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Volumn 17, Issue 1, 2011, Pages 24-31

Peptide vaccine candidates against classical swine fever virus: T cell and neutralizing antibody responses of dendrimers displaying E2 and NS2-3 epitopes

Author keywords

Classical swine fever; Dendrimeric peptides; PEG like flexibilizing units; Peptide vaccines

Indexed keywords

DENDRIMER; EPITOPE; NEUTRALIZING ANTIBODY; PEPTIDE VACCINE; SWINE FEVER VIRUS VACCINE; UNCLASSIFIED DRUG;

EID: 78650253836     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1292     Document Type: Article
Times cited : (31)

References (55)
  • 1
    • 0001331728 scopus 로고
    • Synthetic peptide vaccine design: synthesis and properties of a high-density multiple antigenic peptide system
    • Tam JP. Synthetic peptide vaccine design: synthesis and properties of a high-density multiple antigenic peptide system. Proc. Natl. Acad. Sci. USA 1988; 85: 5409-5413.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5409-5413
    • Tam, J.P.1
  • 3
    • 33745524890 scopus 로고    scopus 로고
    • Influence of sequential oligopeptide carriers on the bioactive structure of conjugated epitopes: comparative study of the conformation of a herpes simplex virus glycoprotein gD-1 epitope in the free and conjugated form, and protein "built-in" crystal structure
    • Krikorian D, Stavrakoudis A, Biris N, Sakarellos C, Andreu D, de Oliveira E, Mezö G, Majer Z, Hudecz F, Welling-Wester S, Cung MT, Tsikaris V. Influence of sequential oligopeptide carriers on the bioactive structure of conjugated epitopes: comparative study of the conformation of a herpes simplex virus glycoprotein gD-1 epitope in the free and conjugated form, and protein "built-in" crystal structure. Biopolymers 2006; 84: 383-399.
    • (2006) Biopolymers , vol.84 , pp. 383-399
    • Krikorian, D.1    Stavrakoudis, A.2    Biris, N.3    Sakarellos, C.4    Andreu, D.5    de Oliveira, E.6    Mezö, G.7    Majer, Z.8    Hudecz, F.9    Welling-Wester, S.10    Cung, M.T.11    Tsikaris, V.12
  • 4
    • 0023839711 scopus 로고
    • Enhancement of peptide immunogenicity by linear polymerization
    • Borrás-Cuesta F, Fedon Y, Petit-Camurdan A. Enhancement of peptide immunogenicity by linear polymerization. Eur. J. Immunol. 1988; 18: 199-202.
    • (1988) Eur. J. Immunol. , vol.18 , pp. 199-202
    • Borrás-Cuesta, F.1    Fedon, Y.2    Petit-Camurdan, A.3
  • 5
    • 0030070347 scopus 로고    scopus 로고
    • Concept and design of a new class of sequential oligopeptide carriers (SOC) for covalent attachment of multiple antigenic peptides
    • Tsikaris V, Sakarellos C, Cung MT, Marraud M, Sakarellos-Daitsiotis M. Concept and design of a new class of sequential oligopeptide carriers (SOC) for covalent attachment of multiple antigenic peptides. Biopolymers 1996; 38: 291-293.
    • (1996) Biopolymers , vol.38 , pp. 291-293
    • Tsikaris, V.1    Sakarellos, C.2    Cung, M.T.3    Marraud, M.4    Sakarellos-Daitsiotis, M.5
  • 6
    • 0035804439 scopus 로고    scopus 로고
    • Orthogonal solid-phase synthesis of tetramannosylated peptide constructs carrying three independent branched epitopes
    • Kragol G, Otvos L. Orthogonal solid-phase synthesis of tetramannosylated peptide constructs carrying three independent branched epitopes. Tetrahedron 2001; 57: 957-966.
    • (2001) Tetrahedron , vol.57 , pp. 957-966
    • Kragol, G.1    Otvos, L.2
  • 7
    • 0038402706 scopus 로고    scopus 로고
    • Induction of influenza type A virus-specific resistance by immunization of mice with a synthetic multiple antigenic peptide vaccine that contains ectodomains of matrix protein 2
    • Mozdzanowska K, Feng J, Eid M, Kragol G, Cudic M, Otvos L, Gerhard W. Induction of influenza type A virus-specific resistance by immunization of mice with a synthetic multiple antigenic peptide vaccine that contains ectodomains of matrix protein 2. Vaccine 2003; 21: 2616-2626.
