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Original Paper

Identification of Potentially Cross-Reactive Peanut-Lupine Proteins by Computer-Assisted Search for Amino Acid Sequence Homology

Guarneri F.a · Guarneri C.a · Benvenga S.b, c

Author affiliations

aIstituto di Dermatologia, Policlinico Gaetano Martino, and bSezione di Endocrinologia del Dipartimento Clinico Sperimentale di Medicina e Farmacologia, Università di Messina, cProgramma Infradipartimentale di Endocrinologia Molecolare Clinica, Azienda Ospedaliera Universitaria Policlinico Gaetano Martino, Messina, Italia

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Int Arch Allergy Immunol 2005;138:273–277

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Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: February 15, 2005
Accepted: May 18, 2005
Published online: November 18, 2005
Issue release date: December 2005

Number of Print Pages: 5
Number of Figures: 4
Number of Tables: 0

ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)

For additional information: https://www.karger.com/IAA

Abstract

Background: Allergic cross-reactions are an issue of major concern because of implications for public health. The molecular basis of cross-allergy is the similarity of epitopes belonging to proteins of different organisms. Lupine is an emerging cause of food allergy, which has become a ‘hot topic’ because of recent large-scale introduction into processed foods and frequent cross-reactions with other members of the legume family. However, no lupine allergen has been characterized thus far. Prompted by a recently reported case of peanut-lupine cross-allergy, we wished to identify the possible cross-reactive allergen(s) between the two vegetal species. Methods: We used computer-aided amino acid sequence comparison, a well-established technique for the study of protein homology, and followed the FAO/WHO guidelines for the identification of potential allergens. We also performed a three-dimensional modeling of the suspected cross-reactive proteins to compare their molecular surfaces. Results: We found a highly significant sequence homology and molecular similarity between allergen Ara h 8 of peanut and pathogenesis-related protein PR-10 of white lupine. Another protein of lupine, the β-conglutin precursor, was found to be significantly homologous to the Ara h 1 allergen of peanut. The molecular surfaces of Ara h 8 and PR-10 were remarkably similar. Conclusions: Our in silico data allow to predict the allergenicity of PR-10 and β-conglutin precursor of white lupine according to FAO/WHO guidelines. Amino acid sequence homology also suggests that these proteins could be responsible, at least in part, for some of the allergic cross-reactions between peanut and lupine reported in the literature.

© 2005 S. Karger AG, Basel


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Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: February 15, 2005
Accepted: May 18, 2005
Published online: November 18, 2005
Issue release date: December 2005

Number of Print Pages: 5
Number of Figures: 4
Number of Tables: 0

ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)

For additional information: https://www.karger.com/IAA


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