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Original Paper

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

Author affiliations

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

Related Articles for ""

Int Arch Allergy Immunol 2012;157:51–57

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Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: July 08, 2010
Accepted: February 07, 2011
Published online: September 06, 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: https://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


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Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: July 08, 2010
Accepted: February 07, 2011
Published online: September 06, 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: https://www.karger.com/IAA


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