    • (2003) Vaccine , vol.21 , pp. 2616-2626
    • Mozdzanowska, K.1    Feng, J.2    Eid, M.3    Kragol, G.4    Cudic, M.5    Otvos, L.6    Gerhard, W.7
  • 8
    • 0029833251 scopus 로고    scopus 로고
    • Recent advances in multiple antigen peptides
    • Tam JP. Recent advances in multiple antigen peptides. J. Immunol. Methods 1996; 196: 17-32.
    • (1996) J. Immunol. Methods , vol.196 , pp. 17-32
    • Tam, J.P.1
  • 10
    • 0036183822 scopus 로고    scopus 로고
    • Antimicrobial dendrimeric peptides
    • Tam JP, Lu YA, Yang JL. Antimicrobial dendrimeric peptides. Eur. J. Biochem. 2002; 269: 923-932.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 923-932
    • Tam, J.P.1    Lu, Y.A.2    Yang, J.L.3
  • 13
    • 47049094820 scopus 로고    scopus 로고
    • Enhanced mucosal immunoglobulin A response and solid protection against foot-and-mouth disease virus challenge induced by a novel dendrimeric peptide
    • Cubillos C, de la Torre BG, Jakab A, Clementi G, Borràs E, Bárcena J, Andreu D, Sobrino F, Blanco E. Enhanced mucosal immunoglobulin A response and solid protection against foot-and-mouth disease virus challenge induced by a novel dendrimeric peptide. J. Virol. 2008; 82: 7223-7230.
    • (2008) J. Virol. , vol.82 , pp. 7223-7230
    • Cubillos, C.1    de la Torre, B.G.2    Jakab, A.3    Clementi, G.4    Borràs, E.5    Bárcena, J.6    Andreu, D.7    Sobrino, F.8    Blanco, E.9
  • 14
    • 33845288971 scopus 로고    scopus 로고
    • Marker vaccine strategies and candidate CSFV marker vaccines
    • Dong XN, Chen YH. Marker vaccine strategies and candidate CSFV marker vaccines. Vaccine 2007; 25: 205-230.
    • (2007) Vaccine , vol.25 , pp. 205-230
    • Dong, X.N.1    Chen, Y.H.2
  • 15
    • 18844379112 scopus 로고    scopus 로고
    • A DNA vaccine expressing the E2 protein of classical swine fever virus elicits T cell responses that can prime for rapid antibody production and confer total protection upon viral challenge
    • Ganges L, Barrera M, Núñez JI, Blanco I, Frías MT, Rodríguez F, Sobrino F. A DNA vaccine expressing the E2 protein of classical swine fever virus elicits T cell responses that can prime for rapid antibody production and confer total protection upon viral challenge. Vaccine 2005; 23: 3741-3752.
    • (2005) Vaccine , vol.23 , pp. 3741-3752
    • Ganges, L.1    Barrera, M.2    Núñez, J.I.3    Blanco, I.4    Frías, M.T.5    Rodríguez, F.6    Sobrino, F.7
  • 16
    • 0027456327 scopus 로고
    • Cellular immune response to hog cholera virus (HCV): T cells of immune pigs proliferate in vitro upon stimulation with live HCV, but the E1 envelope glycoprotein is not a major T-cell antigen
    • Kimman TG, Bianchi AT, Wensvoort G, de Bruin TG, Meliefste C. Cellular immune response to hog cholera virus (HCV): T cells of immune pigs proliferate in vitro upon stimulation with live HCV, but the E1 envelope glycoprotein is not a major T-cell antigen. J. Virol. 1993; 67: 2922-2927.
    • (1993) J. Virol. , vol.67 , pp. 2922-2927
    • Kimman, T.G.1    Bianchi, A.T.2    Wensvoort, G.3    de Bruin, T.G.4    Meliefste, C.5
  • 17
    • 2642645434 scopus 로고    scopus 로고
    • Lymphocyte apoptosis during classical swine fever: implication of activation-induced cell death
    • Summerfield A, Knötig SM, McCullough KC. Lymphocyte apoptosis during classical swine fever: implication of activation-induced cell death. J. Virol. 1998; 72: 1853-1861.
