메뉴 건너뛰기




Volumn 50, Issue 1, 2006, Pages 58-67

Production and characterization of clinical grade Escherichia coli derived Plasmodium falciparum 42 kDa merozoite surface protein 1 (MSP142) in the absence of an affinity tag

Author keywords

Escherichia coli; MSP1; Plasmodium falciparum; Refold; Vaccine

Indexed keywords

MEROZOITE SURFACE PROTEIN 1; RECOMBINANT PROTEIN;

EID: 33751046331     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.06.018     Document Type: Article
Times cited : (27)

References (30)
  • 1
    • 0023159777 scopus 로고
    • Fragments of the polymorphic Mr 185,000 glycoprotein from the surface of isolated Plasmodium falciparum merozoites form an antigenic complex
    • McBride J.S., and Heidrich H.G. Fragments of the polymorphic Mr 185,000 glycoprotein from the surface of isolated Plasmodium falciparum merozoites form an antigenic complex. Mol. Biochem. Parasitol. 23 (1987) 71-84
    • (1987) Mol. Biochem. Parasitol. , vol.23 , pp. 71-84
    • McBride, J.S.1    Heidrich, H.G.2
  • 2
    • 0026010023 scopus 로고
    • Processing of the Plasmodium falciparum major merozoite surface protein-1: identification of a 33-kilodalton secondary processing product which is shed prior to erythrocyte invasion
    • Blackman M.J., Whittle H., and Holder A.A. Processing of the Plasmodium falciparum major merozoite surface protein-1: identification of a 33-kilodalton secondary processing product which is shed prior to erythrocyte invasion. Mol. Biochem. Parasitol. 49 (1991) 35-44
    • (1991) Mol. Biochem. Parasitol. , vol.49 , pp. 35-44
    • Blackman, M.J.1    Whittle, H.2    Holder, A.A.3
  • 3
    • 0027241045 scopus 로고
    • Analysis of sequence diversity in the Plasmodium falciparum merozoite surface protein-1 (MSP-1)
    • Miller L.H., Roberts T., Shahabuddin M., and McCutchan T.F. Analysis of sequence diversity in the Plasmodium falciparum merozoite surface protein-1 (MSP-1). Mol. Biochem. Parasitol. 59 (1993) 1-14
    • (1993) Mol. Biochem. Parasitol. , vol.59 , pp. 1-14
    • Miller, L.H.1    Roberts, T.2    Shahabuddin, M.3    McCutchan, T.F.4
  • 4
    • 0023236613 scopus 로고
    • Allelic dimorphism in a surface antigen gene of the malaria parasite Plasmodium falciparum
    • Tanabe K., Mackay M., Goman M., and Scaife J.G. Allelic dimorphism in a surface antigen gene of the malaria parasite Plasmodium falciparum. J. Mol. Biol. 195 (1987) 273-287
    • (1987) J. Mol. Biol. , vol.195 , pp. 273-287
    • Tanabe, K.1    Mackay, M.2    Goman, M.3    Scaife, J.G.4
  • 5
    • 19944369747 scopus 로고    scopus 로고
    • The clinical-grade 42-kilodalton fragment of merozoite surface protein 1 of Plasmodium falciparum strain FVO expressed in Escherichia coli protects Aotus nancymai against challenge with homologous erythrocytic-stage parasites
    • Darko C.A., Angov E., Collins W.E., Bergmann-Leitner E.S., Girouard A.S., Hitt S.L., McBride J.S., Diggs C.L., Holder A.A., Long C.A., Barnwell J.W., and Lyon J.A. The clinical-grade 42-kilodalton fragment of merozoite surface protein 1 of Plasmodium falciparum strain FVO expressed in Escherichia coli protects Aotus nancymai against challenge with homologous erythrocytic-stage parasites. Infect. Immun. 73 (2005) 287-297
    • (2005) Infect. Immun. , vol.73 , pp. 287-297
    • Darko, C.A.1    Angov, E.2    Collins, W.E.3    Bergmann-Leitner, E.S.4    Girouard, A.S.5    Hitt, S.L.6    McBride, J.S.7    Diggs, C.L.8    Holder, A.A.9    Long, C.A.10    Barnwell, J.W.11    Lyon, J.A.12
