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Vol. 138, No. 4, 2005
Issue release date: December 2005
Section title: Original Paper
Int Arch Allergy Immunol 2005;138:273–277
(DOI:10.1159/000088864)

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

Guarneri F. · Guarneri C. · Benvenga S.
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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Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: 2/15/2005
Accepted: 5/18/2005
Published online: 11/18/2005

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

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

For additional information: http://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.


  

Author Contacts

Correspondence to: Fabrizio Guarneri, MD
Viale Annunziata, Residence dei Fiori
Villa 7
IT–98168 Messina (Italy)
Tel. +39 090 357070, Fax +39 090 2927691, E-Mail f.guarneri@tiscali.it

  

Article Information

Received: February 15, 2005
Accepted after revision: May 18, 2005
Published online: October 7, 2005
Number of Print Pages : 5
Number of Figures : 4, Number of Tables : 0, Number of References : 15

  

Publication Details

International Archives of Allergy and Immunology

Vol. 138, No. 4, Year 2005 (Cover Date: December 2005)

Journal Editor: Valenta, R. (Vienna)
ISSN: 1018–2438 (print), 1423–0097 (Online)

For additional information: http://www.karger.com/iaa


Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: 2/15/2005
Accepted: 5/18/2005
Published online: 11/18/2005

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

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

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


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