    • (1998) J. Virol. , vol.72 , pp. 1853-1861
    • Summerfield, A.1    Knötig, S.M.2    McCullough, K.C.3
  • 18
    • 0034691175 scopus 로고    scopus 로고
    • Pathogenesis of granulocytopenia and bone marrow atrophy during classical swine fever involves apoptosis and necrosis of uninfected cells
    • Summerfield A, Knoetig SM, Tschudin R, McCullough KC. Pathogenesis of granulocytopenia and bone marrow atrophy during classical swine fever involves apoptosis and necrosis of uninfected cells. Virology 2000; 272: 50-60.
    • (2000) Virology , vol.272 , pp. 50-60
    • Summerfield, A.1    Knoetig, S.M.2    Tschudin, R.3    McCullough, K.C.4
  • 19
    • 34447106750 scopus 로고    scopus 로고
    • Novel marker vaccines against classical swine fever
    • Beer M, Reimann I, Hoffmann B, Depner K. Novel marker vaccines against classical swine fever. Vaccine 2007; 25: 5665-5670.
    • (2007) Vaccine , vol.25 , pp. 5665-5670
    • Beer, M.1    Reimann, I.2    Hoffmann, B.3    Depner, K.4
  • 20
    • 0025864175 scopus 로고
    • Live attenuated pseudorabies virus expressing envelope glycoprotein E1 of hog cholera virus protects swine against both pseudorabies and hog cholera
    • van Zijl M, Wensvoort G, de Kluyver E, Hulst M, van der Gulden H, Gielkens A, Berns A, Moormann R. Live attenuated pseudorabies virus expressing envelope glycoprotein E1 of hog cholera virus protects swine against both pseudorabies and hog cholera. J. Virol. 1991; 65: 2761-2765.
    • (1991) J. Virol. , vol.65 , pp. 2761-2765
    • van Zijl, M.1    Wensvoort, G.2    de Kluyver, E.3    Hulst, M.4    van der Gulden, H.5    Gielkens, A.6    Berns, A.7    Moormann, R.8
  • 21
    • 0027204176 scopus 로고
    • Glycoprotein E1 of hog cholera virus expressed in insect cells protects swine from hog cholera
    • Hulst MM, Westra DF, Wensvoort G, Moormann RJ. Glycoprotein E1 of hog cholera virus expressed in insect cells protects swine from hog cholera. J. Virol. 1993; 67: 5435-5442.
    • (1993) J. Virol. , vol.67 , pp. 5435-5442
    • Hulst, M.M.1    Westra, D.F.2    Wensvoort, G.3    Moormann, R.J.4
  • 22
    • 0029134624 scopus 로고
    • Classical swine fever virus: independent induction of protective immunity by two structural glycoproteins
    • König M, Lengsfeld T, Pauly T, Stark R, Thiel HJ. Classical swine fever virus: independent induction of protective immunity by two structural glycoproteins. J. Virol. 1995; 69: 6479-6486.
    • (1995) J. Virol. , vol.69 , pp. 6479-6486
    • König, M.1    Lengsfeld, T.2    Pauly, T.3    Stark, R.4    Thiel, H.J.5
  • 24
    • 0031034962 scopus 로고    scopus 로고
    • Immune response to vaccination with DNA encoding the bovine viral diarrhea virus major glycoprotein gp53 (E2)
    • Harpin S, Talbot B, Mbikay M, Elazhary Y. Immune response to vaccination with DNA encoding the bovine viral diarrhea virus major glycoprotein gp53 (E2). FEMS Microbiol. Lett. 1997; 146: 229-234.
    • (1997) FEMS Microbiol. Lett. , vol.146 , pp. 229-234
    • Harpin, S.1    Talbot, B.2    Mbikay, M.3    Elazhary, Y.4
  • 25
    • 0035825085 scopus 로고    scopus 로고
    • DNA-mediated protection against classical swine fever virus
    • Yu X, Tu C, Li H, Hu R, Chen C, Li Z, Zhang M, Yin Z. DNA-mediated protection against classical swine fever virus. Vaccine 2001; 19: 1520-1525.