  • 6
    • 0345283125 scopus 로고    scopus 로고
    • Biochemical and immunological characterization of bacterially expressed and refolded Plasmodium falciparum 42-kilodalton C-terminal merozoite surface protein 1
    • Singh S., Kennedy M.C., Long C.A., Saul A.J., Miller L.H., and Stowers A.W. Biochemical and immunological characterization of bacterially expressed and refolded Plasmodium falciparum 42-kilodalton C-terminal merozoite surface protein 1. Infect. Immun. 71 (2003) 6766-6774
    • (2003) Infect. Immun. , vol.71 , pp. 6766-6774
    • Singh, S.1    Kennedy, M.C.2    Long, C.A.3    Saul, A.J.4    Miller, L.H.5    Stowers, A.W.6
  • 8
    • 1842374388 scopus 로고    scopus 로고
    • Immunization with a recombinant C-terminal fragment of Plasmodium yoelii merozoite surface protein 1 protects mice against homologous but not heterologous P. yoelii sporozoite challenge
    • Renia L., Ling I.T., Marusing M., Miltgen F., Holder A.A., and Mazier D. Immunization with a recombinant C-terminal fragment of Plasmodium yoelii merozoite surface protein 1 protects mice against homologous but not heterologous P. yoelii sporozoite challenge. Infect. Immun. 65 (1997) 4419-4423
    • (1997) Infect. Immun. , vol.65 , pp. 4419-4423
    • Renia, L.1    Ling, I.T.2    Marusing, M.3    Miltgen, F.4    Holder, A.A.5    Mazier, D.6
  • 9
    • 0036893441 scopus 로고    scopus 로고
    • Vaccination of monkeys with recombinant Plasmodium falciparum apical membrane antigen 1 confers protection against blood-stage malaria
    • Stowers A.W., Kennedy M.C., Keegan B.P., Saul A., Long C.A., and Miller L.H. Vaccination of monkeys with recombinant Plasmodium falciparum apical membrane antigen 1 confers protection against blood-stage malaria. Infect. Immun. 70 (2002) 6961-6967
    • (2002) Infect. Immun. , vol.70 , pp. 6961-6967
    • Stowers, A.W.1    Kennedy, M.C.2    Keegan, B.P.3    Saul, A.4    Long, C.A.5    Miller, L.H.6
  • 11
    • 23944502355 scopus 로고    scopus 로고
    • Merozoite surface protein 1 of Plasmodium vivax induces a protective response against Plasmodium cynomolgi challenge in rhesus monkeys
    • Dutta D., Kaushal D.C., Ware L.A., Puri S.K., Kaushal N.A., Narula A., Upadhyaya D.S., and Lanar D.E. Merozoite surface protein 1 of Plasmodium vivax induces a protective response against Plasmodium cynomolgi challenge in rhesus monkeys. Infect. Immun. 73 (2005) 5936-5944
    • (2005) Infect. Immun. , vol.73 , pp. 5936-5944
    • Dutta, D.1    Kaushal, D.C.2    Ware, L.A.3    Puri, S.K.4    Kaushal, N.A.5    Narula, A.6    Upadhyaya, D.S.7    Lanar, D.E.8
  • 12
    • 0030047110 scopus 로고    scopus 로고
    • Clinical immunity to Plasmodium falciparum malaria is associated with serum antibodies to the 19-kDa C-terminal fragment of the merozoite surface antigen PfMSP-1
    • Egan A.F., Morris J., Barnish G., Saul A., Greenwood B.M., Kaslow D.C., Holder A.A., and Riley E.M. Clinical immunity to Plasmodium falciparum malaria is associated with serum antibodies to the 19-kDa C-terminal fragment of the merozoite surface antigen PfMSP-1. J. Infect. Dis. 173 (1996) 765-769
    • (1996) J. Infect. Dis. , vol.173 , pp. 765-769
    • Egan, A.F.1    Morris, J.2    Barnish, G.3    Saul, A.4    Greenwood, B.M.5    Kaslow, D.C.6    Holder, A.A.7    Riley, E.M.8
  • 13
    • 0023707175 scopus 로고
    • Plasmodium falciparum: gene structure and hydropathy profile of the major merozoite surface antigen (gp195) of the Uganda-Palo Alto isolate
