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Volumn 24, Issue 22, 2006, Pages 4716-4726

A synthetic dengue virus antigen elicits enhanced antibody titers when linked to, but not mixed with, Mycobacterium tuberculosis HSP70 domain II

Author keywords

Dengue virus; HSP70; Immune response; Immunodominant epitopes; Mycobacterium tuberculosis

Indexed keywords

AMINO ACID; HEAT SHOCK PROTEIN 70; PLASMID VECTOR; RECOMBINANT DENGUE MULTIEPITOPE IMMUNOGLOBULIN G VACCINE; RECOMBINANT VACCINE; UNCLASSIFIED DRUG; VIRUS ANTIGEN;

EID: 33646832928     PISSN: 0264410X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vaccine.2006.03.030     Document Type: Article
Times cited : (9)

References (34)
  • 1
    • 0036468861 scopus 로고    scopus 로고
    • Epidemic dengue/dengue hemorrhagic fever as a public health, social and economic problem in the 21st century
    • Gubler D.J. Epidemic dengue/dengue hemorrhagic fever as a public health, social and economic problem in the 21st century. Trends Microbiol 10 (2002) 100-103
    • (2002) Trends Microbiol , vol.10 , pp. 100-103
    • Gubler, D.J.1
  • 2
    • 0037193818 scopus 로고    scopus 로고
    • Dengue: an escalating problem
    • Gibbons R.V., and Vaughn D.W. Dengue: an escalating problem. Brit Med J 324 (2002) 1563-1566
    • (2002) Brit Med J , vol.324 , pp. 1563-1566
    • Gibbons, R.V.1    Vaughn, D.W.2
  • 4
    • 0000163169 scopus 로고    scopus 로고
    • Flaviviridae: the viruses and their replication
    • Knipe D.M., and Howley P.M. (Eds), Lippincott Williams & Wilkins, Philadelphia, PA
    • Lindenbach B.D., and Rice C.M. Flaviviridae: the viruses and their replication. In: Knipe D.M., and Howley P.M. (Eds). Field's Virology. 4th ed. (2001), Lippincott Williams & Wilkins, Philadelphia, PA 991-1041
    • (2001) Field's Virology. 4th ed. , pp. 991-1041
    • Lindenbach, B.D.1    Rice, C.M.2
  • 5
    • 0037805585 scopus 로고    scopus 로고
    • Vaccines for the prevention of neglected diseases-dengue fever
    • Pang T. Vaccines for the prevention of neglected diseases-dengue fever. Curr Opin Biotechnol 14 (2003) 332-336
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 332-336
    • Pang, T.1
  • 6
    • 10444256421 scopus 로고    scopus 로고
    • Halstead SB, Heinz FX, Barrett ADT, Roehrig JT. Conference report on Dengue virus: molecular basis of cell entry and pathogenesis, 25-27 June 2003. Vienna, Austria. Vaccine 2005; 23: 849-56.
  • 7
    • 15044359108 scopus 로고    scopus 로고
    • Hombach J, Barrett AD, Cardosa MJ, Deubel V, Guzman M, Kurane I, et al. Meeting report "Review on flavivirus vaccine development: proceedings of a meeting jointly organized by the World Health Organization and the Thai ministry of public health", 26-27 April 2004. Bangkok, Thailand. Vaccine 2005; 23: 2689-95.
  • 8
    • 2142827156 scopus 로고    scopus 로고
    • Dengue: defining protective versus pathologic immunity
    • Rothman A.L. Dengue: defining protective versus pathologic immunity. J Clin Invest 113 (2004) 946-951
    • (2004) J Clin Invest , vol.113 , pp. 946-951
    • Rothman, A.L.1
  • 9
    • 0037136939 scopus 로고    scopus 로고
    • The future of dengue vaccines
    • Halstead S.B., and Deen J. The future of dengue vaccines. Lancet 360 (2002) 1243-1245
    • (2002) Lancet , vol.360 , pp. 1243-1245
    • Halstead, S.B.1    Deen, J.2
  • 10
    • 0025945430 scopus 로고
    • Dengue virus premembrane and membrane proteins elicit a protective immune response