    • (2001) Vaccine , vol.19 , pp. 1520-1525
    • Yu, X.1    Tu, C.2    Li, H.3    Hu, R.4    Chen, C.5    Li, Z.6    Zhang, M.7    Yin, Z.8
  • 26
    • 0037449113 scopus 로고    scopus 로고
    • DNA vaccination against bovine viral diarrhoea virus induces humoral and cellular responses in cattle with evidence for protection against viral challenge
    • Nobiron I, Thompson I, Brownlie J, Collins ME. DNA vaccination against bovine viral diarrhoea virus induces humoral and cellular responses in cattle with evidence for protection against viral challenge. Vaccine 2003; 21: 2082-2092.
    • (2003) Vaccine , vol.21 , pp. 2082-2092
    • Nobiron, I.1    Thompson, I.2    Brownlie, J.3    Collins, M.E.4
  • 27
    • 26644470073 scopus 로고    scopus 로고
    • Immunization with plasmid DNA encoding a truncated, secreted form of the bovine viral diarrhea virus E2 protein elicits strong humoral and cellular immune responses
    • Liang R, van den Hurk JV, Zheng C, Yu H, Pontarollo RA, Babiuk LA, van Drunen Littel-van den Hurk S. Immunization with plasmid DNA encoding a truncated, secreted form of the bovine viral diarrhea virus E2 protein elicits strong humoral and cellular immune responses. Vaccine 2005; 23: 5252-5262.
    • (2005) Vaccine , vol.23 , pp. 5252-5262
    • Liang, R.1    van den Hurk, J.V.2    Zheng, C.3    Yu, H.4    Pontarollo, R.A.5    Babiuk, L.A.6    van Drunen Littel-van den Hurk, S.7
  • 28
    • 21844467997 scopus 로고    scopus 로고
    • Immunomodulatory effect of plasmids co-expressing cytokines in classical swine fever virus subunit gp55/E2-DNA vaccination
    • Wienhold D, Armengol E, Marquardt A, Marquardt C, Voigt H, Büttner M, Saalmüller A, Pfaff E. Immunomodulatory effect of plasmids co-expressing cytokines in classical swine fever virus subunit gp55/E2-DNA vaccination. Vet. Res. 2005; 36: 571-587.
    • (2005) Vet. Res. , vol.36 , pp. 571-587
    • Wienhold, D.1    Armengol, E.2    Marquardt, A.3    Marquardt, C.4    Voigt, H.5    Büttner, M.6    Saalmüller, A.7    Pfaff, E.8
  • 30
    • 0030041655 scopus 로고    scopus 로고
    • Comparison of the protective efficacy of recombinant pseudorabies viruses against pseudorabies and classical swine fever in pigs; influence of different promoters on gene expression and on protection
    • Hooft van Iddekinge BJ, de Wind N, Wensvoort G, Kimman TG, Gielkens AL, Moormann RJ. Comparison of the protective efficacy of recombinant pseudorabies viruses against pseudorabies and classical swine fever in pigs; influence of different promoters on gene expression and on protection. Vaccine 1996; 14: 6-12.
    • (1996) Vaccine , vol.14 , pp. 6-12
    • Hooft van Iddekinge, B.J.1    de Wind, N.2    Wensvoort, G.3    Kimman, T.G.4    Gielkens, A.L.5    Moormann, R.J.6
  • 31
    • 0028040003 scopus 로고
    • Virulence and pathogenesis of nonvirulent and virulent strains of pseudorabies virus expressing envelope glycoprotein E1 of hog cholera virus
    • Mulder WA, Priem J, Glazenburg KL, Wagenaar F, Gruys E, Gielkens AL, Pol JM, Kimman TG. Virulence and pathogenesis of nonvirulent and virulent strains of pseudorabies virus expressing envelope glycoprotein E1 of hog cholera virus. J. Gen. Virol. 1994; 75: 117-124.
