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Volumn 25, Issue 23, 2007, Pages 4611-4622

A rAb screening method for improving the probability of identifying peptide mimotopes of carbohydrate antigens

Author keywords

Carbohydrate antigens; High throughput; Peptide mimotopes; Recombinant antibodies libraries

Indexed keywords

CARBOHYDRATE ANTIGEN; PEPTIDE DERIVATIVE; POLYSACCHARIDE; PROTEIN MIMOTOPE; RECOMBINANT ANTIBODY; UNCLASSIFIED DRUG;

EID: 34248395603     PISSN: 0264410X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vaccine.2007.03.037     Document Type: Article
Times cited : (11)

References (57)
  • 1
    • 0036301031 scopus 로고    scopus 로고
    • Selection of large diversities of antiidiotypic antibody fragments by phage display
    • Goletz S., Christensen A., Kristensen P., Blohm D., Tomlinson I., Winter G., et al. Selection of large diversities of antiidiotypic antibody fragments by phage display. J Mol Biol 315 5 (2002) 1087-1097
    • (2002) J Mol Biol , vol.315 , Issue.5 , pp. 1087-1097
    • Goletz, S.1    Christensen, A.2    Kristensen, P.3    Blohm, D.4    Tomlinson, I.5    Winter, G.6
  • 2
    • 0042335951 scopus 로고    scopus 로고
    • Glycoconjugate vaccines to prevent group B streptococcal infections
    • Paoletti L.C., and Kasper D.L. Glycoconjugate vaccines to prevent group B streptococcal infections. Expert Opin Biol Ther 3 6 (2003) 975-984
    • (2003) Expert Opin Biol Ther , vol.3 , Issue.6 , pp. 975-984
    • Paoletti, L.C.1    Kasper, D.L.2
  • 3
    • 2942528885 scopus 로고    scopus 로고
    • Development of experimental carbohydrate-conjugate vaccines composed of Streptococcus pneumoniae capsular polysaccharides and the universal helper T-lymphocyte epitope (PADRE)
    • Alexander J., del Guercio M.F., Frame B., Maewal A., Sette A., Nahm M.H., et al. Development of experimental carbohydrate-conjugate vaccines composed of Streptococcus pneumoniae capsular polysaccharides and the universal helper T-lymphocyte epitope (PADRE). Vaccine 22 19 (2004) 2362-2367
    • (2004) Vaccine , vol.22 , Issue.19 , pp. 2362-2367
    • Alexander, J.1    del Guercio, M.F.2    Frame, B.3    Maewal, A.4    Sette, A.5    Nahm, M.H.6
  • 4
    • 0035449899 scopus 로고    scopus 로고
    • Polysaccharides, mimotopes and vaccines for fungal and encapsulated pathogens
    • Pirofski L.A. Polysaccharides, mimotopes and vaccines for fungal and encapsulated pathogens. Trends Microbiol 9 9 (2001) 445-455
    • (2001) Trends Microbiol , vol.9 , Issue.9 , pp. 445-455
    • Pirofski, L.A.1
  • 5
    • 0036568536 scopus 로고    scopus 로고
    • Peptide mimotopes as surrogate antigens of carbohydrates in vaccine discovery
    • Monzavi-Karbassi B., Cunto-Amesty G., Luo P., and Kieber-Emmons T. Peptide mimotopes as surrogate antigens of carbohydrates in vaccine discovery. Trends Biotechnol 20 5 (2002) 207-214
    • (2002) Trends Biotechnol , vol.20 , Issue.5 , pp. 207-214
    • Monzavi-Karbassi, B.1    Cunto-Amesty, G.2    Luo, P.3    Kieber-Emmons, T.4
  • 6
    • 11144302532 scopus 로고    scopus 로고
    • A peptide mimotope of type 8 pneumococcal capsular polysaccharide induces a protective immune response in mice
    • Buchwald U.K., Lees A., Steinitz M., and Pirofski L.A. A peptide mimotope of type 8 pneumococcal capsular polysaccharide induces a protective immune response in mice. Infect Immun 73 1 (2005) 325-333