    • Chang S.P., Kramer K.J., Yamaga K.M., Kato A., Case S.E., and Siddiqui W.A. Plasmodium falciparum: gene structure and hydropathy profile of the major merozoite surface antigen (gp195) of the Uganda-Palo Alto isolate. Exp. Parasitol. 67 (1988) 1-11
    • (1988) Exp. Parasitol. , vol.67 , pp. 1-11
    • Chang, S.P.1    Kramer, K.J.2    Yamaga, K.M.3    Kato, A.4    Case, S.E.5    Siddiqui, W.A.6
  • 16
    • 33751406418 scopus 로고    scopus 로고
    • J.A. Stoute, J. Gombe, M.R. Withers, J. Siangla, D. McKinney, M. Onyango, J.F. Cummings, J. Milman, K. Tucker, L. Soisson,V.A. Stewart, J.A. Lyon, E. Angov, A. Leach, J. Cohen, K.E. Kester, C.F. Ochenhouse, C.A. Holland, C.L. Diggs, J. Wittes, D.G. Heppner Jr., Phase 1 randomized double-blind safety and immunogenicity trial of Plasmodium falciparum malaria merozoite surface protein FMP1 vaccine, adjuvanted with AS02A, in adults in western Kenya', Vaccine (2006), in press, doi:10.1016/J.Vaccine.2005.11.037.
  • 17
    • 0035543204 scopus 로고    scopus 로고
    • High-level production and purification of P30P2MSP1(19), an important vaccine antigen for malaria, expressed in the methylotropic yeast Pichia pastoris
    • Brady C.P., Shimp R.L., Miles A.P., Whitmore M., and Stowers A.W. High-level production and purification of P30P2MSP1(19), an important vaccine antigen for malaria, expressed in the methylotropic yeast Pichia pastoris. Protein Expr. Purif. 23 (2001) 468-475
    • (2001) Protein Expr. Purif. , vol.23 , pp. 468-475
    • Brady, C.P.1    Shimp, R.L.2    Miles, A.P.3    Whitmore, M.4    Stowers, A.W.5
  • 18
    • 4444243454 scopus 로고    scopus 로고
    • Determination of molecular masses of proteins in solution: implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory
    • Folta-Stogniew E., and Williams K.R. Determination of molecular masses of proteins in solution: implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory. J. Biomol. Tech. 10 (1999) 51-63
    • (1999) J. Biomol. Tech. , vol.10 , pp. 51-63
    • Folta-Stogniew, E.1    Williams, K.R.2
  • 19
    • 0036154258 scopus 로고    scopus 로고
    • size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems
    • Schuck P., Perugini M.A., Gonzales N.R., Howlett G.J., and Schubert D. size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems. Biophys. J. 82 (2002) 1096-1111
    • (2002) Biophys. J. , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 20
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: a tutorial review
    • Lebowitz J., Lewis M.S., and Schuck P. Modern analytical ultracentrifugation in protein science: a tutorial review. Protein Sci. 11 (2002) 2067-2079
    • (2002) Protein Sci. , vol.11 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 21
    • 32044443408 scopus 로고    scopus 로고
    • Overproduction of Pichia pastoris or Plasmodium falciparum protein disulfide isomerase affects expression, folding and O-linked glycosylation of a malaria vaccine candidate expressed in P. pastoris
    • Tsai C.W., Duggan P.F., Shimp Jr. R.L., Miller L.H., and Narum D.L. Overproduction of Pichia pastoris or Plasmodium falciparum protein disulfide isomerase affects expression, folding and O-linked glycosylation of a malaria vaccine candidate expressed in P. pastoris. J. Biotechnol. 121 (2006) 458-470
    • (2006) J. Biotechnol. , vol.121 , pp. 458-470
    • Tsai, C.W.1    Duggan, P.F.2    Shimp Jr., R.L.3    Miller, L.H.4    Narum, D.L.5
  • 22
    • 3242698844 scopus 로고    scopus 로고
