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Related Experiment Videos

Sequence homology: a poor predictive value for profilins cross-reactivity.

Mojtaba Sankian1, Abdolreza Varasteh, Nazanin Pazouki

  • 1Immunology Research Center, Bu-Ali Research Institute, Mashhad, Iran. m_sankian@hotmail.com

Clinical and Molecular Allergy : CMA
|September 13, 2005
PubMed
Summary

Melon profilin’s cross-reactivity in plant allergies is driven by its conserved conformational structure, not just sequence identity. Human IgE antibodies bind to intact melon profilin, highlighting the importance of its 3D shape for allergic reactions.

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Area of Science:

  • Allergen immunotherapy
  • Molecular allergology
  • Immunology

Background:

  • Profilins are common cross-reactive allergens found in plants, eliciting IgE antibody responses in approximately 20% of individuals with plant allergies.
  • Understanding cross-reactivity between profilins is crucial for diagnosing and managing plant-food allergies.

Purpose of the Study:

  • To investigate the cross-reactivity of melon profilin with other plant profilins.
  • To determine the role of linear and conformational epitopes in human IgE cross-reactivity to melon profilin.

Main Methods:

  • Recombinant melon profilin was expressed and its IgE binding and cross-reactivity were assessed using ELISA and inhibition ELISA.
  • Amino acid sequences and 3D structures of melon profilin and other profilins were compared.

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  • Chemical cleavage and immunoblotting were employed to differentiate the roles of linear and conformational epitopes.

    • Main Results:

    • Melon profilin was identified as a major IgE-binding component in melon allergy.
    • Significant cross-reactivity was observed with profilins from tomato, peach, grape, and Bermuda grass.
    • Human IgE reactivity was dependent on the intact conformational structure of melon profilin, with differences in 3D models influencing conformational epitopes.

    Conclusions:

    • Human IgE reactivity to melon profilin is primarily dictated by its conserved conformational structure.
    • Amino acid sequence identity and linear epitopes play a lesser role in IgE cross-reactivity compared to conformational epitopes.