    • (1994) J. Gen. Virol. , vol.75 , pp. 117-124
    • Mulder, W.A.1    Priem, J.2    Glazenburg, K.L.3    Wagenaar, F.4    Gruys, E.5    Gielkens, A.L.6    Pol, J.M.7    Kimman, T.G.8
  • 32
    • 0030784878 scopus 로고    scopus 로고
    • Biologically safe, nontransmissible pseudorabies virus vector vaccine protects pigs against both Aujeszky's disease and classical swine fever
    • Peeters B, Bienkowska-Szewczyk K, Hulst M, Gielkens A, Kimman T. Biologically safe, nontransmissible pseudorabies virus vector vaccine protects pigs against both Aujeszky's disease and classical swine fever. J. Gen. Virol. 1997; 78: 3311-3315.
    • (1997) J. Gen. Virol. , vol.78 , pp. 3311-3315
    • Peeters, B.1    Bienkowska-Szewczyk, K.2    Hulst, M.3    Gielkens, A.4    Kimman, T.5
  • 33
    • 0033990732 scopus 로고    scopus 로고
    • Vaccination with a single dose of a recombinant porcine adenovirus expressing the classical swine fever virus gp55 (E2) gene protects pigs against classical swine fever
    • Hammond JM, McCoy RJ, Jansen ES, Morrissy CJ, Hodgson AL, Johnson MA. Vaccination with a single dose of a recombinant porcine adenovirus expressing the classical swine fever virus gp55 (E2) gene protects pigs against classical swine fever. Vaccine 2000; 18: 1040-1050.
    • (2000) Vaccine , vol.18 , pp. 1040-1050
    • Hammond, J.M.1    McCoy, R.J.2    Jansen, E.S.3    Morrissy, C.J.4    Hodgson, A.L.5    Johnson, M.A.6
  • 34
    • 0034668183 scopus 로고    scopus 로고
    • Chimeric classical swine fever viruses containing envelope protein E(RNS) or E2 of bovine viral diarrhoea virus protect pigs against challenge with CSFV and induce a distinguishable antibody response
    • van Gennip HG, van Rijn PA, Widjojoatmodjo MN, de Smit AJ, Moormann RJ. Chimeric classical swine fever viruses containing envelope protein E(RNS) or E2 of bovine viral diarrhoea virus protect pigs against challenge with CSFV and induce a distinguishable antibody response. Vaccine 2000; 19: 447-459.
    • (2000) Vaccine , vol.19 , pp. 447-459
    • van Gennip, H.G.1    van Rijn, P.A.2    Widjojoatmodjo, M.N.3    de Smit, A.J.4    Moormann, R.J.5
  • 35
    • 0035952188 scopus 로고    scopus 로고
    • Duration of the protection of an E2 subunit marker vaccine against classical swine fever after a single vaccination
    • de Smit AJ, Bouma A, de Kluijver EP, Terpstra C, Moormann RJ. Duration of the protection of an E2 subunit marker vaccine against classical swine fever after a single vaccination. Vet. Microbiol. 2001; 78: 307-317.
    • (2001) Vet. Microbiol. , vol.78 , pp. 307-317
    • de Smit, A.J.1    Bouma, A.2    de Kluijver, E.P.3    Terpstra, C.4    Moormann, R.J.5
  • 36
    • 1942517974 scopus 로고    scopus 로고
    • An avirulent chimeric Pestivirus with altered cell tropism protects pigs against lethal infection with classical swine fever virus
    • Reimann I, Depner K, Trapp S, Beer M. An avirulent chimeric Pestivirus with altered cell tropism protects pigs against lethal infection with classical swine fever virus. Virology 2004; 322: 143-157.
    • (2004) Virology , vol.322 , pp. 143-157
    • Reimann, I.1    Depner, K.2    Trapp, S.3    Beer, M.4
  • 37
    • 18944385094 scopus 로고    scopus 로고
    • Candidate multi-peptide-vaccine against classical swine fever virus induced potent immunity with serological marker
    • Dong XN, Chen Y, Wu Y, Chen YH. Candidate multi-peptide-vaccine against classical swine fever virus induced potent immunity with serological marker. Vaccine 2005; 23: 3630-3633.