    • Characterization of a lysyl aminopeptidase activity associated with phosphoglucose isomerase of Vibrio vulnificus
    • Richards G.P., Hammer C.H., Garfield M.K., and Parveen S. Characterization of a lysyl aminopeptidase activity associated with phosphoglucose isomerase of Vibrio vulnificus. Biochim. Biophys. Acta 1700 (2004) 219-229
    • (2004) Biochim. Biophys. Acta , vol.1700 , pp. 219-229
    • Richards, G.P.1    Hammer, C.H.2    Garfield, M.K.3    Parveen, S.4
  • 23
    • 0000631035 scopus 로고
    • The role of endotoxin in the extracellular coagulation of limulus blood
    • Levin J., and Bang F.B. The role of endotoxin in the extracellular coagulation of limulus blood. Bull. Johns Hopkins Hosp. 115 (1964) 265-274
    • (1964) Bull. Johns Hopkins Hosp. , vol.115 , pp. 265-274
    • Levin, J.1    Bang, F.B.2
  • 24
    • 0015375454 scopus 로고
    • The Limulus test for endotoxin (Pyrogen) in radiopharmaceuticals and biologicals
    • Cooper J.F., Hochstein H.D., and Seligmann Jr. E.B. The Limulus test for endotoxin (Pyrogen) in radiopharmaceuticals and biologicals. Bull. Parenter Drug Assoc. 26 (1972) 153-162
    • (1972) Bull. Parenter Drug Assoc. , vol.26 , pp. 153-162
    • Cooper, J.F.1    Hochstein, H.D.2    Seligmann Jr., E.B.3
  • 25
    • 24344496154 scopus 로고    scopus 로고
    • Determining residual host cell antigen levels in purified recombinant proteins by slot blot and scanning laser densitometry
    • Miles A.P., Zhu D., and Saul A.J. Determining residual host cell antigen levels in purified recombinant proteins by slot blot and scanning laser densitometry. Methods Mol. Biol. 308 (2005) 233-242
    • (2005) Methods Mol. Biol. , vol.308 , pp. 233-242
    • Miles, A.P.1    Zhu, D.2    Saul, A.J.3
  • 26
    • 28444439937 scopus 로고    scopus 로고
    • A quantitative slot blot assay for host cell protein impurities in recombinant protein expressed in E. coli
    • Zhu D., Saul A.J., and Miles A.P. A quantitative slot blot assay for host cell protein impurities in recombinant protein expressed in E. coli. JIM 306 (2005) 40-50
    • (2005) JIM , vol.306 , pp. 40-50
    • Zhu, D.1    Saul, A.J.2    Miles, A.P.3
  • 27
    • 0027225715 scopus 로고    scopus 로고
    • Monoclonal antibodies inhibit Plasmodium falciparum invasion in vitro recognize the first growth factor-like domain of merozoite surface protein-1
    • Chappel J.A., and Holder A.A. Monoclonal antibodies inhibit Plasmodium falciparum invasion in vitro recognize the first growth factor-like domain of merozoite surface protein-1. Mol. Biochem. Parasitol. 60 (2003) 303-312
    • (2003) Mol. Biochem. Parasitol. , vol.60 , pp. 303-312
    • Chappel, J.A.1    Holder, A.A.2
  • 29
    • 0028053015 scopus 로고
    • Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation
    • Mazel D., Pochet S., and Marliere P. Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation. EMBO J. 13 (1994) 914-923
    • (1994) EMBO J. , vol.13 , pp. 914-923
    • Mazel, D.1    Pochet, S.2    Marliere, P.3
  • 30
    • 1442274756 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition
    • Vistica J., Dam J., Balbo A., Yikilmaz E., Mariuzza R.A., Rouault T.A., and Schuck P. Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition. Anal. Biochem. 326 (2004) 234-256
    • (2004) Anal. Biochem. , vol.326 , pp. 234-256
    • Vistica, J.1    Dam, J.2    Balbo, A.3    Yikilmaz, E.4    Mariuzza, R.A.5    Rouault, T.A.6    Schuck, P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.