihydrofolate reductase-thymidylate synthase
    • Mudeppa D.G., et al. Cell-free production of functional Plasmodium falciparum dihydrofolate reductase-thymidylate synthase. Mol. Biochem. Parasitol. 2007, 151:216-219.
    • (2007) Mol. Biochem. Parasitol. , vol.151 , pp. 216-219
    • Mudeppa, D.G.1
  • 72
    • 42149195334 scopus 로고    scopus 로고
    • Wheat germ cell-free system-based production of malaria proteins for discovery of novel vaccine candidates
    • Tsuboi T., et al. Wheat germ cell-free system-based production of malaria proteins for discovery of novel vaccine candidates. Infect. Immun. 2008, 76:1702-1708.
    • (2008) Infect. Immun. , vol.76 , pp. 1702-1708
    • Tsuboi, T.1
  • 73
  • 74
    • 0037217056 scopus 로고    scopus 로고
    • Multiple protein phylogenies show that Oxyrrhis marina and Perkinsus marinus are early branches of the dinoflagellate lineage
    • Saldarriaga J.F., et al. Multiple protein phylogenies show that Oxyrrhis marina and Perkinsus marinus are early branches of the dinoflagellate lineage. Int. J. Syst. Evol. Microbiol. 2003, 53:355-365.
    • (2003) Int. J. Syst. Evol. Microbiol. , vol.53 , pp. 355-365
    • Saldarriaga, J.F.1
  • 75
    • 0029294002 scopus 로고
    • Effect of fetal bovine serum glycoproteins on the in vitro proliferation of the oyster parasite Perkinsus marinus: development of a fully defined medium
    • Gauthier J.D., et al. Effect of fetal bovine serum glycoproteins on the in vitro proliferation of the oyster parasite Perkinsus marinus: development of a fully defined medium. J. Eukaryot. Microbiol. 1995, 42:307-313.
    • (1995) J. Eukaryot. Microbiol. , vol.42 , pp. 307-313
    • Gauthier, J.D.1
  • 76
    • 0002227942 scopus 로고    scopus 로고
    • Development of a protein-free chemically defined culture medium for the propagation of the oyster pathogen Perkinsus marinus
    • La Peyre J.F., Faisal M. Development of a protein-free chemically defined culture medium for the propagation of the oyster pathogen Perkinsus marinus. Parasite 1997, 4:67-73.
    • (1997) Parasite , vol.4 , pp. 67-73
    • La Peyre, J.F.1    Faisal, M.2
  • 77
    • 36349006964 scopus 로고    scopus 로고
    • Transfection of the protozoan parasite Perkinsus marinus
    • Fernández-Robledo J.A., et al. Transfection of the protozoan parasite Perkinsus marinus. Mol. Biochem. Parasitol. 2008, 157:44-53.
    • (2008) Mol. Biochem. Parasitol. , vol.157 , pp. 44-53
    • Fernández-Robledo, J.A.1
  • 78
    • 39749177154 scopus 로고    scopus 로고
    • Evolutionary biology: bridge over troublesome plastids
    • Keeling P.J. Evolutionary biology: bridge over troublesome plastids. Nature 2008, 451:896-897.
    • (2008) Nature , vol.451 , pp. 896-897
    • Keeling, P.J.1
  • 79
    • 39749142234 scopus 로고    scopus 로고
    • A photosynthetic alveolate closely related to apicomplexan parasites
    • Moore R.B., et al. A photosynthetic alveolate closely related to apicomplexan parasites. Nature 2008, 451:959-963.
    • (2008) Nature , vol.451 , pp. 959-963
    • Moore, R.B.1
  • 80
    • 45849103886 scopus 로고    scopus 로고
    • A perspective on the biotechnological potential of microalgae
    • Raja R., et al. A perspective on the biotechnological potential of microalgae. Crit. Rev. Microbiol. 2008, 34:77-88.
    • (2008) Crit. Rev. Microbiol. , vol.34 , pp. 77-88
    • Raja, R.1
  • 81
    • 64549111428 scopus 로고    scopus 로고
    • Yeast systems biotechnology for the production of heterologous proteins
    • Graf A., et al. Yeast systems biotechnology for the production of heterologous proteins. FEMS Yeast Res. 2009, 9:335-348.
    • (2009) FEMS Yeast Res. , vol.9 , pp. 335-348
    • Graf, A.1
  • 82
    • 0021958555 scopus 로고
    • The identity of Leishmania tarentolae Wenyon 1921
    • Wallbanks K.R., et al. The identity of Leishmania tarentolae Wenyon 1921. Parasitology 1985, 90:67-78.
    • (1985) Parasitology , vol.90 , pp. 67-78
    • Wallbanks, K.R.1
  • 83
    • 84934442053 scopus 로고    scopus 로고
    • Gateway cloning for protein expression
    • Esposito D., et al. Gateway cloning for protein expression. Methods Mol. Biol. 2009, 498:31-54.
    • (2009) Methods Mol. Biol. , vol.498 , pp. 31-54
    • Esposito, D.1
  • 84
    • 85057635226 scopus 로고    scopus 로고
    • Use of the gateway system for protein expression in multiple hosts
    • Chapter 5, Unit 5.17
    • Hartley J.L. Use of the gateway system for protein expression in multiple hosts. Curr. Protoc. Protein Sci. 2003, Chapter 5, Unit 5.17.
    • (2003) Curr. Protoc. Protein Sci.
    • Hartley, J.L.1
  • 85
    • 0033676098 scopus 로고    scopus 로고
    • DNA cloning using in vitro site-specific recombination
    • Hartley J.L., et al. DNA cloning using in vitro site-specific recombination. Genome Res. 2000, 10:1788-1795.
    • (2000) Genome Res. , vol.10 , pp. 1788-1795
    • Hartley, J.L.1
  • 86
    • 10744222063 scopus 로고    scopus 로고
    • Novel antigen identification method for discovery of protective malaria antigens by rapid testing of DNA vaccines encoding exons from the parasite genome
    • Haddad D., et al. Novel antigen identification method for discovery of protective malaria antigens by rapid testing of DNA vaccines encoding exons from the parasite genome. Infect. Immun. 2004, 72:1594-1602.
    • (2004) Infect. Immun. , vol.72 , pp. 1594-1602
    • Haddad, D.1
  • 87
    • 59249093177 scopus 로고    scopus 로고
    • Development of the Gateway system for cloning and expressing genes in Entamoeba histolytica
    • Abhyankar M.M., et al. Development of the Gateway system for cloning and expressing genes in Entamoeba histolytica. Parasitol. Int. 2009, 58:95-97.
    • (2009) Parasitol. Int. , vol.58 , pp. 95-97
    • Abhyankar, M.M.1
  • 88
    • 29544440398 scopus 로고    scopus 로고
    • Hydrophobic moeties in recombinant proteins are crucial to generate efficient saponin-based vaccine against apicomplexan Babesia divergens
    • Delbecq S., et al. Hydrophobic moeties in recombinant proteins are crucial to generate efficient saponin-based vaccine against apicomplexan Babesia divergens. Vaccine 2006, 24:613-621.
    • (2006) Vaccine , vol.24 , pp. 613-621
    • Delbecq, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.