    • (2005) Infect Immun , vol.73 , Issue.1 , pp. 325-333
    • Buchwald, U.K.1    Lees, A.2    Steinitz, M.3    Pirofski, L.A.4
  • 7
    • 10344232463 scopus 로고    scopus 로고
    • Isolation and structural analysis of peptide mimotopes for the disialoganglioside GD2, a neuroblastoma tumor antigen
    • Förster-Waldl E., Riemer A.B., Dehof A.K., Neumann D., Brämswig K., Boltz-Nitulescu G., et al. Isolation and structural analysis of peptide mimotopes for the disialoganglioside GD2, a neuroblastoma tumor antigen. Mol Immunol 42 3 (2005) 319-325
    • (2005) Mol Immunol , vol.42 , Issue.3 , pp. 319-325
    • Förster-Waldl, E.1    Riemer, A.B.2    Dehof, A.K.3    Neumann, D.4    Brämswig, K.5    Boltz-Nitulescu, G.6
  • 8
    • 4644267073 scopus 로고    scopus 로고
    • Peptide mimotopes of Neisseria meningitidis group B capsular polysaccharide
    • Park I., Choi I.H., Kim S.J., and Shin J.S. Peptide mimotopes of Neisseria meningitidis group B capsular polysaccharide. Yonsei Med J 45 4 (2004) 755-758
    • (2004) Yonsei Med J , vol.45 , Issue.4 , pp. 755-758
    • Park, I.1    Choi, I.H.2    Kim, S.J.3    Shin, J.S.4
  • 9
    • 0347511923 scopus 로고    scopus 로고
    • Immunogenicity and efficacy of Cryptococcus neoformans capsular polysaccharide glucuronoxylomannan peptide mimotope-protein conjugates in human immunoglobulin transgenic mice
    • Maitta R.W., Datta K., Lees A., Belouski S.S., and Pirofski L.A. Immunogenicity and efficacy of Cryptococcus neoformans capsular polysaccharide glucuronoxylomannan peptide mimotope-protein conjugates in human immunoglobulin transgenic mice. Infect Immun 72 1 (2004) 196-208
    • (2004) Infect Immun , vol.72 , Issue.1 , pp. 196-208
    • Maitta, R.W.1    Datta, K.2    Lees, A.3    Belouski, S.S.4    Pirofski, L.A.5
  • 10
    • 16544392222 scopus 로고    scopus 로고
    • Production and characterization of peptide mimotopes of phenolic glycolipid-I of Mycobacterium leprae
    • Youn J.H., Myung H.J., Liav A., Chatterjee D., Brennan P.J., Choi I.H., et al. Production and characterization of peptide mimotopes of phenolic glycolipid-I of Mycobacterium leprae. FEMS Immunol Med Microbiol 41 1 (2004) 51-57
    • (2004) FEMS Immunol Med Microbiol , vol.41 , Issue.1 , pp. 51-57
    • Youn, J.H.1    Myung, H.J.2    Liav, A.3    Chatterjee, D.4    Brennan, P.J.5    Choi, I.H.6
  • 11
    • 0032529204 scopus 로고    scopus 로고
    • Aspects of antigen mimicry revealed by immunization with a peptide mimetic of Cryptococcus neoformans polysaccharide
    • Valadon P., Nussbaum G., Oh J., and Scharff M. Aspects of antigen mimicry revealed by immunization with a peptide mimetic of Cryptococcus neoformans polysaccharide. J Immuol 161 4 (1998) 1829-1836
    • (1998) J Immuol , vol.161 , Issue.4 , pp. 1829-1836
    • Valadon, P.1    Nussbaum, G.2    Oh, J.3    Scharff, M.4
  • 12
    • 0032830331 scopus 로고    scopus 로고
    • Crossreactivity of mimotopes and peptide homologues of a sequential epitope with a monoclonal antibody does not predict crossreactive immunogenicity
    • El Kasmi K.C., Deroo S., Theisen D.M., Brons N.H.C., and Muller C.P. Crossreactivity of mimotopes and peptide homologues of a sequential epitope with a monoclonal antibody does not predict crossreactive immunogenicity. Vaccine 18 3-4 (2000) 284-290
    • (2000) Vaccine , vol.18 , Issue.3-4 , pp. 284-290