    • Bray M., and Lai C.J. Dengue virus premembrane and membrane proteins elicit a protective immune response. Virology 185 (1991) 505-508
    • (1991) Virology , vol.185 , pp. 505-508
    • Bray, M.1    Lai, C.J.2
  • 11
    • 0028039833 scopus 로고
    • Recombinant vaccinia viruses co-expressing dengue-1 glycoproteins prM and E induce neutralizing antibodies in mice
    • Fonseca B.A.L., Pincus S., Shope R.E., Paoletti E., and Mason P.W. Recombinant vaccinia viruses co-expressing dengue-1 glycoproteins prM and E induce neutralizing antibodies in mice. Vaccine 12 (1994) 279-285
    • (1994) Vaccine , vol.12 , pp. 279-285
    • Fonseca, B.A.L.1    Pincus, S.2    Shope, R.E.3    Paoletti, E.4    Mason, P.W.5
  • 12
    • 0027977656 scopus 로고
    • Precise location of sequential dengue virus subcomplex and complex B cell epitopes on the non-structural-1 glycoprotein
    • Falconar A.K.I., Young P.R., and Miles M.A. Precise location of sequential dengue virus subcomplex and complex B cell epitopes on the non-structural-1 glycoprotein. Arch Virol 137 (1994) 315-326
    • (1994) Arch Virol , vol.137 , pp. 315-326
    • Falconar, A.K.I.1    Young, P.R.2    Miles, M.A.3
  • 13
    • 0030988913 scopus 로고    scopus 로고
    • Recognition of synthetic oligopeptides from non-structural proteins NS1 and NS3 of dengue-4 virus by sera from dengue virus-infected children
    • Garcia G., Vaughn D.W., and Del Angel R.M. Recognition of synthetic oligopeptides from non-structural proteins NS1 and NS3 of dengue-4 virus by sera from dengue virus-infected children. Am J Trop Med Hyg 56 4 (1997) 466-470
    • (1997) Am J Trop Med Hyg , vol.56 , Issue.4 , pp. 466-470
    • Garcia, G.1    Vaughn, D.W.2    Del Angel, R.M.3
  • 14
    • 0032889977 scopus 로고    scopus 로고
    • Antibody responses to an immunodominant non-structural 1 synthetic peptide in patients with dengue fever and dengue hemorrhagic fever
    • Huang J.H., Wey J.J., Sun Y.C., Chin C., Chien L.J., and Wu Y.C. Antibody responses to an immunodominant non-structural 1 synthetic peptide in patients with dengue fever and dengue hemorrhagic fever. J Med Virol 57 (1999) 1-8
    • (1999) J Med Virol , vol.57 , pp. 1-8
    • Huang, J.H.1    Wey, J.J.2    Sun, Y.C.3    Chin, C.4    Chien, L.J.5    Wu, Y.C.6
  • 15
    • 0032101221 scopus 로고    scopus 로고
    • Heat shock proteins come of age: primitive functions acquire new roles in an adaptive world
    • Srivastava P.K., Menoret A., Basu S., Binder R.J., and McQuade K.L. Heat shock proteins come of age: primitive functions acquire new roles in an adaptive world. Immunity 8 (1998) 657-665
    • (1998) Immunity , vol.8 , pp. 657-665
    • Srivastava, P.K.1    Menoret, A.2    Basu, S.3    Binder, R.J.4    McQuade, K.L.5
  • 16
    • 0035925608 scopus 로고    scopus 로고
    • Heat shock proteins: the 'Swiss army knife' vaccines against cancers and infectious agents
    • Srivastava P.K., and Amato R.J. Heat shock proteins: the 'Swiss army knife' vaccines against cancers and infectious agents. Vaccine 19 (2001) 2590-2597
    • (2001) Vaccine , vol.19 , pp. 2590-2597
    • Srivastava, P.K.1    Amato, R.J.2
  • 17
    • 0042235547 scopus 로고    scopus 로고
    • Heat shock proteins as regulators of the immune response
    • Pockley A.G. Heat shock proteins as regulators of the immune response. Lancet 362 (2003) 469-476
    • (2003) Lancet , vol.362 , pp. 469-476
    • Pockley, A.G.1
  • 18
    • 0037409604 scopus 로고    scopus 로고
