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Volumn 1760, Issue 12, 2006, Pages 1884-1893

Tandem copies of a human rotavirus VP8 epitope can induce specific neutralizing antibodies in BALB/c mice

Author keywords

Antibody response; B and T cell epitope; Human rotavirus; Neutralization epitope; Peptide antigen; VP8

Indexed keywords

ANTIGEN; CARRIER PROTEIN; EPITOPE; GLUTAMINYLTYROSYLISOLEUCYLLYSYLALANYLASPARAGINYLSERYL LYSYLPHENYLALANYLISOLEUCYLGLYCYLISOLEUCYLTHREONYLGLUTAMYLLEUCINE; HYBRID PROTEIN; METHIONYLALANYLSERYLLEUCYLISOLEUCYLTYROSYLARGINYLGLUTAMINYLLEUCYLLEUCINE; NEUTRALIZING ANTIBODY; PEPTIDE ANTIBODY; PROTEIN SUBUNIT; ROTAVIRUS VACCINE; TETANUS TOXIN; THIOREDOXIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 33750610963     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2006.07.015     Document Type: Article
Times cited : (28)

References (51)
  • 1
    • 0033973780 scopus 로고    scopus 로고
    • Policy analysis of the use of hepatitis B, Haemophilus influenzae type B-, Streptococcus pneumoniae-conjugate, and rotavirus vaccines in national immunization schedules
    • Miller M.A., and McCann L. Policy analysis of the use of hepatitis B, Haemophilus influenzae type B-, Streptococcus pneumoniae-conjugate, and rotavirus vaccines in national immunization schedules. Health Econ. 9 (2000) 19-35
    • (2000) Health Econ. , vol.9 , pp. 19-35
    • Miller, M.A.1    McCann, L.2
  • 3
    • 1842510039 scopus 로고    scopus 로고
    • Isolation of monoclonal antibodies that neutralize human rotavirus
    • Higo-Moriguchi K., Akahori Y., Iba Y., Kurosawa Y., and Taniguchi K. Isolation of monoclonal antibodies that neutralize human rotavirus. J. Virol. 78 (2004) 3325-3332
    • (2004) J. Virol. , vol.78 , pp. 3325-3332
    • Higo-Moriguchi, K.1    Akahori, Y.2    Iba, Y.3    Kurosawa, Y.4    Taniguchi, K.5
  • 4
    • 0030939883 scopus 로고    scopus 로고
    • Oral delivery of antibodies-Future pharmacokinetic trends
    • Reilly R.M., Domingo R., and Sandhu J. Oral delivery of antibodies-Future pharmacokinetic trends. Clin. Pharmacokinet. 4 (1997) 313-323
    • (1997) Clin. Pharmacokinet. , vol.4 , pp. 313-323
    • Reilly, R.M.1    Domingo, R.2    Sandhu, J.3
  • 5
    • 0001659603 scopus 로고    scopus 로고
    • Knipe D.M., and Howley P.M. (Eds), Lippincott Williams and Wilkins, Philadelphia
    • Kapikian A.Z., Hoshino Y., and Chanock R.M. In: Knipe D.M., and Howley P.M. (Eds). Field's Virology. 4th Ed. (2001), Lippincott Williams and Wilkins, Philadelphia 1787-1833
    • (2001) Field's Virology. 4th Ed. , pp. 1787-1833
    • Kapikian, A.Z.1    Hoshino, Y.2    Chanock, R.M.3
  • 8
    • 0028858176 scopus 로고
    • Immunological response to recombinant VP8* subunit protein of bovine rotavirus in pregnant cattle
    • Lee J., Babiuk L.A., Harland R., Gibbons E., Elazhary Y., and Yoo D. Immunological response to recombinant VP8* subunit protein of bovine rotavirus in pregnant cattle. J. Gen. Virol. 76 (1995) 2477-2483
    • (1995) J. Gen. Virol. , vol.76 , pp. 2477-2483
    • Lee, J.1    Babiuk, L.A.2    Harland, R.3    Gibbons, E.4    Elazhary, Y.5    Yoo, D.6
  • 9
    • 0030906383 scopus 로고    scopus 로고
    • Maternal immunization of pregnant cattle with recombinant VP8* protein of bovine rotavirus elicits neutralizing antibodies to multiple serotypes. Colostral neutralizing antibody by rotavirus VP8*
    • Yoo D., Lee J., Harland R., Gibbons E., Elazhary Y., and Babiuk L.A. Maternal immunization of pregnant cattle with recombinant VP8* protein of bovine rotavirus elicits neutralizing antibodies to multiple serotypes. Colostral neutralizing antibody by rotavirus VP8*. Adv. Exp. Med. Biol. 412 (1997) 405-411
    • (1997) Adv. Exp. Med. Biol. , vol.412 , pp. 405-411