    • El Kasmi, K.C.1    Deroo, S.2    Theisen, D.M.3    Brons, N.H.C.4    Muller, C.P.5
  • 13
    • 0037114161 scopus 로고    scopus 로고
    • High affinity mimotope of the polysaccharide capsule of Cryptococcus neoformans identified from an evolutionary phage peptide library
    • Beenhower D.O., May R.J., Valadon P., and Scharrf M.D. High affinity mimotope of the polysaccharide capsule of Cryptococcus neoformans identified from an evolutionary phage peptide library. J Immunol 169 12 (2002) 6992-6999
    • (2002) J Immunol , vol.169 , Issue.12 , pp. 6992-6999
    • Beenhower, D.O.1    May, R.J.2    Valadon, P.3    Scharrf, M.D.4
  • 14
    • 18344366726 scopus 로고    scopus 로고
    • Cross-reactivity of mimotopes with a monoclonal antibody against the high molecular weight melanoma-associated antigen (HMW-MAA) does not predict cross-reactive immunogenicity
    • Hafner C., Wagner S., Allwardt D., Riemer A.B., Scheiner O., Pehamberger H., et al. Cross-reactivity of mimotopes with a monoclonal antibody against the high molecular weight melanoma-associated antigen (HMW-MAA) does not predict cross-reactive immunogenicity. Melanoma Res 15 2 (2005) 111-117
    • (2005) Melanoma Res , vol.15 , Issue.2 , pp. 111-117
    • Hafner, C.1    Wagner, S.2    Allwardt, D.3    Riemer, A.B.4    Scheiner, O.5    Pehamberger, H.6
  • 15
    • 0028291823 scopus 로고
    • Isolation of high affinity human antibodys directly from large synthetic repertoires
    • Griffiths A.D., Williams S.C., Hartley O., Tomlinson I.M., Waterhouse P., Crosby W.L., et al. Isolation of high affinity human antibodys directly from large synthetic repertoires. EMBO J 13 14 (1994) 3245-3260
    • (1994) EMBO J , vol.13 , Issue.14 , pp. 3245-3260
    • Griffiths, A.D.1    Williams, S.C.2    Hartley, O.3    Tomlinson, I.M.4    Waterhouse, P.5    Crosby, W.L.6
  • 17
    • 3142743794 scopus 로고    scopus 로고
    • Antibodys from phage antibody libraries
    • Bradbury A.R., and Marks J.D. Antibodys from phage antibody libraries. J Immunol Methods 290 1-2 (2004) 29-49
    • (2004) J Immunol Methods , vol.290 , Issue.1-2 , pp. 29-49
    • Bradbury, A.R.1    Marks, J.D.2
  • 18
    • 0034425742 scopus 로고    scopus 로고
    • Antibody arrays for high-throughput screening of antibody-antigen interactions
    • de Wildt R.M., Mundy C.R., Gorick B.D., and Tomlinson I.M. Antibody arrays for high-throughput screening of antibody-antigen interactions. Nat Biotechnol 18 9 (2000) 989-994
    • (2000) Nat Biotechnol , vol.18 , Issue.9 , pp. 989-994
    • de Wildt, R.M.1    Mundy, C.R.2    Gorick, B.D.3    Tomlinson, I.M.4
  • 21
    • 14144254365 scopus 로고    scopus 로고
    • Engineering high affinity superantigens by phage display
    • Enever C., Tomlinson I.M., Lund J., Levens M., and Holliger P. Engineering high affinity superantigens by phage display. J Mol Biol 347 1 (2005) 107-120
    • (2005) J Mol Biol , vol.347 , Issue.1 , pp. 107-120
    • Enever, C.1    Tomlinson, I.M.2    Lund, J.3    Levens, M.4    Holliger, P.5
  • 22
    • 0031882455 scopus 로고    scopus 로고
    • Peptides that mimic the group B streptococcal type III capsular polysaccharide antigen
    • Pincus S.H., Smith M.J., Jennings H.J., Burritt J.B., and Glee P.M. Peptides that mimic the group B streptococcal type III capsular polysaccharide antigen. J Immunol 160 1 (1998) 293-298
