Epitope mapping

Horsfall, Angela C.; Hay, Frank C.; Soltys, A; Jones, Meinir

doi:10.1016/0167-5699(91)90029-s

Cited by 44 publications

(23 citation statements)

References 9 publications

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“…The use of synthetic peptides to map the epitope specificity of the antibody response must be approached with caution ( 18,34 (14,22,23,35,36) and can prevent experimental infection (8). Because V3 synthetic peptides can induce neutralizing antibody, it is thought that the V3 neutralizing determinant may be a linear epitope.…”

Section: Resultsmentioning

confidence: 99%

Differences in the antibody response to human immunodeficiency virus-1 envelope glycoprotein (gp160) in infected laboratory workers and vaccinees.

Pincus

Messer²,

Schwartz³

et al. 1993

J. Clin. Invest.

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Studies of the immune response to the human immunodeficiency virus (HIV) have been hampered by the antigenic diversity of the HIV envelope protein. In an effort to predict the efficacy of vaccination we have compared the systemic antienvelope antibody response in seronegative volunteers immunized with recombinant gpl60 (either in vaccinia or as soluble protein produced in baculovirus) derived from the HTLV-IIIB strain of HIV-1 and in two laboratory workers accidentally infected with the same strain. 11 of 14 vaccinees responded to immunization by producing anti-gpl60 of similar titer and the same isotype as that seen in the laboratory workers. Four vaccinees also had antibody to the principal neutralizing domain (V3 loop) that was comparable in titer with that seen in the laboratory workers, but the fine specificity of anti-V3 antibody was qualitatively different in the two groups. Antibody that can block the interaction between CD4 and gpl20 was present at comparable levels in three vaccinees and the lab workers. Neutralizing antibody titers were markedly lower in the vaccinees than in the laboratory workers. In seven of the vaccinees, an immunodominant epitope was at amino acid 720-740. Analyses of monoclonal antibodies to this region indicate that they do not neutralize, bind to infected cells, nor function as immunotoxins. Although the anti-gpl60 antibody response was of similar magnitude in both infected and vaccinated individuals, there were important qualitative differences. (J. Clin. Invest. 1993.

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Section: Resultsmentioning

confidence: 99%

Differences in the antibody response to human immunodeficiency virus-1 envelope glycoprotein (gp160) in infected laboratory workers and vaccinees.

Pincus

Messer²,

Schwartz³

et al. 1993

J. Clin. Invest.

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“…Recent advances in peptide synthesis have made possible the use of an ELISA to screen antibody (inhibitor) binding to synthetic peptides that have been immobilized on blocks of 96 polyethylene pins. This technique permits precise mapping of epitopes based on a protein's known amino acid sequence, is capable of screening multiple peptides simulta neously and also allows for regeneration of the pin peptides by removal of the bound antibodies after each use [25,27]. We have used these peptide arrays to map antibody-defined epitopes of FVIII.…”

Section: Concurrence Of Fviii Inhibitor Specificitiesmentioning

confidence: 99%

“…Recent advances in peptide synthesis technology [25,26], coupled to an EL ISA, permitted the screening of antibody binding to a li brary of immobilized synthetic FVIII peptides [27]. We ob tained a detailed and highly precise picture of the reactivity of antibodies against a large number of FVIII peptides and have identified several novel epitopes.…”

mentioning

confidence: 99%

Identification of Novel Factor VIII Inhibitor Epitopes using Synthetic Peptide Arrays

Palmer¹,

Dudani²,

Drouin³

et al. 1997

Vox Sanguinis

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Objectives: Mapping the antibody-binding sites on the factor VIII (FVIII) protein opens the prospect of studying the development of FVIII inhibitors and the alteration of inhibitor specificities over time. This paper describes a novel approach to the mapping of FVIII antibody-binding sites. Methods: Immobilized synthetic peptide arrays covering 80% of the complete 2351 amino acid sequence of factor VIII (FVIII) were used to determine epitope specificity of 6 alloantibodies and 3 autoantibodies inhibitory to FVIII activity. This detailed assessment was carried out using a modified enzyme-linked immunosorbent assay with plasma from normal persons or hemophilia A patients without inhibitors as negative controls. Results: Antibody-combining sites could be differentiated in both a qualitative and quantitative manner and were patient-specific. Highly reactive peptides were restricted to specific sites in the A1-A3 and C1-C2 domains and were not proximal to known proteolytic cleavage sites. Free peptides incubated in vitro with the plasmas of 3 patients significantly reduced residual inhibitor titers in a dose-dependent manner. Conclusion: This technique permits the study of the development and specificity of FVIII inhibitors, can detect and differentiate between inhibitory and noninhibitory antibodies using immobilized or free peptides respectively, permits correlation of antibody-combining sites with inhibition of FVIII activity and provides a basis for the development of inhibitor adsorption or neutralization technology.

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“…The approach presented in this study may benefit similar attempts to localize B cell epitopes on other antigens, espe cially when the epitopes are discontinuous as it is the case with more than 90% of the antigens studied [24], 268 Schncidcr/Dudlcr/Gelb/Suter PLA Lysines and B Cell Epitopes …”

Section: Discussionmentioning

confidence: 99%

Lysine Residues in Bee Venom Phospholipase A<sub>2</sub> Are Important for Binding to Human Monoclonal or Polyclonal Antibodies of the lgG4 Isotope

Schneider¹,

Dudler

Gelb

et al. 1994

Int Arch Allergy Immunol

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Discontinuous antigenic sites on bee venom phospholipase A₂ (PLA) have been mapped using human monoclonal antibodies or human polyclonal serum antibodies (hpAbs) of the IgG4 isotype from beekeepers or of the IgE isotype from individuals allergic to PLA. Lysine residues of PLA have been specifically modified by acetylation or acylation by treatment with citraconic anhydride of their ε-amino groups to analyze their role in antigen-antibody binding. After the modifications, the binding of PLA to the human monoclonal antibodies is lost, whereas the binding to IgG4 hpAbs is significantly decreased. In contrast, the effect on the binding of PLA to IgE hpAbs appears to be more heterogeneous. The data indicate the importance of lysine residues as being part of B cell epitopes in PLA-specifíc antibodies of the IgG4 isotype, but less so for those of the IgE isotype.

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Epitope mapping

Cited by 44 publications

References 9 publications

Differences in the antibody response to human immunodeficiency virus-1 envelope glycoprotein (gp160) in infected laboratory workers and vaccinees.

Differences in the antibody response to human immunodeficiency virus-1 envelope glycoprotein (gp160) in infected laboratory workers and vaccinees.

Identification of Novel Factor VIII Inhibitor Epitopes using Synthetic Peptide Arrays

Lysine Residues in Bee Venom Phospholipase A<sub>2</sub> Are Important for Binding to Human Monoclonal or Polyclonal Antibodies of the lgG4 Isotope

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