메뉴 건너뛰기




Volumn 17, Issue 3, 1999, Pages 392-400

Expression of a recombinant Toxoplasma gondii ROP2 fragment as a fusion protein in bacteria circumvents insolubility and proteolytic degradation

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXY TERMINAL SEQUENCE; CHROMATOGRAPHY; DETERGENT; ESCHERICHIA COLI; GEL FILTRATION; HYBRID PROTEIN; IMMUNOGENICITY; MALTOSE BINDING PROTEIN; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN HYDROLYSIS; PROTEIN PURIFICATION; RECOMBINANT PROTEIN; SOLUBILITY; SOLUBILIZATION; THIOREDOXIN; TOXOPLASMA GONDII;

EID: 0033486169     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1999.1150     Document Type: Article
Times cited : (36)

References (22)
  • 3
    • 0026901767 scopus 로고
    • Toxoplasmosis encephalitis in AIDS
    • Luft B. J., Remington J. S. Toxoplasmosis encephalitis in AIDS. Clin. Infect. Dis. 15:1992;211-222.
    • (1992) Clin. Infect. Dis. , vol.15 , pp. 211-222
    • Luft, B.J.1    Remington, J.S.2
  • 4
    • 0026021838 scopus 로고
    • + T lymphocytes in IFN-γ production and protective immunity induced by an attenuated Toxoplasma gondii vaccine
    • + T lymphocytes in IFN-γ production and protective immunity induced by an attenuated Toxoplasma gondii vaccine. J. Immunol. 146:1991;286-292.
    • (1991) J. Immunol. , vol.146 , pp. 286-292
    • Gazzinelli, R.T.1    Hakim, F.T.2    Hieny, S.3    Shearer, G.M.4    Sher, A.5
  • 5
    • 0023895411 scopus 로고
    • Interferon-γ: The major mediator of resistance against Toxoplasma gondii
    • Suzuki Y., Orellana M. A., Schreiber R. D., Remington J. S. Interferon-γ: The major mediator of resistance against Toxoplasma gondii. Science. 240:1988;516-518.
    • (1988) Science , vol.240 , pp. 516-518
    • Suzuki, Y.1    Orellana, M.A.2    Schreiber, R.D.3    Remington, J.S.4
  • 7
    • 0028134806 scopus 로고
    • The Toxoplasma gondii rhoptry protein ROP2 is inserted into the parasitophorous vacuole membrane, surrounding the intracellular parasite, and is exposed to the host cell cytoplasm
    • Beckers C. J. M., Dubremetz J-F., Mercereau-Puijalon O., Joiner K. The Toxoplasma gondii rhoptry protein ROP2 is inserted into the parasitophorous vacuole membrane, surrounding the intracellular parasite, and is exposed to the host cell cytoplasm. J. Cell Biol. 4:1994;947-961.
    • (1994) J. Cell Biol. , vol.4 , pp. 947-961
    • Beckers, C.J.M.1    Dubremetz, J.-F.2    Mercereau-Puijalon, O.3    Joiner, K.4
  • 8
    • 0026076742 scopus 로고
    • Human T cell clone identifies a potentially protective 54-kDa protein antigen of Toxoplasma gondii cloned and expressed in E
    • Saavedra R., de Meuter F., Delcourt J.-L., Hérion P. Human T cell clone identifies a potentially protective 54-kDa protein antigen of Toxoplasma gondii cloned and expressed in E. coli. J. Immunol. 147:1991;1975-1982.
    • (1991) Coli. J. Immunol. , vol.147 , pp. 1975-1982
    • Saavedra, R.1    De Meuter, F.2    Delcourt, J.-L.3    Hérion, P.4
  • 10
    • 0027508691 scopus 로고
    • Serodiagnosis of toxoplasmosis by using a recombinant form of the 54-kilodalton rhoptry antigen expressed in Escherichia coli
    • Van Gelder P., Bosman F., De Meuter F., Van Heuverswyn H., Hérion P. Serodiagnosis of toxoplasmosis by using a recombinant form of the 54-kilodalton rhoptry antigen expressed in Escherichia coli. J. Clin. Microbiol. 31:1993;9-15.
    • (1993) J. Clin. Microbiol. , vol.31 , pp. 9-15
    • Van Gelder, P.1    Bosman, F.2    De Meuter, F.3    Van Heuverswyn, H.4    Hérion, P.5
  • 12
    • 0028886745 scopus 로고
    • Cellular and humoral immune responses to recombinant antigens in sheep infected with Toxoplasma gondii
    • Coughlan S. N., Saman S., Jacobs D., Mercier C., Cesbron-Delauw M. F., Trees A. J. Cellular and humoral immune responses to recombinant antigens in sheep infected with Toxoplasma gondii. Parasite Immunol. 17:1995;465-468.
    • (1995) Parasite Immunol. , vol.17 , pp. 465-468
    • Coughlan, S.N.1    Saman, S.2    Jacobs, D.3    Mercier, C.4    Cesbron-Delauw, M.F.5    Trees, A.J.6