    • (1998) J Immunol , vol.160 , Issue.1 , pp. 293-298
    • Pincus, S.H.1    Smith, M.J.2    Jennings, H.J.3    Burritt, J.B.4    Glee, P.M.5
  • 23
    • 0031759422 scopus 로고    scopus 로고
    • Proteolytic selection for protein folding using filamentous bacteriophages
    • Kristensen P., and Winter G. Proteolytic selection for protein folding using filamentous bacteriophages. Fold Des 3 5 (1998) 321-328
    • (1998) Fold Des , vol.3 , Issue.5 , pp. 321-328
    • Kristensen, P.1    Winter, G.2
  • 24
    • 0023889342 scopus 로고
    • Protective efficacy of IgM monoclonal antibodys in experimental group B Streptococcal infections is a function of antibody avidity
    • Pincus S.H., Shigeoka A.O., Moe A.A., Ewing L.P., and Hill H.R. Protective efficacy of IgM monoclonal antibodys in experimental group B Streptococcal infections is a function of antibody avidity. J Immunol 140 8 (1988) 2779-2785
    • (1988) J Immunol , vol.140 , Issue.8 , pp. 2779-2785
    • Pincus, S.H.1    Shigeoka, A.O.2    Moe, A.A.3    Ewing, L.P.4    Hill, H.R.5
  • 25
    • 0034244316 scopus 로고    scopus 로고
    • By-passing selection: direct screening for antibody-antigen interactions using protein arrays
    • Holt L.J., Bussow K., Walter G., and Tomlinson I.M. By-passing selection: direct screening for antibody-antigen interactions using protein arrays. Nucleic Acids Res 28 15 (2000) E72
    • (2000) Nucleic Acids Res , vol.28 , Issue.15
    • Holt, L.J.1    Bussow, K.2    Walter, G.3    Tomlinson, I.M.4
  • 26
    • 10344222117 scopus 로고    scopus 로고
    • Enhancement of scFv fragment reactivity with target antigens in binding assays following mixing with anti-tag monoclonal antibodys
    • Wang X., Campoli M., Ko E., Luo W., and Ferrone S. Enhancement of scFv fragment reactivity with target antigens in binding assays following mixing with anti-tag monoclonal antibodys. J Immunol Methods 294 1-2 (2004) 23-25
    • (2004) J Immunol Methods , vol.294 , Issue.1-2 , pp. 23-25
    • Wang, X.1    Campoli, M.2    Ko, E.3    Luo, W.4    Ferrone, S.5
  • 27
    • 0033593356 scopus 로고    scopus 로고
    • Analysis of heavy and light chain pairings indicates that receptor editing shapes the human antibody repertoire
    • de Wildt R.M., Hoet R.M., van Venrooij W.J., Tomlinson I.M., and Winter G. Analysis of heavy and light chain pairings indicates that receptor editing shapes the human antibody repertoire. J Mol Biol 285 3 (1999) 895-901
    • (1999) J Mol Biol , vol.285 , Issue.3 , pp. 895-901
    • de Wildt, R.M.1    Hoet, R.M.2    van Venrooij, W.J.3    Tomlinson, I.M.4    Winter, G.5
  • 28
  • 29
    • 0036717716 scopus 로고    scopus 로고
    • Structure-function relationships for human antibodies to pneumococcal capsular polysaccharide form transgenic mice with human immunoglobulin loci
    • Chang Q., Zhong Z., Lees A., Pekna M., and Pirofski L. Structure-function relationships for human antibodies to pneumococcal capsular polysaccharide form transgenic mice with human immunoglobulin loci. Infect Immun 70 9 (2002) 4977-4986
    • (2002) Infect Immun , vol.70 , Issue.9 , pp. 4977-4986
    • Chang, Q.1    Zhong, Z.2    Lees, A.3    Pekna, M.4    Pirofski, L.5
  • 30
    • 0033014029 scopus 로고    scopus 로고
    • Molecular analysis of the heavy chain of antibodies that recognize the capsular polysaccharide of Neisseria meningitidis in hu-PBMC reconstituted SCID mice and in the immunized human donor