    • Evolution of heat shock protein and immunity
    • Robert J. Evolution of heat shock protein and immunity. Dev Comp Immunol 27 (2003) 449-464
    • (2003) Dev Comp Immunol , vol.27 , pp. 449-464
    • Robert, J.1
  • 19
    • 0038737428 scopus 로고    scopus 로고
    • Role of heat shock proteins in protection from and pathogenesis of infectious diseases
    • Zügel U., and Kaufmann S.H.E. Role of heat shock proteins in protection from and pathogenesis of infectious diseases. Clin Microbiol Rev 12 (1999) 19-39
    • (1999) Clin Microbiol Rev , vol.12 , pp. 19-39
    • Zügel, U.1    Kaufmann, S.H.E.2
  • 20
    • 0026343040 scopus 로고
    • Biological role and regulation of the universally conserved heat shock proteins
    • Ang D., Liberek K., Skowyra D., Zylicz M., and Georgeopoulos C. Biological role and regulation of the universally conserved heat shock proteins. J Biol Chem 266 (1991) 24233-24236
    • (1991) J Biol Chem , vol.266 , pp. 24233-24236
    • Ang, D.1    Liberek, K.2    Skowyra, D.3    Zylicz, M.4    Georgeopoulos, C.5
  • 21
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething M.J., and Sambrook J. Protein folding in the cell. Nature 355 (1992) 33-45
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 22
    • 0031964659 scopus 로고    scopus 로고
    • Characterization of the immunostimulatory properties of Leishmania infantum HSP70 by fusion to the Escherichia coli maltose-binding protein in normal and nu/nu BALB/c mice
    • Rico A.I., Del Real G., Soto M., Quijada L., Martinez-A C., Alonso C., et al. Characterization of the immunostimulatory properties of Leishmania infantum HSP70 by fusion to the Escherichia coli maltose-binding protein in normal and nu/nu BALB/c mice. Infect Immun 66 (1998) 347-352
    • (1998) Infect Immun , vol.66 , pp. 347-352
    • Rico, A.I.1    Del Real, G.2    Soto, M.3    Quijada, L.4    Martinez-A, C.5    Alonso, C.6
  • 23
    • 0030667939 scopus 로고    scopus 로고
    • Heat shock protein fusion proteins as vehicles for antigen delivery into the major histocompatibility complex class I presentation pathway
    • Suzue K., Zhou X., Eisen H.N., and Young R.A. Heat shock protein fusion proteins as vehicles for antigen delivery into the major histocompatibility complex class I presentation pathway. Proc Natl Acad Sci USA 94 (1997) 13146-13151
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13146-13151
    • Suzue, K.1    Zhou, X.2    Eisen, H.N.3    Young, R.A.4
  • 24
    • 0034652784 scopus 로고    scopus 로고
    • Enhancement of DNA vaccine potency by linkage of antigen gene to an HSP70 gene
    • Chen C.H., Wang T.L., Hung C.F., Yang Y., Young R.A., Pardoll D.M., et al. Enhancement of DNA vaccine potency by linkage of antigen gene to an HSP70 gene. Cancer Res 60 (2000) 1035-1042
    • (2000) Cancer Res , vol.60 , pp. 1035-1042
    • Chen, C.H.1    Wang, T.L.2    Hung, C.F.3    Yang, Y.4    Young, R.A.5    Pardoll, D.M.6
  • 25
    • 0141625683 scopus 로고    scopus 로고
    • Augmentation of DNA vaccine potency through secretory heat shock protein-mediated antigen targeting
    • Hauser H., and Chen S.Y. Augmentation of DNA vaccine potency through secretory heat shock protein-mediated antigen targeting. Methods 31 (2003) 225-231
    • (2003) Methods , vol.31 , pp. 225-231
    • Hauser, H.1    Chen, S.Y.2
  • 26
    • 0030028801 scopus 로고    scopus 로고
    • Adjuvant-free HSP70 fusion protein system elicits humoral and cellular responses to HIV-1 p24