    • (2005) Vaccine , vol.23 , pp. 3630-3633
    • Dong, X.N.1    Chen, Y.2    Wu, Y.3    Chen, Y.H.4
  • 38
    • 32544458624 scopus 로고    scopus 로고
    • Candidate peptide-vaccines induced immunity against CSFV and identified sequential neutralizing determinants in antigenic domain A of glycoprotein E2
    • Dong XN, Chen YH. Candidate peptide-vaccines induced immunity against CSFV and identified sequential neutralizing determinants in antigenic domain A of glycoprotein E2. Vaccine 2006; 24: 1906-1913.
    • (2006) Vaccine , vol.24 , pp. 1906-1913
    • Dong, X.N.1    Chen, Y.H.2
  • 39
    • 33646474126 scopus 로고    scopus 로고
    • Spying the neutralizing epitopes on E2 N-terminal by candidate epitope-vaccines against classical swine fever virus
    • Dong XN, Chen YH. Spying the neutralizing epitopes on E2 N-terminal by candidate epitope-vaccines against classical swine fever virus. Vaccine 2006; 24: 4029-4034.
    • (2006) Vaccine , vol.24 , pp. 4029-4034
    • Dong, X.N.1    Chen, Y.H.2
  • 40
    • 29244472441 scopus 로고    scopus 로고
    • Candidate peptide-vaccine induced potent protection against CSFV and identified a principal sequential neutralizing determinant on E2
    • Dong XN, Qi Y, Ying J, Chen X, Chen YH. Candidate peptide-vaccine induced potent protection against CSFV and identified a principal sequential neutralizing determinant on E2. Vaccine 2006; 24: 426-434.
    • (2006) Vaccine , vol.24 , pp. 426-434
    • Dong, X.N.1    Qi, Y.2    Ying, J.3    Chen, X.4    Chen, Y.H.5
  • 41
    • 0037073596 scopus 로고    scopus 로고
    • Candidate peptide vaccine induced protection against classical swine fever virus
    • Dong XN, Wei K, Liu ZQ, Chen YH. Candidate peptide vaccine induced protection against classical swine fever virus. Vaccine 2002; 21: 167-173.
    • (2002) Vaccine , vol.21 , pp. 167-173
    • Dong, X.N.1    Wei, K.2    Liu, Z.Q.3    Chen, Y.H.4
  • 42
    • 33746720154 scopus 로고    scopus 로고
    • The protective immune response induced by B cell epitope of classical swine fever virus glycoprotein E2
    • Liu S, Tu C, Wang C, Yu X, Wu J, Guo S, Shao M, Gong Q, Zhu Q, Kong X. The protective immune response induced by B cell epitope of classical swine fever virus glycoprotein E2. J. Virol. Methods 2006; 134: 125-129.
    • (2006) J. Virol. Methods , vol.134 , pp. 125-129
    • Liu, S.1    Tu, C.2    Wang, C.3    Yu, X.4    Wu, J.5    Guo, S.6    Shao, M.7    Gong, Q.8    Zhu, Q.9    Kong, X.10
  • 43
    • 0034469130 scopus 로고    scopus 로고
    • Deletions of structural glycoprotein E2 of classical swine fever virus strain alfort/187 resolve a linear epitope of monoclonal antibody WH303 and the minimal N-terminal domain essential for binding immunoglobulin G antibodies of a pig hyperimmune serum
    • Lin M, Lin F, Mallory M, Clavijo A. Deletions of structural glycoprotein E2 of classical swine fever virus strain alfort/187 resolve a linear epitope of monoclonal antibody WH303 and the minimal N-terminal domain essential for binding immunoglobulin G antibodies of a pig hyperimmune serum. J. Virol. 2000; 74: 11619-11625.
    • (2000) J. Virol. , vol.74 , pp. 11619-11625
    • Lin, M.1    Lin, F.2    Mallory, M.3    Clavijo, A.4
  • 45
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • Fields GB, Noble RL. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pept. Protein Res. 1990; 35: 161-214.
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 46
    • 0021280136 scopus 로고
    • The neutralizing peroxidase-linked assay for detection of antibody against swine fever virus
    • Terpstra C, Bloemraad M, Gielkens AL. The neutralizing peroxidase-linked assay for detection of antibody against swine fever virus. Vet. Microbiol. 1984; 9: 113-120.