    • Smithson S.L., Srivastava N., Hutchins W.A., and Westerink M.A.J. Molecular analysis of the heavy chain of antibodies that recognize the capsular polysaccharide of Neisseria meningitidis in hu-PBMC reconstituted SCID mice and in the immunized human donor. Mol Immunol 36 2 (1999) 113-124
    • (1999) Mol Immunol , vol.36 , Issue.2 , pp. 113-124
    • Smithson, S.L.1    Srivastava, N.2    Hutchins, W.A.3    Westerink, M.A.J.4
  • 31
    • 0028213356 scopus 로고
    • Variable region sequence and idiotypic expression of a protective human immunoglobulin M antibody to capsular polysaccharides of Neisseria meningitides group B and Escherichia coli K1
    • Azmi F.H., Lucas A.H., Raff H.V., and Granoff D.M. Variable region sequence and idiotypic expression of a protective human immunoglobulin M antibody to capsular polysaccharides of Neisseria meningitides group B and Escherichia coli K1. Infect Immun 62 5 (1994) 1776-1786
    • (1994) Infect Immun , vol.62 , Issue.5 , pp. 1776-1786
    • Azmi, F.H.1    Lucas, A.H.2    Raff, H.V.3    Granoff, D.M.4
  • 32
    • 0032529425 scopus 로고    scopus 로고
    • Molecular analysis of polyreactive monoclonal antibodies from rheumatic carditis: human anti-N-acetylglucosamine/anti-myosin antibody V region genes
    • Adderson E.E., Shikhman A.R., Ward K.E., and Cunningham M.W. Molecular analysis of polyreactive monoclonal antibodies from rheumatic carditis: human anti-N-acetylglucosamine/anti-myosin antibody V region genes. J Immunol 161 15 (1998) 2020-2031
    • (1998) J Immunol , vol.161 , Issue.15 , pp. 2020-2031
    • Adderson, E.E.1    Shikhman, A.R.2    Ward, K.E.3    Cunningham, M.W.4
  • 33
    • 33846308870 scopus 로고    scopus 로고
    • Analysis of the young and elderly variable gene repertoire in response to pneumococcal polysaccharides using a reconstituted SCID mouse model
    • Shriner A.K., Smithson S.L., Rabquer B., Khuder S., and Westerink M.A.J. Analysis of the young and elderly variable gene repertoire in response to pneumococcal polysaccharides using a reconstituted SCID mouse model. Vaccine 24 49-50 (2006) 7159-7166
    • (2006) Vaccine , vol.24 , Issue.49-50 , pp. 7159-7166
    • Shriner, A.K.1    Smithson, S.L.2    Rabquer, B.3    Khuder, S.4    Westerink, M.A.J.5
  • 34
    • 0031808932 scopus 로고    scopus 로고
    • Human IgM antibodies to tumor-associated gangliosides share VHIII(V3-23) and VKIV family subgroups
    • Nishinaka Y., Hoon D.S.B., and Irie R.F. Human IgM antibodies to tumor-associated gangliosides share VHIII(V3-23) and VKIV family subgroups. Immunogenetics 48 1 (1998) 73-75
    • (1998) Immunogenetics , vol.48 , Issue.1 , pp. 73-75
    • Nishinaka, Y.1    Hoon, D.S.B.2    Irie, R.F.3
  • 36
    • 0042265270 scopus 로고    scopus 로고
    • VH3 gene usage in neutralizing human antibodies specific for the Entamoeba histolytica Gal/GalNac lestin heavy subunit
    • Tachibana H., Wantanabe K., Cheng X.-J., Tsukamoto H., Kaneda Y., Takeuchi T., et al. VH3 gene usage in neutralizing human antibodies specific for the Entamoeba histolytica Gal/GalNac lestin heavy subunit. Infect Immun 71 8 (2003) 4313-4319
    • (2003) Infect Immun , vol.71 , Issue.8 , pp. 4313-4319
    • Tachibana, H.1    Wantanabe, K.2    Cheng, X.-J.3    Tsukamoto, H.4    Kaneda, Y.5    Takeuchi, T.6
