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Identification of peptide motifs recognized by a human IgG autoanti-IgE antibody using a phage display library

Authors

  • Shakib,

    1. Division of Molecular and Clinical Immunology, University of Nottingham, Faculty of Medicine & Health Sciences, Nottingham, NG7 2UH, United Kingdom
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  • Hooi,

    1. Division of Molecular and Clinical Immunology, University of Nottingham, Faculty of Medicine & Health Sciences, Nottingham, NG7 2UH, United Kingdom
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  • Smith,

    1. Division of Molecular and Clinical Immunology, University of Nottingham, Faculty of Medicine & Health Sciences, Nottingham, NG7 2UH, United Kingdom
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  • Furmonaviciene,

    1. Division of Molecular and Clinical Immunology, University of Nottingham, Faculty of Medicine & Health Sciences, Nottingham, NG7 2UH, United Kingdom
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  • Sewell

    1. Division of Molecular and Clinical Immunology, University of Nottingham, Faculty of Medicine & Health Sciences, Nottingham, NG7 2UH, United Kingdom
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Dr Shakib Division of Molecular and Clinical Immunology, University of Nottingham, Faculty of Medicine & Health Sciences, Queen's Medical Centre, Nottingham, NG7 2UH, UK.

Abstract

Background

The potential of murine monoclonal anti-IgE antibodies as long-term therapy for atopic diseases will have to rely, for the time being, on passive antibody administration. There is therefore considerable interest in developing a peptide-based vaccine for active immunization to elicit long-term protective anti-IgE antibodies in the patient. It has been shown that some human IgG autoanti-IgE antibodies have the ability to partially block the binding of IgE to Fc receptors such as FcεRI. Therefore, the epitopes recognized by such antibodies could have vaccine potential.

Objective

To determine the epitope specificity of one such human IgG anti-IgE antibody.

Methods

A 15-mer phage-peptide library was used to establish the epitope specificity of an IgG anti-IgE antibody isolated from the serum of an asthma patient.

Results

The SRPSP sequence, or part of it (i.e. RPS, RPSP, SPS or PSP), was present in all 18 phage-peptides that have been sequenced. This common motif was found to be within the human ε chain sequence Ser341-Thr355 near the N-terminus of the Cε3 domain. According to the human Fcε model, the most accessible residues in this sequence are Arg342, Ile350, Arg351, Lys352 and Ser353.

Conclusions

The present data should provide the molecular basis for the rational design of a suitable peptide immunogen (vaccine) for boosting the production of protective autoanti-IgE antibodies.

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