    • Yoo, D.1    Lee, J.2    Harland, R.3    Gibbons, E.4    Elazhary, Y.5    Babiuk, L.A.6
  • 10
    • 0033621293 scopus 로고    scopus 로고
    • Peroral immunization of microencapsulated human VP8 in combination with cholera toxin induces intestinal antibody responses
    • Kang D.K., Kim P.H., Ko E.J., Seo J.Y., Seong S.Y., Kim Y.H., Kwon I.C., Jeong S.Y., and Yang J.M. Peroral immunization of microencapsulated human VP8 in combination with cholera toxin induces intestinal antibody responses. Mol. Cells 9 (1999) 609-616
    • (1999) Mol. Cells , vol.9 , pp. 609-616
    • Kang, D.K.1    Kim, P.H.2    Ko, E.J.3    Seo, J.Y.4    Seong, S.Y.5    Kim, Y.H.6    Kwon, I.C.7    Jeong, S.Y.8    Yang, J.M.9
  • 11
    • 0033943573 scopus 로고    scopus 로고
    • Homotypic protection against rotavirus-induced diarrhea in infant mice breast-fed by dams immunized with the recombinant VP8* subunit of the VP4 capsid protein
    • Gil M.T., de Souza C.O., Asensi M., and Buesa J. Homotypic protection against rotavirus-induced diarrhea in infant mice breast-fed by dams immunized with the recombinant VP8* subunit of the VP4 capsid protein. Viral Immunol. 13 (2000) 187-200
    • (2000) Viral Immunol. , vol.13 , pp. 187-200
    • Gil, M.T.1    de Souza, C.O.2    Asensi, M.3    Buesa, J.4
  • 12
    • 0344393601 scopus 로고    scopus 로고
    • Fine mapping of sequential neutralization epitopes on the subunit protein VP8 of human rotavirus
    • Kovacs-Nolan J., Mine Y., and Yoo D. Fine mapping of sequential neutralization epitopes on the subunit protein VP8 of human rotavirus. Biochem. J. 376 (2003) 269-275
    • (2003) Biochem. J. , vol.376 , pp. 269-275
    • Kovacs-Nolan, J.1    Mine, Y.2    Yoo, D.3
  • 13
    • 0033042783 scopus 로고    scopus 로고
    • Design of highly immunogenic liposomal constructs combining structurally independent B cell and T helper cell peptide epitopes
    • Boeckler C., Dautel D., Schelte P., Frisch B., Wachsmann D., Klein J.P., and Schuber F. Design of highly immunogenic liposomal constructs combining structurally independent B cell and T helper cell peptide epitopes. Eur. J. Immunol. 29 (1999) 2297-2308
    • (1999) Eur. J. Immunol. , vol.29 , pp. 2297-2308
    • Boeckler, C.1    Dautel, D.2    Schelte, P.3    Frisch, B.4    Wachsmann, D.5    Klein, J.P.6    Schuber, F.7
  • 14
    • 33750628473 scopus 로고    scopus 로고
    • Synthetic peptides
    • Robinson A., Farrar G., and Wiblin C. (Eds), Humana Press Inc., Totowaf
    • Francis M.J. Synthetic peptides. In: Robinson A., Farrar G., and Wiblin C. (Eds). Methods in Molecular Medicine: Vaccine Protocols (1996), Humana Press Inc., Totowaf 75-90
    • (1996) Methods in Molecular Medicine: Vaccine Protocols , pp. 75-90
    • Francis, M.J.1
  • 15
    • 0346742537 scopus 로고    scopus 로고
    • Different approaches to potentiate the immune response induced by a 12-mer synthetic peptide
    • Haro I., and Gomara M.J. Different approaches to potentiate the immune response induced by a 12-mer synthetic peptide. Curr. Protein Pept. Sci. 1 (2000) 125-137
    • (2000) Curr. Protein Pept. Sci. , vol.1 , pp. 125-137
    • Haro, I.1    Gomara, M.J.2
  • 16
    • 9244230030 scopus 로고    scopus 로고
    • Design of synthetic peptide constructs for the vaccine development against viral infections
    • Haro I., and Gomara M.J. Design of synthetic peptide constructs for the vaccine development against viral infections. Curr. Protein Pept. Sci. 5 (2004) 425-433
    • (2004) Curr. Protein Pept. Sci. , vol.5 , pp. 425-433
    • Haro, I.1    Gomara, M.J.2
  • 17
    • 0004853015 scopus 로고
    • Use of T cell epitopes in raising immune responses
    • Zegers N.D., Boersma W.J.A., and Claassen E. (Eds), CRC Press, Inc., New York