  • 38
    • 0043092240 scopus 로고    scopus 로고
    • NMR studies of carbohydrates and carbohydrate-mimetic peptides recognized by an anti-group B Streptococcus antibody
    • Johnson M.A., Jaseja M., Zou W., Jennings H.J., Copié V., Pinto B.M., et al. NMR studies of carbohydrates and carbohydrate-mimetic peptides recognized by an anti-group B Streptococcus antibody. J Biol Chem 278 27 (2003) 24740-24752
    • (2003) J Biol Chem , vol.278 , Issue.27 , pp. 24740-24752
    • Johnson, M.A.1    Jaseja, M.2    Zou, W.3    Jennings, H.J.4    Copié, V.5    Pinto, B.M.6
  • 39
    • 33644860729 scopus 로고    scopus 로고
    • Toward a better understanding of the basis of the molecular mimicry of polysaccharide antigens by peptides: the example of Shigella flexneri 5a
    • Clèment M.-J., Fortuné A., Phalipon A., Marcel-Peyre V., Simenel C., Imbery A., et al. Toward a better understanding of the basis of the molecular mimicry of polysaccharide antigens by peptides: the example of Shigella flexneri 5a. J Biol Chem 281 4 (2006) 2317-2332
    • (2006) J Biol Chem , vol.281 , Issue.4 , pp. 2317-2332
    • Clèment, M.-J.1    Fortuné, A.2    Phalipon, A.3    Marcel-Peyre, V.4    Simenel, C.5    Imbery, A.6
  • 40
    • 0032532032 scopus 로고    scopus 로고
    • Haemophilus influenzae type B polysaccharides-protein conjugate vaccine elicits a more diverse antibody repertoire in infants than in adults
    • Adderson E.E., Wilson P.M., Cunningham M.W., and Shackelford P.G. Haemophilus influenzae type B polysaccharides-protein conjugate vaccine elicits a more diverse antibody repertoire in infants than in adults. J Immunol 161 8 (1998) 4177-4182
    • (1998) J Immunol , vol.161 , Issue.8 , pp. 4177-4182
    • Adderson, E.E.1    Wilson, P.M.2    Cunningham, M.W.3    Shackelford, P.G.4
  • 41
    • 0036276927 scopus 로고    scopus 로고
    • A novel approach to study variable heavy chain gene usage in response to the capsular polysaccharide of Neisseria meningitides serogroup C
    • Srivastava N., Smithson S.L., and Westerink M.A.J. A novel approach to study variable heavy chain gene usage in response to the capsular polysaccharide of Neisseria meningitides serogroup C. J Immunol Methods 50 3 (2002) 249-262
    • (2002) J Immunol Methods , vol.50 , Issue.3 , pp. 249-262
    • Srivastava, N.1    Smithson, S.L.2    Westerink, M.A.J.3
  • 42
    • 0037035423 scopus 로고    scopus 로고
    • Rapid selection of anti-hapten antibodies isolated from synthetic and semi-synthetic antibody phage display libraries expressed in Escherichia coli
    • Strachen G., McElhiney J., Drever M.R., Mcintosh F., Lawton L.A., and Porter A.J.R. Rapid selection of anti-hapten antibodies isolated from synthetic and semi-synthetic antibody phage display libraries expressed in Escherichia coli. FEMS Microbiol Lett 210 2 (2002) 257-261
    • (2002) FEMS Microbiol Lett , vol.210 , Issue.2 , pp. 257-261
    • Strachen, G.1    McElhiney, J.2    Drever, M.R.3    Mcintosh, F.4    Lawton, L.A.5    Porter, A.J.R.6
  • 44
    • 10344224000 scopus 로고    scopus 로고
    • Molecular analysis of monoclonal antibodies to group variant capsular polysaccharides of Neisseria meningitidis: recurrent heavy chains and alternative light chain partners
