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Volumn 34, Issue 9, 2017, Pages 1970-1983

Expression, Purification and Characterization of GMZ2’.10C, a Complex Disulphide-Bonded Fusion Protein Vaccine Candidate against the Asexual and Sexual Life-Stages of the Malaria-Causing Plasmodium falciparum Parasite

Author keywords

disulphide bond mapping; malaria vaccine; mass spectrometry of biopharmaceuticals; Pfs48 45; production and stability analysis of biopharmaceuticals

Indexed keywords

DISULPHIDE BONDED FUSION PROTEIN VACCINE; HYBRID PROTEIN; MALARIA VACCINE; UNCLASSIFIED DRUG; PARASITE ANTIGEN; PROTOZOAL PROTEIN;

EID: 85021188094     PISSN: 07248741     EISSN: 1573904X     Source Type: Journal    
DOI: 10.1007/s11095-017-2208-1     Document Type: Article
Times cited : (10)

References (40)
  • 1
    • 84976242105 scopus 로고    scopus 로고
    • Geneva, Switzerland: World Health Organization, 2015 December
    • WHO. World Malaria Report 2015. Geneva, Switzerland: World Health Organization, 2015 December. Report No.: 8.
    • (2015) Report No. , pp. 8
  • 4
    • 0034078401 scopus 로고    scopus 로고
    • Naturally acquired antibodies to the glutamate-rich protein are associated with protection against Plasmodium falciparum malaria
    • COI: 1:CAS:528:DC%2BD3cXivVOns7o%3D, PID: 10720556
    • Dodoo D, Theisen M, Kurtzhals JA, Akanmori BD, Koram KA, Jepsen S, et al. Naturally acquired antibodies to the glutamate-rich protein are associated with protection against Plasmodium falciparum malaria. J Infect Dis. 2000;181(3):1202–5.
    • (2000) J Infect Dis , vol.181 , Issue.3 , pp. 1202-1205
    • Dodoo, D.1    Theisen, M.2    Kurtzhals, J.A.3    Akanmori, B.D.4    Koram, K.A.5    Jepsen, S.6    Nkrumah, F.K.7    Theander, T.G.8    Hviid, L.9
  • 5
  • 6
    • 0027989813 scopus 로고
    • Merozoite surface protein-3: a malaria protein inducing antibodies that promote Plasmodium falciparum killing by cooperation with blood monocytes
    • COI: 1:CAS:528:DyaK2cXmtVartbk%3D, PID: 8068948
    • Oeuvray C, Bouharoun-Tayoun H, Gras-Masse H, Bottius E, Kaidoh T, Aikawa M, et al. Merozoite surface protein-3: a malaria protein inducing antibodies that promote Plasmodium falciparum killing by cooperation with blood monocytes. Blood. 1994;84:1594–602.
    • (1994) Blood , vol.84 , pp. 1594-1602
    • Oeuvray, C.1    Bouharoun-Tayoun, H.2    Gras-Masse, H.3    Bottius, E.4    Kaidoh, T.5    Aikawa, M.6    Filgueira, M.C.7    Tartar, A.8    Druilhe, P.9
  • 7
    • 0348141901 scopus 로고    scopus 로고
    • Association between protection against clinical malaria and antibodies to merozoite surface antigens in an area of hyperendemicity in Myanmar: complementarity between responses to merozoite surface protein 3 and the 220-kilodalton glutamate-rich protein
    • COI: 1:CAS:528:DC%2BD2cXpvFek, PID: 14688102
    • Soe S, Theisen M, Roussilhon C, Aye KS, Druilhe P. Association between protection against clinical malaria and antibodies to merozoite surface antigens in an area of hyperendemicity in Myanmar: complementarity between responses to merozoite surface protein 3 and the 220-kilodalton glutamate-rich protein. Infect Immun. 2004;72(1):247–52.
    • (2004) Infect Immun , vol.72 , Issue.1 , pp. 247-252
    • Soe, S.1    Theisen, M.2    Roussilhon, C.3    Aye, K.S.4    Druilhe, P.5
  • 9
    • 0031975242 scopus 로고    scopus 로고
    • The glutamate-rich protein (GLURP) of Plasmodium falciparum is a target for antibody-dependent monocyte-mediated inhibition of parasite growth in vitro
    • COI: 1:CAS:528:DyaK1cXnsl2q, PID: 9423833
    • Theisen M, Soe S, Oeuvray C, Thomas AW, Vuust J, Danielsen S, et al. The glutamate-rich protein (GLURP) of Plasmodium falciparum is a target for antibody-dependent monocyte-mediated inhibition of parasite growth in vitro. Infect Immun. 1998;66(1):11–7.
