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Volumn 46, Issue 1, 2008, Pages 125-134

A novel computer algorithm improves antibody epitope prediction using affinity-selected mimotopes: A case study using monoclonal antibodies against the West Nile virus E protein

Author keywords

Epitope mapping; Flavivirus; Monoclonal antibody; Neutralization; Phage display

Indexed keywords

EPITOPE; MIMOTOPE; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; UNCLASSIFIED DRUG; VIRUS PROTEIN; WEST NILE VIRUS E PROTEIN;

EID: 52949094267     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2008.07.020     Document Type: Article
Times cited : (24)

References (25)
  • 1
    • 0029920670 scopus 로고    scopus 로고
    • Probing the basis of antibody reactivity with a panel of constrained peptide libraries displayed by filamentous phage
    • Bonnycastle L.L., Mehroke J.S., Rashed M., Gong X., and Scott J.K. Probing the basis of antibody reactivity with a panel of constrained peptide libraries displayed by filamentous phage. J. Mol. Biol. 258 (1996) 747-762
    • (1996) J. Mol. Biol. , vol.258 , pp. 747-762
    • Bonnycastle, L.L.1    Mehroke, J.S.2    Rashed, M.3    Gong, X.4    Scott, J.K.5
  • 2
    • 0028708594 scopus 로고
    • Epitope mapping of a protein using the Geysen (PEPSCAN) procedure
    • Carter J.M. Epitope mapping of a protein using the Geysen (PEPSCAN) procedure. Methods Mol. Biol. 36 (1994) 207-223
    • (1994) Methods Mol. Biol. , vol.36 , pp. 207-223
    • Carter, J.M.1
  • 3
    • 33645794229 scopus 로고    scopus 로고
    • Nuclear magnetic resonance structure-based epitope mapping and modulation of dust mite group 13 allergen as a hypoallergen
    • Chan S.L., Ong S.T., Ong S.Y., Chew F.T., and Mok Y.K. Nuclear magnetic resonance structure-based epitope mapping and modulation of dust mite group 13 allergen as a hypoallergen. J. Immunol. 176 (2006) 4852-4860
    • (2006) J. Immunol. , vol.176 , pp. 4852-4860
    • Chan, S.L.1    Ong, S.T.2    Ong, S.Y.3    Chew, F.T.4    Mok, Y.K.5
  • 4
    • 0024368992 scopus 로고
    • Significant structural and functional change of an antigen-binding site by a distant amino acid substitution: proposal of a structural mechanism
    • Chien N.C., Roberts V.A., Giusti A.M., Scharff M.D., and Getzoff E.D. Significant structural and functional change of an antigen-binding site by a distant amino acid substitution: proposal of a structural mechanism. Proc. Natl. Acad. Sci. U.S.A. 86 (1989) 5532-5536
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 5532-5536
    • Chien, N.C.1    Roberts, V.A.2    Giusti, A.M.3    Scharff, M.D.4    Getzoff, E.D.5
  • 6
    • 36348931103 scopus 로고    scopus 로고
    • A monoclonal Fab derived from a human nonimmune phage library reveals a new epitope on gp41 and neutralizes diverse human immunodeficiency virus type 1 strains
    • Gustchina E., Louis J.M., Lam S.N., Bewley C.A., and Clore G.M. A monoclonal Fab derived from a human nonimmune phage library reveals a new epitope on gp41 and neutralizes diverse human immunodeficiency virus type 1 strains. J. Virol. 81 (2007) 12946-12953
    • (2007) J. Virol. , vol.81 , pp. 12946-12953
    • Gustchina, E.1    Louis, J.M.2    Lam, S.N.3    Bewley, C.A.4    Clore, G.M.5
  • 7
    • 0037081391 scopus 로고    scopus 로고
    • Construction of recombinant targeting immunogens incorporating an HIV-1 neutralizing epitope into sites of differing conformational constraint
    • Ho J., MacDonald K.S., and Barber B.H. Construction of recombinant targeting immunogens incorporating an HIV-1 neutralizing epitope into sites of differing conformational constraint. Vaccine 20 (2002) 1169-1180
    • (2002) Vaccine , vol.20 , pp. 1169-1180
    • Ho, J.1    MacDonald, K.S.2    Barber, B.H.3
  • 8
    • 0030855425 scopus 로고    scopus 로고