    • Zegers N.D., and Boersma W.J.M. Use of T cell epitopes in raising immune responses. In: Zegers N.D., Boersma W.J.A., and Claassen E. (Eds). Immunological Recognition of Peptides in Medicine and Biology (1995), CRC Press, Inc., New York 105-123
    • (1995) Immunological Recognition of Peptides in Medicine and Biology , pp. 105-123
    • Zegers, N.D.1    Boersma, W.J.M.2
  • 18
  • 20
    • 0027605718 scopus 로고
    • Peptide vaccines incorporating a 'promiscuous' T-cell epitope bypass certain haplotype restricted immune responses and provide broad spectrum immunogenicity
    • Kaumaya P.T.P., Kobs-Conrad S., Seo Y.H., Lee H., VanBuiskirk A.M., Feng N., Sheridan J.F., and Stevens V. Peptide vaccines incorporating a 'promiscuous' T-cell epitope bypass certain haplotype restricted immune responses and provide broad spectrum immunogenicity. J. Mol. Recognit. 6 (1993) 81-94
    • (1993) J. Mol. Recognit. , vol.6 , pp. 81-94
    • Kaumaya, P.T.P.1    Kobs-Conrad, S.2    Seo, Y.H.3    Lee, H.4    VanBuiskirk, A.M.5    Feng, N.6    Sheridan, J.F.7    Stevens, V.8
  • 23
    • 0031255317 scopus 로고    scopus 로고
    • Induction of protective CTL responses against the Plasmodium yoelii circumsporozoite protein by immunization with peptides
    • Franke E.D., Corradin G., and Hoffman S.L. Induction of protective CTL responses against the Plasmodium yoelii circumsporozoite protein by immunization with peptides. J. Immunol. 159 (1997) 3424-3433
    • (1997) J. Immunol. , vol.159 , pp. 3424-3433
    • Franke, E.D.1    Corradin, G.2    Hoffman, S.L.3
  • 24
    • 0039493080 scopus 로고
    • Effects of conformation, amino acid sequence, and carrier coupling on the immunological recognition of peptide and protein antigens
    • Zegers N.D., Boersma W.J.A., and Claassen E. (Eds), CRC Press, Inc., New York
    • Jemmerson R. Effects of conformation, amino acid sequence, and carrier coupling on the immunological recognition of peptide and protein antigens. In: Zegers N.D., Boersma W.J.A., and Claassen E. (Eds). Immunological Recognition of Peptides in Medicine and Biology (1995), CRC Press, Inc., New York 213-225
    • (1995) Immunological Recognition of Peptides in Medicine and Biology , pp. 213-225
    • Jemmerson, R.1
  • 25
    • 0015385368 scopus 로고
    • Nonchromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA
    • Cohen S.N., Chang A.C.Y., and Hsu L. Nonchromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA. Proc. Natl. Acad. Sci. U. S. A. 69 (1972) 2110-2114
    • (1972) Proc. Natl. Acad. Sci. U. S. A. , vol.69 , pp. 2110-2114
    • Cohen, S.N.1    Chang, A.C.Y.2    Hsu, L.3
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227 (1970) 680-695
    • (1970) Nature , vol.227 , pp. 680-695
    • Laemmli, U.K.1
  • 27
    • 0034812331 scopus 로고    scopus 로고
    • Cloning and expression of human rotavirus spike protein, VP8*, in Escherichia coli
    • Kovacs-Nolan J., Sasaki E., Yoo D., and Mine Y. Cloning and expression of human rotavirus spike protein, VP8*, in Escherichia coli. Biochem. Biophys. Res. Commun. 282 (2001) 1183-1188
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 1183-1188
    • Kovacs-Nolan, J.1    Sasaki, E.2    Yoo, D.3    Mine, Y.4
  • 28
    • 0030329981 scopus 로고    scopus 로고
    • SPOT synthesis
    • Morris G.E. (Ed), Humana Press Inc, New Jersey
    • Frank R., and Owerwin H. SPOT synthesis. In: Morris G.E. (Ed). Methods in Molecular Biology vol. 66 (1996), Humana Press Inc, New Jersey 149-169
    • (1996) Methods in Molecular Biology , vol.66 , pp. 149-169
    • Frank, R.1    Owerwin, H.2
  • 29
    • 0025368007 scopus 로고
    • Measurement of rotavirus-neutralizing coproantibody in children by fluorescent focus reduction assay