    • (1998) Infect Immun , vol.66 , Issue.1 , pp. 11-17
    • Theisen, M.1    Soe, S.2    Oeuvray, C.3    Thomas, A.W.4    Vuust, J.5    Danielsen, S.6    Jepsen, S.7    Druilhe, P.8
  • 11
    • 0022355221 scopus 로고
    • Sequential expression of antigens on sexual stages of Plasmodium falciparum accessible to transmission-blocking antibodies in the mosquito
    • COI: 1:STN:280:DyaL28%2FjsF2gsQ%3D%3D, PID: 2865324
    • Vermeulen AN, Ponnudurai T, Beckers P, Verhave J, Smits M, Meuwissen J. Sequential expression of antigens on sexual stages of Plasmodium falciparum accessible to transmission-blocking antibodies in the mosquito. J Exp Med. 1985;162(5):1460–76.
    • (1985) J Exp Med , vol.162 , Issue.5 , pp. 1460-1476
    • Vermeulen, A.N.1    Ponnudurai, T.2    Beckers, P.3    Verhave, J.4    Smits, M.5    Meuwissen, J.6
  • 12
    • 84933180087 scopus 로고    scopus 로고
    • A Plasmodium falciparum 48/45 single epitope R0.6C subunit protein elicits high levels of transmission blocking antibodies
    • COI: 1:CAS:528:DC%2BC2MXjsF2mt78%3D, PID: 25728318
    • Singh SK, Roeffen W, Andersen G, Bousema T, Christiansen M, Sauerwein R, et al. A Plasmodium falciparum 48/45 single epitope R0.6C subunit protein elicits high levels of transmission blocking antibodies. Vaccine. 2015;33(16):1981–6.
    • (2015) Vaccine , vol.33 , Issue.16 , pp. 1981-1986
    • Singh, S.K.1    Roeffen, W.2    Andersen, G.3    Bousema, T.4    Christiansen, M.5    Sauerwein, R.6    Theisen, M.7
  • 15
    • 26444605506 scopus 로고    scopus 로고
    • Structural models for the protein family characterized by gamete surface protein Pfs230 of Plasmodium falciparum
    • COI: 1:CAS:528:DC%2BD2MXhtVygtr%2FO, PID: 16155126
    • Gerloff DL, Creasey A, Maslau S, Carter R. Structural models for the protein family characterized by gamete surface protein Pfs230 of Plasmodium falciparum. Proc Natl Acad Sci U S A. 2005;102(38):13598–603.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.38 , pp. 13598-13603
    • Gerloff, D.L.1    Creasey, A.2    Maslau, S.3    Carter, R.4
  • 18
    • 0025144749 scopus 로고
    • Properties of epitopes of Pfs 48/45, a target of transmission blocking monoclonal antibodies, on gametes of different isolates of Plasmodium falciparum
    • COI: 1:CAS:528:DyaK3MXmtVGgtbw%3D
    • Carter R, Graves PM, Keister DB, Quakyi IA. Properties of epitopes of Pfs 48/45, a target of transmission blocking monoclonal antibodies, on gametes of different isolates of Plasmodium falciparum. Parasite Immununol. 1990;12(6):587–603.
    • (1990) Parasite Immununol , vol.12 , Issue.6 , pp. 587-603
    • Carter, R.1    Graves, P.M.2    Keister, D.B.3    Quakyi, I.A.4
  • 21
    • 84874109457 scopus 로고    scopus 로고
    • Heterologous expression of the C-terminal antigenic domain of the malaria vaccine candidate Pfs48/45 in the green algae Chlamydomonas reinhardtii
    • COI: 1:CAS:528:DC%2BC3sXitlCgtLc%3D, PID: 22592550
    • Jones CS, Luong T, Hannon M, Tran M, Gregory JA, Shen Z, et al. Heterologous expression of the C-terminal antigenic domain of the malaria vaccine candidate Pfs48/45 in the green algae Chlamydomonas reinhardtii. Appl Microbiol Biotechnol. 2013;97(5):1987–95.
    • (2013) Appl Microbiol Biotechnol , vol.97 , Issue.5 , pp. 1987-1995
    • Jones, C.S.1    Luong, T.2    Hannon, M.3    Tran, M.4    Gregory, J.A.5    Shen, Z.6    Briggs, S.P.7    Mayfield, S.P.8
  • 22
    • 84963540105 scopus 로고    scopus 로고
    • Synthetic TLR4 agonists enhance functional antibodies and CD4+ T-cell responses against the Plasmodium falciparum GMZ2.6C multi-stage vaccine antigen
    • COI: 1:CAS:528:DC%2BC28XksFKjtrc%3D, PID: 26994314
