메뉴 건너뛰기




Volumn 25, Issue 1, 2002, Pages 87-96

Large-scale purification and characterization of malaria vaccine candidate antigen Pvs25H for use in clinical trials

Author keywords

[No Author keywords available]

Indexed keywords

PLASMODIUM VIVAX; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE; SACCHAROMYCETALES;

EID: 0036931119     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2001.1613     Document Type: Article
Times cited : (36)

References (14)
  • 2
    • 0013842098 scopus 로고
    • Chloroquine-resistant falciparum malaria in Thailand
    • Harinasuta, T., Suntharasamai, P., and Viravan, C. (1965) Chloroquine-resistant falciparum malaria in Thailand. Lancet 2, 657-660.
    • (1965) Lancet , vol.2 , pp. 657-660
    • Harinasuta, T.1    Suntharasamai, P.2    Viravan, C.3
  • 3
    • 0024387301 scopus 로고
    • Plasmodium vivax resistance to chloroquine?
    • Rieckmann, K. H., Davis, D. R., and Hutton, D. C. (1989) Plasmodium vivax resistance to chloroquine? Lancet 2, 1183-1184.
    • (1989) Lancet , vol.2 , pp. 1183-1184
    • Rieckmann, K.H.1    Davis, D.R.2    Hutton, D.C.3
  • 4
    • 0028290195 scopus 로고
    • Insecticide resistance issues in vector-borne disease control
    • Roberts, D. R., and Andre, R. G. (1994) Insecticide resistance issues in vector-borne disease control. Am. J. Trop. Med. Hyg. 50, 21-34.
    • (1994) Am. J. Trop. Med. Hyg. , vol.50 , pp. 21-34
    • Roberts, D.R.1    Andre, R.G.2
  • 5
    • 0031921082 scopus 로고    scopus 로고
    • Pathways and strategies for developing a malaria blood-stage vaccine
    • Good, M. F., Kaslow, D. C., and Miller, L. H. (1998) Pathways and strategies for developing a malaria blood-stage vaccine. Annu. Rev. Immunol. 16, 57-87.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 57-87
    • Good, M.F.1    Kaslow, D.C.2    Miller, L.H.3
  • 6
    • 0031060905 scopus 로고    scopus 로고
    • Transmission-blocking vaccines: Uses and current status of development
    • Kaslow, D. C. (1997) Transmission-blocking vaccines: Uses and current status of development. Int. J. Parasitol. 27, 183-189.
    • (1997) Int. J. Parasitol. , vol.27 , pp. 183-189
    • Kaslow, D.C.1
  • 7
    • 0032427485 scopus 로고    scopus 로고
    • Sequence polymorphism in two novel Plasmodium vivax ookinete surface proteins, Pvs25 and Pvs28, that are malaria transmission-blocking vaccine candidates
    • Tsuboi, T., Kaslow, D. C., Gozar, M. M., Tachibana, M., Cao, Y. M., and Torii, M. (1998) Sequence polymorphism in two novel Plasmodium vivax ookinete surface proteins, Pvs25 and Pvs28, that are malaria transmission-blocking vaccine candidates. Mol. Med. 4, 772-782.
    • (1998) Mol. Med. , vol.4 , pp. 772-782
    • Tsuboi, T.1    Kaslow, D.C.2    Gozar, M.M.3    Tachibana, M.4    Cao, Y.M.5    Torii, M.6
  • 8
    • 0034445516 scopus 로고    scopus 로고
    • Antibodies to malaria vaccine candidates pvs25 and pvs28 completely block the ability of Plasmodium vivax to infect mosquitoes
    • Hisaeda, H., Stowers, A. W., Tsuboi, T., Collins, W. E., Sattabongkot, J. S., Suwanabun, N., Torii, M., and Kaslow, D. C. (2000) Antibodies to malaria vaccine candidates pvs25 and pvs28 completely block the ability of Plasmodium vivax to infect mosquitoes. Infect. Immun. 68, 6618-6623.
    • (2000) Infect. Immun. , vol.68 , pp. 6618-6623
    • Hisaeda, H.1    Stowers, A.W.2    Tsuboi, T.3    Collins, W.E.4    Sattabongkot, J.S.5    Suwanabun, N.6    Torii, M.7    Kaslow, D.C.8