    • Coulson B.S., and Masendycz P.J. Measurement of rotavirus-neutralizing coproantibody in children by fluorescent focus reduction assay. J. Clin. Microbiol. 28 (1990) 1652-1654
    • (1990) J. Clin. Microbiol. , vol.28 , pp. 1652-1654
    • Coulson, B.S.1    Masendycz, P.J.2
  • 30
    • 0025020393 scopus 로고
    • Neutralizing antibodies to all seven serotypes of foot-and-mouth disease virus elicited by synthetic peptides
    • Francis M.J., Hastings G.Z., Clarke B.E., Brown A.L., Beddel A.L., Rowlands D.J., and Brown F. Neutralizing antibodies to all seven serotypes of foot-and-mouth disease virus elicited by synthetic peptides. Immunology 69 (1990) 171-176
    • (1990) Immunology , vol.69 , pp. 171-176
    • Francis, M.J.1    Hastings, G.Z.2    Clarke, B.E.3    Brown, A.L.4    Beddel, A.L.5    Rowlands, D.J.6    Brown, F.7
  • 31
    • 0026788007 scopus 로고
    • The influence of orientation and number of copies of T and B cell epitopes on the specificity and affinity of antibodies induced by chimeric peptides
    • Partidos C., Stanley C., and Steward M. The influence of orientation and number of copies of T and B cell epitopes on the specificity and affinity of antibodies induced by chimeric peptides. Eur. J. Immunol. 22 (1992) 2675-2680
    • (1992) Eur. J. Immunol. , vol.22 , pp. 2675-2680
    • Partidos, C.1    Stanley, C.2    Steward, M.3
  • 32
    • 0023270889 scopus 로고
    • Engineering of immunogenic peptides by co-linear synthesis of determinants recognized by B and T cells
    • Borras-Cuesta F., Petit-Camurdan A., and Fedon Y. Engineering of immunogenic peptides by co-linear synthesis of determinants recognized by B and T cells. Eur. J. Immunol. 17 (1987) 1213-1215
    • (1987) Eur. J. Immunol. , vol.17 , pp. 1213-1215
    • Borras-Cuesta, F.1    Petit-Camurdan, A.2    Fedon, Y.3
  • 33
    • 0028935464 scopus 로고
    • Immunogenicity of genetically engineered glutathione S-transferase fusion proteins containing a T-cell epitope from diphtheria toxin
    • Pillai S., Dermody K., and Metcalf B. Immunogenicity of genetically engineered glutathione S-transferase fusion proteins containing a T-cell epitope from diphtheria toxin. Infect. Immun. 63 (1995) 1535-1540
    • (1995) Infect. Immun. , vol.63 , pp. 1535-1540
    • Pillai, S.1    Dermody, K.2    Metcalf, B.3
  • 35
    • 0026515267 scopus 로고
    • Universal T helper cell determinants enhance immunogenicity of a Plasmodium falciparum merozoite surface antigen peptide
    • Kumar A., Arora R., Kaur P., Chauhan V.S., and Sharma P. Universal T helper cell determinants enhance immunogenicity of a Plasmodium falciparum merozoite surface antigen peptide. J. Immunol. 148 (1992) 1499-1505
    • (1992) J. Immunol. , vol.148 , pp. 1499-1505
    • Kumar, A.1    Arora, R.2    Kaur, P.3    Chauhan, V.S.4    Sharma, P.5
  • 36
    • 7744222635 scopus 로고    scopus 로고
    • Differential antibody responses to Plasmodium falciparum-derived B-cell epitopes induced by diepitope multiple antigen peptides (MAP) containing different T-cell epitopes
    • Vasconcelos N.-M., Siddique A.B., Ahlborg N., and Berzins K. Differential antibody responses to Plasmodium falciparum-derived B-cell epitopes induced by diepitope multiple antigen peptides (MAP) containing different T-cell epitopes. Vaccine 23 (2004) 343-352
    • (2004) Vaccine , vol.23 , pp. 343-352
    • Vasconcelos, N.-M.1    Siddique, A.B.2    Ahlborg, N.3    Berzins, K.4
  • 37
    • 0033179463 scopus 로고    scopus 로고
    • The immunogenicity of various peptide antigens inducing cross-reacting antibodies to a cell surface protein antigen of Streptococcus mutans