    • The three-dimensional structure of a T-cell antigen receptor V alpha V beta heterodimer reveals a novel arrangement of the V beta domain
    • Housset D., Mazza G., Gregoire C., Piras C., Malissen B., and Fontecilla-Camps J.C. The three-dimensional structure of a T-cell antigen receptor V alpha V beta heterodimer reveals a novel arrangement of the V beta domain. EMBO J. 16 (1997) 4205-4216
    • (1997) EMBO J. , vol.16 , pp. 4205-4216
    • Housset, D.1    Mazza, G.2    Gregoire, C.3    Piras, C.4    Malissen, B.5    Fontecilla-Camps, J.C.6
  • 9
    • 34447096122 scopus 로고    scopus 로고
    • Sequence analysis and rule development of predicting protein stability change upon mutation using decision tree model
    • Huang L.T., Gromiha M.M., and Ho S.Y. Sequence analysis and rule development of predicting protein stability change upon mutation using decision tree model. J. Mol. Model 13 (2007) 879-890
    • (2007) J. Mol. Model , vol.13 , pp. 879-890
    • Huang, L.T.1    Gromiha, M.M.2    Ho, S.Y.3
  • 11
    • 0027533024 scopus 로고
    • Mutations that significantly change the stability, flexibility and quaternary structure of the l-lactate dehydrogenase from Bacillus megaterium
    • Kotik M., and Zuber H. Mutations that significantly change the stability, flexibility and quaternary structure of the l-lactate dehydrogenase from Bacillus megaterium. Eur. J. Biochem. 211 (1993) 267-280
    • (1993) Eur. J. Biochem. , vol.211 , pp. 267-280
    • Kotik, M.1    Zuber, H.2
  • 12
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong P.D., Wyatt R., Robinson J., Sweet R.W., Sodroski J., and Hendrickson W.A. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393 (1998) 648-659
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 15
    • 0024830833 scopus 로고
    • Replacement of a conserved proline and the alkaline conformational change in iso-2-cytochrome c
    • Nall B.T., Zuniga E.H., White T.B., Wood L.C., and Ramdas L. Replacement of a conserved proline and the alkaline conformational change in iso-2-cytochrome c. Biochemistry 28 (1989) 9834-9839
    • (1989) Biochemistry , vol.28 , pp. 9834-9839
    • Nall, B.T.1    Zuniga, E.H.2    White, T.B.3    Wood, L.C.4    Ramdas, L.5
  • 16
  • 20
    • 0032410325 scopus 로고    scopus 로고
    • Evaluation of Pepscan analyses for epitope mapping of anti-MUC1 monoclonal antibodies-a comparative study and review of five antibodies
    • Petrakou E., Murray A., Rosamund C., Graves L., and Price M.R. Evaluation of Pepscan analyses for epitope mapping of anti-MUC1 monoclonal antibodies-a comparative study and review of five antibodies. Anticancer Res 18 (1998) 4419-4421
    • (1998) Anticancer Res , vol.18 , pp. 4419-4421
    • Petrakou, E.1    Murray, A.2    Rosamund, C.3    Graves, L.4    Price, M.R.5
  • 21
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott J.K., and Smith G.P. Searching for peptide ligands with an epitope library. Science 249 (1990) 386-390
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 23
    • 0026233070 scopus 로고
    • Surface presentation of protein epitopes using bacteriophage expression systems
    • Smith G.P. Surface presentation of protein epitopes using bacteriophage expression systems. Curr. Opin. Biotechnol. 2 (1991) 668-673
    • (1991) Curr. Opin. Biotechnol. , vol.2 , pp. 668-673
    • Smith, G.P.1
  • 24
    • 52949127085 scopus 로고    scopus 로고
    • Smith, G.P., Phage-Display Vectors and Libraries Based on Filamentous Phage Strain fd-tet, 2006 http://www.biosci.missouri.edu/smithgp/PhageDisplayWebsite/PhageDisplayWebsiteIndex.html.
    • Smith, G.P., Phage-Display Vectors and Libraries Based on Filamentous Phage Strain fd-tet, 2006 http://www.biosci.missouri.edu/smithgp/PhageDisplayWebsite/PhageDisplayWebsiteIndex.html.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.