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Vol. 157, No. 1, 2012
Issue release date: December 2011
Section title: Original Paper
Int Arch Allergy Immunol 2012;157:51–57
(DOI:10.1159/000324946)

Lentil (Lens culinaris) Lipid Transfer Protein Len c 3: A Novel Legume Allergen

Akkerdaas J.e · Finkina E.I.b · Balandin S.V.b · Santos Magadán S.c · Knulst A.d · Fernandez-Rivas M.c · Asero R.a · van Ree R.e, f · Ovchinnikova T.V.b
aClinica San Carlo, Paderno Dugnano, Italy; bShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia; cAllergy Department, Hospital Clinico San Carlos, Madrid, Spain; dDepartment of Dermatology and Allergology, University Medical Center of Utrecht, Utrecht, and Departments of eExperimental Immunology and fOtorhinolaryngology, Academic Medical Center, Amsterdam, The Netherlands

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Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: 7/8/2010
Accepted: 2/7/2011
Published online: 9/6/2011
Issue release date: December 2011

Number of Print Pages: 7
Number of Figures: 5
Number of Tables: 1

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

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

Abstract

Background: Lentils are increasingly consumed in many parts of the world.Two allergens, Len c 1 and 2, have been reported previously. Recently, peanut and green bean lipid transfer proteins (LTPs) have been identified as the first two members of an important group of allergens that might be associated with severe food allergies. Objective: To investigate lentil LTP as a potential new allergen. Methods: Efficacy of LTP extraction was monitored at different acidic pH values, using immunoblotting with cross-reactive anti-peach LTP antiserum. Natural LTP was purified from lentil extract and expressed as recombinant allergen in Escherichia coli. Sera from 10 lentil-allergic and/or -sensitized patients (Spain: 6, Italy: 1 and the Netherlands: 3) were used to further characterize lentil LTP. Results: Natural lentil LTP, purified from the homogenized germinated seeds and optimally extracted at pH 3, was identified and designated as allergen Len c 3. By CAP, 9/10 sera showed specific IgE to Len c 3. Recombinant (r) Len c 3 was successfully purified. The natural (n) Len c 3 CAP was completely inhibited by rLen c 3/rPru p 3. IgE binding to lentil pH 3 extract blot was completely inhibited by rLen c 3. Conclusion: The availability of immunochemically active nLen/rLen c 3 as a novel legume allergen facilitates further development and implementation of a third (next to peanut and green bean) legume LTP in component-resolved diagnosis strategies and contributes to evaluate the clinical importance of legume LTPs. Preferential extraction of Len c 3 (pH 3) will affect the production of sensitive extract-based diagnostic tests.

© 2011 S. Karger AG, Basel


  

Author Contacts

Correspondence to: Prof. Dr. R. van Ree
Department of Experimental Immunology
Academic Medical Center, Meibergdreef 9
NL–1105 AZ Amsterdam (The Netherlands)
Tel. +31 20 566 6819, E-Mail R.vanRee@amc.uva.nl

  

Article Information

J.A. and E.I.F. contributed equally to this work.

Received: July 8, 2010
Accepted after revision: February 7, 2011
Published online: September 6, 2011
Number of Print Pages : 7
Number of Figures : 5, Number of Tables : 1, Number of References : 26

  

Publication Details

International Archives of Allergy and Immunology

Vol. 157, No. 1, Year 2012 (Cover Date: December 2011)

Journal Editor: Valenta R. (Vienna)
ISSN: 1018-2438 (Print), eISSN: 1423-0097 (Online)

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


Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: 7/8/2010
Accepted: 2/7/2011
Published online: 9/6/2011
Issue release date: December 2011

Number of Print Pages: 7
Number of Figures: 5
Number of Tables: 1

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

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


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