    • Kato H., Takeuchi H., Oishi Y., Senpuku H., Shimura N., Hanada N., and Nisizawa T. The immunogenicity of various peptide antigens inducing cross-reacting antibodies to a cell surface protein antigen of Streptococcus mutans. Oral Microbiol. Immunol. 14 (1999) 213-219
    • (1999) Oral Microbiol. Immunol. , vol.14 , pp. 213-219
    • Kato, H.1    Takeuchi, H.2    Oishi, Y.3    Senpuku, H.4    Shimura, N.5    Hanada, N.6    Nisizawa, T.7
  • 38
    • 0027165462 scopus 로고
    • Influence of epitope polarity and adjuvants on the immunogenicity and efficacy of a synthetic peptide vaccine against Semliki Forest virus
    • Fernández M., Snijders A., Benaissa-Trouw B.J., Harmsen M., Snippe H., and Kraaijeveld C.A. Influence of epitope polarity and adjuvants on the immunogenicity and efficacy of a synthetic peptide vaccine against Semliki Forest virus. J. Virol. 67 (1993) 5843-5848
    • (1993) J. Virol. , vol.67 , pp. 5843-5848
    • Fernández, M.1    Snijders, A.2    Benaissa-Trouw, B.J.3    Harmsen, M.4    Snippe, H.5    Kraaijeveld, C.A.6
  • 39
    • 0041167210 scopus 로고    scopus 로고
    • The specificity of antibodies raised against a T-cell peptide is influenced by peptide amidation
    • Maillère B., and Hervé M. The specificity of antibodies raised against a T-cell peptide is influenced by peptide amidation. Mol. Immunol. 14 (1997) 1003-1009
    • (1997) Mol. Immunol. , vol.14 , pp. 1003-1009
    • Maillère, B.1    Hervé, M.2
  • 40
    • 0026510454 scopus 로고
    • The effect of orientation of epitopes on the immunogenicity of chimeric synthetic peptides representing measles virus protein sequences
    • Partidos C., Stanley C., and Steward M. The effect of orientation of epitopes on the immunogenicity of chimeric synthetic peptides representing measles virus protein sequences. Mol. Immunol. 29 (1992) 651-658
    • (1992) Mol. Immunol. , vol.29 , pp. 651-658
    • Partidos, C.1    Stanley, C.2    Steward, M.3
  • 41
    • 0029954365 scopus 로고    scopus 로고
    • The effect of orientation within a chimeric peptide on the immunogenicity of Chlamydia trachomatis epitopes
    • Peterson E.M., Cheng X., Zhenhai Q., and De La Maza L.M. The effect of orientation within a chimeric peptide on the immunogenicity of Chlamydia trachomatis epitopes. Mol. Immunol. 33 (1996) 335-339
    • (1996) Mol. Immunol. , vol.33 , pp. 335-339
    • Peterson, E.M.1    Cheng, X.2    Zhenhai, Q.3    De La Maza, L.M.4
  • 42
    • 33646049712 scopus 로고    scopus 로고
    • Cytokine responses in gnotobiotic pigs after infection with virulent or attenuated human rotavirus
    • Azevedo M.S.P., Yuan L., Pouly S., Gonzales A.M., Jeong K.I., Nguyen T.V., and Saif L.J. Cytokine responses in gnotobiotic pigs after infection with virulent or attenuated human rotavirus. J. Virol. 80 (2006) 372-382
    • (2006) J. Virol. , vol.80 , pp. 372-382
    • Azevedo, M.S.P.1    Yuan, L.2    Pouly, S.3    Gonzales, A.M.4    Jeong, K.I.5    Nguyen, T.V.6    Saif, L.J.7
  • 43
    • 0023497504 scopus 로고
    • Fusion proteins with multiple copies of the major antigenic determinant and foot-and-mouth disease virus protect both the natural host and laboratory animals
    • Broekhuijsen M.P., Van Rijn J.M.M., Blom A.J.M., Pouwels P.H., Enger-Valk B.E., Brown F., and Francis M.J. Fusion proteins with multiple copies of the major antigenic determinant and foot-and-mouth disease virus protect both the natural host and laboratory animals. J. Gen. Virol. 68 (1987) 3137-3143
    • (1987) J. Gen. Virol. , vol.68 , pp. 3137-3143
    • Broekhuijsen, M.P.1    Van Rijn, J.M.M.2    Blom, A.J.M.3    Pouwels, P.H.4    Enger-Valk, B.E.5    Brown, F.6    Francis, M.J.7
  • 44
    • 0343564256 scopus 로고
    • Circumsporozoite gene of Plasmodium cynomolgi (Gombak): cDNA cloning and expression of the repetitive circumsporoziote epitope