  • 13
    • 0026135241 scopus 로고
    • Fusion tails for the recovery and purification of recombinant proteins
    • Ford C. F., Suominen I., Glatz C. E. Fusion tails for the recovery and purification of recombinant proteins. Protein Expression Purif. 2:1991;95-107.
    • (1991) Protein Expression Purif. , vol.2 , pp. 95-107
    • Ford, C.F.1    Suominen, I.2    Glatz, C.E.3
  • 14
    • 14744292185 scopus 로고
    • A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm
    • LaVallie E. R., DiBlasio E. A., Kovacic S., Grant K. L., Schendel P. F., McCoy J. M. A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm. BioTechnology. 11:1993;187-193.
    • (1993) BioTechnology , vol.11 , pp. 187-193
    • Lavallie, E.R.1    Diblasio, E.A.2    Kovacic, S.3    Grant, K.L.4    Schendel, P.F.5    McCoy, J.M.6
  • 15
    • 0001895061 scopus 로고
    • Introduction to expression by fusion vectors: Expression and purification of maltose-binding protein fusions
    • Ausubel New York: Greene Associates/Wiley Interscience
    • Riggs P. Introduction to expression by fusion vectors: Expression and purification of maltose-binding protein fusions. Ausubel. Current Protocols in Molecular Biology. 1990;16.4.1-16.4.3 Greene Associates/Wiley Interscience, New York.
    • (1990) Current Protocols in Molecular Biology , pp. 1641-1643
    • Riggs, P.1
  • 17
    • 0028901398 scopus 로고
    • Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases. Isolation and characterization of the wild-type enzyme
    • Marinez A., Knappskog P. M., Olafsdottir S., Doskeland A. P., Eiken H. G., Svebak R. M., Bozzini M., Apold J., Flatmark T. Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases. Isolation and characterization of the wild-type enzyme. Biochem. J. 306:1995;589-597.
    • (1995) Biochem. J. , vol.306 , pp. 589-597
    • Marinez, A.1    Knappskog, P.M.2    Olafsdottir, S.3    Doskeland, A.P.4    Eiken, H.G.5    Svebak, R.M.6    Bozzini, M.7    Apold, J.8    Flatmark, T.9
  • 19
    • 0022383959 scopus 로고
    • Vector with restriction site bank IV. PJRD184, a 3793-bp plasmid vector having 43 unique cloning sites
    • Heuterspreute M., Ha Thi V., Emery S., Tournis-Gamble S., Kennedy N., Davison J. Vector with restriction site bank IV. PJRD184, a 3793-bp plasmid vector having 43 unique cloning sites. Gene. 39:1985;299-304.
    • (1985) Gene , vol.39 , pp. 299-304
    • Heuterspreute, M.1    Ha Thi, V.2    Emery, S.3    Tournis-Gamble, S.4    Kennedy, N.5    Davison, J.6
  • 20
    • 11944265249 scopus 로고
    • High level expression of tissue inhibitor of metalloproteinases in chines hamster ovary cells using glutamine synthetase gene amplification
    • Cockett M. I., Bebbington C. R., Yarranton G. T. High level expression of tissue inhibitor of metalloproteinases in chines hamster ovary cells using glutamine synthetase gene amplification. BioTechnology. 8:1990;662-667.
    • (1990) BioTechnology , vol.8 , pp. 662-667
    • Cockett, M.I.1    Bebbington, C.R.2    Yarranton, G.T.3
  • 21
    • 0032006484 scopus 로고    scopus 로고
    • Solubility of proteins isolated from inclusion bodies is enhanced by fusion to maltose-binding protein
    • Sachdev D., Chirgwin J. M. Solubility of proteins isolated from inclusion bodies is enhanced by fusion to maltose-binding protein. Protein Expression Purif. 12:1998;122-132.
    • (1998) Protein Expression Purif. , vol.12 , pp. 122-132
    • Sachdev, D.1    Chirgwin, J.M.2
  • 22
    • 0031839784 scopus 로고    scopus 로고
    • High-level expression of the endo-β-N-acetylglucosaminidase F2 gene in E. coli: One step purification to homogeneity
    • Reddy A., Grimwood B. G., Plummer T. H., Tarentino A. L. High-level expression of the endo-β-N-acetylglucosaminidase F2 gene in E. coli: one step purification to homogeneity. Glycobiology. 8:1998;633-636.
    • (1998) Glycobiology , vol.8 , pp. 633-636
    • Reddy, A.1    Grimwood, B.G.2    Plummer, T.H.3    Tarentino, A.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.