    • Berry J.D., Boese D.J., Law D.K.S., Zollinger W.D., and Tsang R.S.W. Molecular analysis of monoclonal antibodies to group variant capsular polysaccharides of Neisseria meningitidis: recurrent heavy chains and alternative light chain partners. Mol Immunol 42 3 (2005) 335-344
    • (2005) Mol Immunol , vol.42 , Issue.3 , pp. 335-344
    • Berry, J.D.1    Boese, D.J.2    Law, D.K.S.3    Zollinger, W.D.4    Tsang, R.S.W.5
  • 45
    • 0142241395 scopus 로고    scopus 로고
    • Antibodies to keyhole limpet hemocyanin cross-react with an epitope on the polysaccharide capsule of Cryptococcus neoformans and other carbohydrates: implications for vaccine development
    • May R.J., Beenhouwer D.O., and Scharff M.D. Antibodies to keyhole limpet hemocyanin cross-react with an epitope on the polysaccharide capsule of Cryptococcus neoformans and other carbohydrates: implications for vaccine development. J Immunol 171 9 (2003) 4905-4912
    • (2003) J Immunol , vol.171 , Issue.9 , pp. 4905-4912
    • May, R.J.1    Beenhouwer, D.O.2    Scharff, M.D.3
  • 46
    • 1542573039 scopus 로고    scopus 로고
    • Peptide mimotopes as prototypic templates of broad-spectrum surrogates of carbohydrate antigens
    • Cunto-Amesty G., Luo P., Monzavi-Karbassi B., Lees A., Alexander J., del Guercio M.F., et al. Peptide mimotopes as prototypic templates of broad-spectrum surrogates of carbohydrate antigens. Cell Mol Biol 49 2 (2003) 245-254
    • (2003) Cell Mol Biol , vol.49 , Issue.2 , pp. 245-254
    • Cunto-Amesty, G.1    Luo, P.2    Monzavi-Karbassi, B.3    Lees, A.4    Alexander, J.5    del Guercio, M.F.6
  • 47
    • 0442292291 scopus 로고    scopus 로고
    • Two different methods result in the selection of peptides that induce a protective antibody response to Neisseria meningitidis serogroup C
    • Prinz D.M., Smithson S.L., and Westerink M.A. Two different methods result in the selection of peptides that induce a protective antibody response to Neisseria meningitidis serogroup C. J Immunol Methods 285 1 (2004) 1-14
    • (2004) J Immunol Methods , vol.285 , Issue.1 , pp. 1-14
    • Prinz, D.M.1    Smithson, S.L.2    Westerink, M.A.3
  • 48
    • 28944438775 scopus 로고    scopus 로고
    • Peptides mimicking Vibrio cholerae O139 capsular polysaccharide elicit protective antibody response
    • Falklind-Jerkerus S., Felici F., Cavalieri C., Lo Passo C., Garufi G., Pernice I., et al. Peptides mimicking Vibrio cholerae O139 capsular polysaccharide elicit protective antibody response. Microbes Infect 7 15 (2005) 1453-1460
    • (2005) Microbes Infect , vol.7 , Issue.15 , pp. 1453-1460
    • Falklind-Jerkerus, S.1    Felici, F.2    Cavalieri, C.3    Lo Passo, C.4    Garufi, G.5    Pernice, I.6
  • 49
    • 22244433830 scopus 로고    scopus 로고
    • A mimotope peptide-based anti-cancer vaccine selected by BAT monoclonal antibody
    • Hardy B., and Raiter A. A mimotope peptide-based anti-cancer vaccine selected by BAT monoclonal antibody. Vaccine 23 34 (2005) 4283-4291
    • (2005) Vaccine , vol.23 , Issue.34 , pp. 4283-4291
    • Hardy, B.1    Raiter, A.2
  • 50
    • 0030716928 scopus 로고    scopus 로고
    • Induction of anti-carbohydrate antibodies by phage library-selected peptide mimics
    • Phalipon A., Folgori A., Arondel J., Sgaramella G., Fortugno P., Cortese R., et al. Induction of anti-carbohydrate antibodies by phage library-selected peptide mimics. Eur J Immunol 27 10 (1997) 2620-2625