    • Baldwin SL, Roeffen W, Singh SK, Tiendrebeogo RW, Christiansen M, Beebe E, et al. Synthetic TLR4 agonists enhance functional antibodies and CD4+ T-cell responses against the Plasmodium falciparum GMZ2.6C multi-stage vaccine antigen. Vaccine. 2016;34(19):2207–15.
    • (2016) Vaccine , vol.34 , Issue.19 , pp. 2207-2215
    • Baldwin, S.L.1    Roeffen, W.2    Singh, S.K.3    Tiendrebeogo, R.W.4    Christiansen, M.5    Beebe, E.6    Carter, D.7    Fox, C.B.8    Howard, R.F.9    Reed, S.G.10
  • 23
    • 84896700545 scopus 로고    scopus 로고
    • Recombinant protein expression in Lactococcus lactis using the P170 expression system
    • PID: 24303789
    • Jørgensen CM, Vrang A, Madsen SM. Recombinant protein expression in Lactococcus lactis using the P170 expression system. FEMS Microbiol Lett. 2014;351(2):170–8.
    • (2014) FEMS Microbiol Lett , vol.351 , Issue.2 , pp. 170-178
    • Jørgensen, C.M.1    Vrang, A.2    Madsen, S.M.3
  • 24
    • 0029177438 scopus 로고
    • Transformation of Lactococcus by Electroporation. In: Nickoloff JA, editor. Electroporation protocols for microorganisms
    • COI: 1:CAS:528:DyaK2MXot1Cms7w%3D, PID: 7550735
    • Holo H, Nes IF. Transformation of Lactococcus by Electroporation. In: Nickoloff JA, editor. Electroporation protocols for microorganisms. Methods Mol Biol. 1995;47:195–9.
    • (1995) Methods Mol Biol , vol.47 , pp. 195-199
    • Holo, H.1    Nes, I.F.2
  • 25
    • 27344435737 scopus 로고    scopus 로고
    • Arginine as an effective additive in gel permeation chromatography
    • COI: 1:CAS:528:DC%2BD2MXhtFKmtLzF, PID: 16257288
    • Ejima D, Yumioka R, Arakawa T, Tsumoto K. Arginine as an effective additive in gel permeation chromatography. J Chromatogr A. 2005;1094(1):49–55.
    • (2005) J Chromatogr A , vol.1094 , Issue.1 , pp. 49-55
    • Ejima, D.1    Yumioka, R.2    Arakawa, T.3    Tsumoto, K.4
  • 26
    • 0034078401 scopus 로고    scopus 로고
    • Naturally acquired antibodies to the glutamate-rich protein are associated with protection against Plasmodium falciparum malaria
    • COI: 1:CAS:528:DC%2BD3cXivVOns7o%3D, PID: 10720556
    • Dodoo D, Theisen M, Kurtzhals JA, Akanmori BD, Koram KA, Jepsen S, et al. Naturally acquired antibodies to the glutamate-rich protein are associated with protection against Plasmodium falciparum malaria. J Infect Dis. 2000;181(3):1202–5.
    • (2000) J Infect Dis , vol.181 , Issue.3 , pp. 1202-1205
    • Dodoo, D.1    Theisen, M.2    Kurtzhals, J.A.3    Akanmori, B.D.4    Koram, K.A.5    Jepsen, S.6    Nkrumah, F.K.7    Theander, T.G.8    Hviid, L.9
  • 27
    • 0002322469 scopus 로고
    • On a test of whether one of two random variables is stochastically larger than the other
    • Mann HB, Whitney DR. On a test of whether one of two random variables is stochastically larger than the other. Ann Math Stat. 1947:50–60.
    • (1947) Ann Math Stat , pp. 50-60
    • Mann, H.B.1    Whitney, D.R.2
  • 28
    • 0006556045 scopus 로고
    • Immunoaffinity purification of factor IX (Christmas factor) by using conformation-specific antibodies directed against the factor IX-metal complex
    • COI: 1:CAS:528:DyaL2MXksFagtrs%3D, PID: 2408269
    • Liebman HA, Limentani SA, Furie BC, Furie B. Immunoaffinity purification of factor IX (Christmas factor) by using conformation-specific antibodies directed against the factor IX-metal complex. Proc Natl Acad Sci U S A. 1985;82(11):3879–83.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , Issue.11 , pp. 3879-3883
    • Liebman, H.A.1    Limentani, S.A.2    Furie, B.C.3    Furie, B.4
  • 30
    • 0028237472 scopus 로고
    • Immunoaffinity purification of recombinant hepatitis B surface antigen from yeast using a monoclonal antibody
    • COI: 1:CAS:528:DyaK2cXltVKisbw%3D, PID: 8069398