  • 9
    • 0035970019 scopus 로고    scopus 로고
    • Structural conformers produced during malarial vaccine production in yeast
    • Stowers, A. W., Zhang, Y., Shimp, R. L., and Kaslow, D. C. (2001) Structural conformers produced during malarial vaccine production in yeast. Yeast 18, 137-150.
    • (2001) Yeast , vol.18 , pp. 137-150
    • Stowers, A.W.1    Zhang, Y.2    Shimp, R.L.3    Kaslow, D.C.4
  • 10
    • 0032866084 scopus 로고    scopus 로고
    • Phase I trial of two recombinant vaccines containing the 19kd carboxy terminal fragment of Plasmodium falciparum merozoite surface protein 1 (msp-1(19)) and T helper epitopes of tetanus toxoid
    • Keitel, W. A., Kester, K. E., Atmar, R. L., White, A. C., Bond, N. H., Holland, C. A., Krzych, U., Palmer, D. R., Egan, A., Diggs, C., Ballou, W. R., Hall, B. F., and Kaslow, D. (1999) Phase I trial of two recombinant vaccines containing the 19kd carboxy terminal fragment of Plasmodium falciparum merozoite surface protein 1 (msp-1(19)) and T helper epitopes of tetanus toxoid. Vaccine 18, 531-539.
    • (1999) Vaccine , vol.18 , pp. 531-539
    • Keitel, W.A.1    Kester, K.E.2    Atmar, R.L.3    White, A.C.4    Bond, N.H.5    Holland, C.A.6    Krzych, U.7    Palmer, D.R.8    Egan, A.9    Diggs, C.10    Ballou, W.R.11    Hall, B.F.12    Kaslow, D.13
  • 11
    • 0033797216 scopus 로고    scopus 로고
    • A region of plasmodium falciparum antigen pfs25 that is the target of highly potent transmission-blocking antibodies
    • Stowers, A. W., Keister, D. B., Muratova, O., and Kaslow, D. C. (2000) A region of plasmodium falciparum antigen pfs25 that is the target of highly potent transmission-blocking antibodies [in process citation]. Infect. Immun. 68, 5530-5538.
    • (2000) Infect. Immun. , vol.68 , pp. 5530-5538
    • Stowers, A.W.1    Keister, D.B.2    Muratova, O.3    Kaslow, D.C.4
  • 12
    • 0028353230 scopus 로고
    • Production, purification and immunogenicity of a malaria transmission-blocking vaccine candidate: TBV25H expressed in yeast and purified using nickel-NTA agarose
    • Kaslow, D. C., and Shiloach, J. (1994) Production, purification and immunogenicity of a malaria transmission-blocking vaccine candidate: TBV25H expressed in yeast and purified using nickel-NTA agarose. Biotechnology (N.Y.) 12, 494-499.
    • (1994) Biotechnology (N.Y.) , vol.12 , pp. 494-499
    • Kaslow, D.C.1    Shiloach, J.2
  • 13
    • 0019579733 scopus 로고
    • The role of the hydroxy amino acid in the triplet sequence Asn-Xaa-Thr(Ser) for the N-glycosylation step during glycoprotein biosynthesis
    • Bause, E., and Legler, G. (1981) The role of the hydroxy amino acid in the triplet sequence Asn-Xaa-Thr(Ser) for the N-glycosylation step during glycoprotein biosynthesis. Biochem. J. 195, 639-644.
    • (1981) Biochem. J. , vol.195 , pp. 639-644
    • Bause, E.1    Legler, G.2
  • 14
    • 0025297484 scopus 로고
    • Beta protein C is not glycosylated at asparagine 329: The rate of translation may influence the frequency of usage at asparagine-X-cysteine sites
    • Miletich, J. P., and Broze, G. J., Jr. (1990) Beta protein C is not glycosylated at asparagine 329: The rate of translation may influence the frequency of usage at asparagine-X-cysteine sites. J. Biol. Chem. 265, 11397-11404.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11397-11404
    • Miletich, J.P.1    Broze G.J., Jr.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.