    • (1984) Vet. Microbiol. , vol.9 , pp. 113-120
    • Terpstra, C.1    Bloemraad, M.2    Gielkens, A.L.3
  • 48
    • 0025830862 scopus 로고
    • Antigen processing by endosomal proteases determines which sites of sperm-whale myoglobin are eventually recognized by T cells
    • Van Noort JM, Boon J, Van der Drift AC, Wagenaar JP, Boots AM, Boog CJ. Antigen processing by endosomal proteases determines which sites of sperm-whale myoglobin are eventually recognized by T cells. Eur. J. Immunol. 1991; 21: 1989-1996.
    • (1991) Eur. J. Immunol. , vol.21 , pp. 1989-1996
    • Van Noort, J.M.1    Boon, J.2    Van der Drift, A.C.3    Wagenaar, J.P.4    Boots, A.M.5    Boog, C.J.6
  • 49
    • 74949110556 scopus 로고    scopus 로고
    • Strategies and limitations in dendrimeric immunogen synthesis. The influenza virus M2e epitope as a case study
    • Kowalczyk W, de la Torre BG, Andreu D. Strategies and limitations in dendrimeric immunogen synthesis. The influenza virus M2e epitope as a case study. Bioconjug. Chem. 2010; 21: 102-110.
    • (2010) Bioconjug. Chem. , vol.21 , pp. 102-110
    • Kowalczyk, W.1    de la Torre, B.G.2    Andreu, D.3
  • 50
    • 33746776797 scopus 로고    scopus 로고
    • Enzyme-targeted fluorescent imaging probes on a multiple antigenic peptide core
    • Galande AK, Hilderbrand SA, Weissleder R, Tung CH. Enzyme-targeted fluorescent imaging probes on a multiple antigenic peptide core. J. Med. Chem. 2006; 49: 4715-4720.
    • (2006) J. Med. Chem. , vol.49 , pp. 4715-4720
    • Galande, A.K.1    Hilderbrand, S.A.2    Weissleder, R.3    Tung, C.H.4
  • 51
    • 34249986855 scopus 로고    scopus 로고
    • Polyethyleneglycol-based resins as solid supports for the synthesis of difficult or long peptides
    • De la Torre B, Jakab A, Andreu D. Polyethyleneglycol-based resins as solid supports for the synthesis of difficult or long peptides. Int. J. Pept. Res. Ther. 2007; 13: 265-270.
    • (2007) Int. J. Pept. Res. Ther. , vol.13 , pp. 265-270
    • De la Torre, B.1    Jakab, A.2    Andreu, D.3
  • 53
    • 0023959898 scopus 로고
    • The protective value of vaccine-induced neutralising antibody titres in swine fever
    • Terpstra C, Wensvoort G. The protective value of vaccine-induced neutralising antibody titres in swine fever. Vet. Microbiol. 1988; 16: 123-128.
    • (1988) Vet. Microbiol. , vol.16 , pp. 123-128
    • Terpstra, C.1    Wensvoort, G.2
  • 54
    • 0029800973 scopus 로고    scopus 로고
    • Classical swine fever virus (CSFV) envelope glycoprotein E2 containing one structural antigenic unit protects pigs from lethal CSFV Challenger
    • Van Rijn PA, Bossers A, Wensvoort G, Moormann RJ. Classical swine fever virus (CSFV) envelope glycoprotein E2 containing one structural antigenic unit protects pigs from lethal CSFV Challenger. J. Gen. Virol. 1996; 77: 2737-2745.
    • (1996) J. Gen. Virol. , vol.77 , pp. 2737-2745
    • Van Rijn, P.A.1    Bossers, A.2    Wensvoort, G.3    Moormann, R.J.4
  • 55
    • 0033058772 scopus 로고    scopus 로고
    • Efficacy and stability of a subunit vaccine based on glycoprotein E2 of classical swine fever virus
    • Bouma A, de Smit AJ, de Kluijver EP, Terpstra C, Moormann RJ. Efficacy and stability of a subunit vaccine based on glycoprotein E2 of classical swine fever virus. Vet. Microbiol. 1999; 66: 101-114.
    • (1999) Vet. Microbiol. , vol.66 , pp. 101-114
    • Bouma, A.1    de Smit, A.J.2    de Kluijver, E.P.3    Terpstra, C.4    Moormann, R.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.