    • Agraz A, Duarte CA, Costa L, Pérez L, Páez R, Pujol V, et al. Immunoaffinity purification of recombinant hepatitis B surface antigen from yeast using a monoclonal antibody. J Chromatogr A. 1994;672(1):25–33.
    • (1994) J Chromatogr A , vol.672 , Issue.1 , pp. 25-33
    • Agraz, A.1    Duarte, C.A.2    Costa, L.3    Pérez, L.4    Páez, R.5    Pujol, V.6    Fontirrochi, G.7
  • 31
    • 84926283147 scopus 로고    scopus 로고
    • Getting to the core of protein pharmaceuticals – comprehensive structure analysis by mass spectrometry
    • COI: 1:CAS:528:DC%2BC2MXlt1equ74%3D, PID: 25791210
    • Leurs U, Mistarz UH, Rand KD. Getting to the core of protein pharmaceuticals – comprehensive structure analysis by mass spectrometry. Eur J Pharm Biopharm. 2015;93:95–109.
    • (2015) Eur J Pharm Biopharm , vol.93 , pp. 95-109
    • Leurs, U.1    Mistarz, U.H.2    Rand, K.D.3
  • 33
    • 84964475979 scopus 로고    scopus 로고
    • The role of structural proteomics in vaccine development: recent advances and future prospects
    • COI: 1:CAS:528:DC%2BC28XhvFahsw%3D%3D, PID: 26714563
    • Donnarumma D, Faleri A, Costantino P, Rappuoli R, Norais N. The role of structural proteomics in vaccine development: recent advances and future prospects. Expert Rev Proteomics. 2016;13(1):55–68.
    • (2016) Expert Rev Proteomics , vol.13 , Issue.1 , pp. 55-68
    • Donnarumma, D.1    Faleri, A.2    Costantino, P.3    Rappuoli, R.4    Norais, N.5
  • 34
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: an immunologic perspective
    • PID: 17025268
    • Rosenberg AS. Effects of protein aggregates: an immunologic perspective. AAPS J. 2006;8(3):E501–7.
    • (2006) AAPS J , vol.8 , Issue.3 , pp. E501-E507
    • Rosenberg, A.S.1
  • 35
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: a formulation challenge
    • PID: 15803194
    • Frøkjær S, Otzen DE. Protein drug stability: a formulation challenge. Nat Rev Drug Discov. 2005;4(4):298–306.
    • (2005) Nat Rev Drug Discov , vol.4 , Issue.4 , pp. 298-306
    • Frøkjær, S.1    Otzen, D.E.2
  • 36
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation
    • COI: 1:CAS:528:DC%2BD3sXnt1KitLY%3D, PID: 14567625
    • Chi EY, Krishnan S, Randolph TW, Carpenter JF. Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation. Pharm Res. 2003;20(9):1325–36.
    • (2003) Pharm Res , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 37
    • 84870952537 scopus 로고    scopus 로고
    • A review size-exclusion chromatography for the analysis of protein biotherapeutics and their aggregates
    • COI: 1:CAS:528:DC%2BC38Xhs1Sht7jP, PID: 23378719
    • Hong P, Koza S, Bouvier ES. A review size-exclusion chromatography for the analysis of protein biotherapeutics and their aggregates. J Liq Chromatogr Relat Technol. 2012;35(20):2923–50.
    • (2012) J Liq Chromatogr Relat Technol , vol.35 , Issue.20 , pp. 2923-2950
    • Hong, P.1    Koza, S.2    Bouvier, E.S.3
  • 39
    • 0021326226 scopus 로고
    • DARPP-32, a dopamine-and adenosine 3′: 5′-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus
    • COI: 1:CAS:528:DyaL2cXitVCju7k%3D, PID: 6319628
    • Hemmings H, Nairn A, Aswad D, Greengard P. DARPP-32, a dopamine-and adenosine 3′: 5′-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus. J Neurosci. 1984;4(1):99–110.
    • (1984) J Neurosci , vol.4 , Issue.1 , pp. 99-110
    • Hemmings, H.1    Nairn, A.2    Aswad, D.3    Greengard, P.4
  • 40
    • 0027362677 scopus 로고
    • Disulfide bonds and the stability of globular proteins
    • COI: 1:CAS:528:DyaK2cXitlygsbc%3D, PID: 8251931
    • Betz SF. Disulfide bonds and the stability of globular proteins. Protein Sci. 1993;2(10):1551–8.
    • (1993) Protein Sci , vol.2 , Issue.10 , pp. 1551-1558
    • Betz, S.F.1


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