    • (1997) Eur J Immunol , vol.27 , Issue.10 , pp. 2620-2625
    • Phalipon, A.1    Folgori, A.2    Arondel, J.3    Sgaramella, G.4    Fortugno, P.5    Cortese, R.6
  • 51
    • 0035064035 scopus 로고    scopus 로고
    • Monoclonal antibodies specific for Neisseria meningitidis group B polysaccharide and their peptide mimotopes
    • Shin J.S., Lin J.S., Anderson P.W., Insel R.A., and Nahm M.H. Monoclonal antibodies specific for Neisseria meningitidis group B polysaccharide and their peptide mimotopes. Infect Immun 69 5 (2001) 3335-3342
    • (2001) Infect Immun , vol.69 , Issue.5 , pp. 3335-3342
    • Shin, J.S.1    Lin, J.S.2    Anderson, P.W.3    Insel, R.A.4    Nahm, M.H.5
  • 52
    • 3142735056 scopus 로고    scopus 로고
    • Selection of poly-alpha 2,8-sialic acid mimotopes from a random phage peptide library and analysis of their bioactivity
    • Torregrossa P., Buhl L., Bancila M., Durbec P., Schafer C., Schachner M., et al. Selection of poly-alpha 2,8-sialic acid mimotopes from a random phage peptide library and analysis of their bioactivity. J Biol Chem 279 29 (2004) 30707-30714
    • (2004) J Biol Chem , vol.279 , Issue.29 , pp. 30707-30714
    • Torregrossa, P.1    Buhl, L.2    Bancila, M.3    Durbec, P.4    Schafer, C.5    Schachner, M.6
  • 53
    • 15044361492 scopus 로고    scopus 로고
    • Peptide mimics as surrogate immunogens of mosquito midgut carbohydrate malaria transmission blocking targets
    • Dinglasan R.R., Porter-Kelley J.M., Alam U., and Azad A.F. Peptide mimics as surrogate immunogens of mosquito midgut carbohydrate malaria transmission blocking targets. Vaccine 23 21 (2005) 2717-2724
    • (2005) Vaccine , vol.23 , Issue.21 , pp. 2717-2724
    • Dinglasan, R.R.1    Porter-Kelley, J.M.2    Alam, U.3    Azad, A.F.4
  • 54
  • 55
    • 21444439732 scopus 로고    scopus 로고
    • Generation of high-affinity human antibodies by combining donor-derived and synthetic complementarity-determining-region diversity
    • Hoet R.M., Cohen E.H., Kent R.B., Rookey K., Schoonbroodt S., Hogan S., et al. Generation of high-affinity human antibodies by combining donor-derived and synthetic complementarity-determining-region diversity. Nat Biotechnol 23 3 (2005) 344-348
    • (2005) Nat Biotechnol , vol.23 , Issue.3 , pp. 344-348
    • Hoet, R.M.1    Cohen, E.H.2    Kent, R.B.3    Rookey, K.4    Schoonbroodt, S.5    Hogan, S.6
  • 56
    • 0034635335 scopus 로고    scopus 로고
    • Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides
    • Knappik A., Ge L., Honegger A., Pack P., Fischer M., Wellnhofer G., et al. Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides. J Mol Biol 296 1 (2000) 57-86
    • (2000) J Mol Biol , vol.296 , Issue.1 , pp. 57-86
    • Knappik, A.1    Ge, L.2    Honegger, A.3    Pack, P.4    Fischer, M.5    Wellnhofer, G.6
  • 57
    • 20644459237 scopus 로고    scopus 로고
    • Protein microarrays for antibody profiling: specificity and affinity determination on a chip
    • Poetz O., Ostendorp R., Brocks B., Schwenk J.M., Stoll D., Joos T.O., et al. Protein microarrays for antibody profiling: specificity and affinity determination on a chip. Proteomics 5 9 (2005) 2402-2411
    • (2005) Proteomics , vol.5 , Issue.9 , pp. 2402-2411
    • Poetz, O.1    Ostendorp, R.2    Brocks, B.3    Schwenk, J.M.4    Stoll, D.5    Joos, T.O.6


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