    • Suzue K., and Young R.A. Adjuvant-free HSP70 fusion protein system elicits humoral and cellular responses to HIV-1 p24. J Immunol 156 (1996) 873-879
    • (1996) J Immunol , vol.156 , pp. 873-879
    • Suzue, K.1    Young, R.A.2
  • 28
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty K.M., DeLuca-Flaherty C., and McKay D.B. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346 (1990) 623-628
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3
  • 29
    • 15744401409 scopus 로고    scopus 로고
    • A custom-designed recombinant multiepitope protein as a dengue diagnostic reagent
    • AnandaRao R., Swaminathan S., Fernando S., Jana A.M., and Khanna N. A custom-designed recombinant multiepitope protein as a dengue diagnostic reagent. Protein Exp Purif 41 (2005) 136-147
    • (2005) Protein Exp Purif , vol.41 , pp. 136-147
    • AnandaRao, R.1    Swaminathan, S.2    Fernando, S.3    Jana, A.M.4    Khanna, N.5
  • 31
    • 0346966132 scopus 로고    scopus 로고
    • High-level expression and one-step purification of recombinant dengue virus type-2 envelope domain III protein in Escherichia coli
    • Jaiswal S., Khanna N., and Swaminathan S. High-level expression and one-step purification of recombinant dengue virus type-2 envelope domain III protein in Escherichia coli. Protein Exp Purif 33 (2004) 80-91
    • (2004) Protein Exp Purif , vol.33 , pp. 80-91
    • Jaiswal, S.1    Khanna, N.2    Swaminathan, S.3
  • 32
    • 0037062617 scopus 로고    scopus 로고
    • The Mycobacterium leprae HSP65 displays proteolytic activity. Mutagenesis studies indicate that M. leprae hsp65 proteolytic activity is catalytically related to the Hs1VU protease
    • Portaro F.C.V., Hayashi M.A.F., de Arauz L.J., Palma M.S., Assakura M.T., Silva C.L., et al. The Mycobacterium leprae HSP65 displays proteolytic activity. Mutagenesis studies indicate that M. leprae hsp65 proteolytic activity is catalytically related to the Hs1VU protease. Biochemistry 41 (2002) 7400-7406
    • (2002) Biochemistry , vol.41 , pp. 7400-7406
    • Portaro, F.C.V.1    Hayashi, M.A.F.2    de Arauz, L.J.3    Palma, M.S.4    Assakura, M.T.5    Silva, C.L.6
  • 33
    • 3843105896 scopus 로고    scopus 로고
    • Long-lasting specific antibodies against CETP induced by subcutaneous and mucosal administration of a 26-aminoacid CETP epitope carried by heat shock protein 65 kDa in the absence of adjuvants
    • Gaofu Q., Dan M., Jie W., Liao Z., Li Z., Roque R.S., et al. Long-lasting specific antibodies against CETP induced by subcutaneous and mucosal administration of a 26-aminoacid CETP epitope carried by heat shock protein 65 kDa in the absence of adjuvants. Vaccine 22 (2004) 3187-3194
    • (2004) Vaccine , vol.22 , pp. 3187-3194
    • Gaofu, Q.1    Dan, M.2    Jie, W.3    Liao, Z.4    Li, Z.5    Roque, R.S.6
  • 34
    • 0035825064 scopus 로고    scopus 로고
    • Heat shock protein-peptide complexes elicit cytotoxic T-lymphocyte and antibody responses specific for bovine herpesvirus 1
    • Navaratnam M., Deshpande M.S., Hariharan M.J., Zatechka Jr. D.S., and Srikumaran S. Heat shock protein-peptide complexes elicit cytotoxic T-lymphocyte and antibody responses specific for bovine herpesvirus 1. Vaccine 19 (2001) 1425-1434
    • (2001) Vaccine , vol.19 , pp. 1425-1434
    • Navaratnam, M.1    Deshpande, M.S.2    Hariharan, M.J.3    Zatechka Jr., D.S.4    Srikumaran, S.5


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