    • Enea V., Arnot D., Schmidt E.C., Cochrane A., Gwadz R., and Nussenzweig R.S. Circumsporozoite gene of Plasmodium cynomolgi (Gombak): cDNA cloning and expression of the repetitive circumsporoziote epitope. Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 7520-7524
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 7520-7524
    • Enea, V.1    Arnot, D.2    Schmidt, E.C.3    Cochrane, A.4    Gwadz, R.5    Nussenzweig, R.S.6
  • 45
    • 13944259389 scopus 로고    scopus 로고
    • Structural and dynamic consequences of increasing repeats in a MUCI peptide tumor antigen
    • Schuman J.T., Grinstead J.S., Apostolopoulos V., and Campbell P.A. Structural and dynamic consequences of increasing repeats in a MUCI peptide tumor antigen. Biopolymers 77 (2005) 107-120
    • (2005) Biopolymers , vol.77 , pp. 107-120
    • Schuman, J.T.1    Grinstead, J.S.2    Apostolopoulos, V.3    Campbell, P.A.4
  • 47
    • 7744239182 scopus 로고    scopus 로고
    • High epitope density in a single recombinant protein molecule of the extracellular domain of influenza A virus M2 protein significantly enhances protective immunity
    • Liu W., Peng Z., Liu Z., Lu Y., Ding J., and Chen Y.-H. High epitope density in a single recombinant protein molecule of the extracellular domain of influenza A virus M2 protein significantly enhances protective immunity. Vaccine 23 (2004) 366-371
    • (2004) Vaccine , vol.23 , pp. 366-371
    • Liu, W.1    Peng, Z.2    Liu, Z.3    Lu, Y.4    Ding, J.5    Chen, Y.-H.6
  • 48
    • 14744290281 scopus 로고    scopus 로고
    • High epitope density in a single protein molecule significantly enhances antigenicity as well as immunogenicity: a novel strategy for modern vaccine development and a preliminary investigation about B cell discrimination of monomeric proteins
    • Liu W., and Chen Y.-H. High epitope density in a single protein molecule significantly enhances antigenicity as well as immunogenicity: a novel strategy for modern vaccine development and a preliminary investigation about B cell discrimination of monomeric proteins. Eur. J. Immunol. 35 (2005) 505-514
    • (2005) Eur. J. Immunol. , vol.35 , pp. 505-514
    • Liu, W.1    Chen, Y.-H.2
  • 49
    • 0026733470 scopus 로고
    • Antibody responses to non-immunogenic synthetic peptides induced by co-immunization with immunogenic peptides
    • Partidos C.D., Obeid O.E., and Steward M.W. Antibody responses to non-immunogenic synthetic peptides induced by co-immunization with immunogenic peptides. Immunology 77 (1992) 262-266
    • (1992) Immunology , vol.77 , pp. 262-266
    • Partidos, C.D.1    Obeid, O.E.2    Steward, M.W.3
  • 50
    • 0027440046 scopus 로고
    • Specificity of antibodies reactive with hepatitis B surface antigen following immunization with synthetic peptides
    • Steward M.W., Partidos C.D., D'Mello F., and Howard C.R. Specificity of antibodies reactive with hepatitis B surface antigen following immunization with synthetic peptides. Vaccine 11 (1993) 1405-1414
    • (1993) Vaccine , vol.11 , pp. 1405-1414
    • Steward, M.W.1    Partidos, C.D.2    D'Mello, F.3    Howard, C.R.4
  • 51
    • 0027452015 scopus 로고
    • Influence of the T-helper epitope on the titre and affinity of antibodies to B-cell epitopes after co-immunization
    • Shaw D.M., Stanley C.M., Partidos C.D., and Steward M.W. Influence of the T-helper epitope on the titre and affinity of antibodies to B-cell epitopes after co-immunization. Mol. Immunol. 30 (1993) 961-968
    • (1993) Mol. Immunol. , vol.30 , pp. 961-968
    • Shaw, D.M.1    Stanley, C.M.2    Partidos, C.D.3    Steward, M.W.4


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