Literature DB >> 19609960

2-D DIGE analysis of the proteome of extracts from peanut variants reveals striking differences in major allergen contents.

Hendrik Schmidt1, Christoph Gelhaus, Ties Latendorf, Melanie Nebendahl, Arnd Petersen, Susanne Krause, Matthias Leippe, Wolf-Meinhard Becker, Ottmar Janssen.   

Abstract

Over the last decade, an increasing prevalence of peanut allergies was observed worldwide. Peanuts are meanwhile categorized among the most dangerous food allergens. This is particularly relevant since peanut-derived ingredients are widely used in industrial food production. To minimize the problem of hidden food allergens causing severe anaphylactic reactions, pre-packaged food containing peanut components needs to be classified according to European ruling since 2005. Food companies search for strategies to reduce the allergenicity of peanut-derived food additives either by genetically altering the allergen content or by identifying peanut varieties with low levels of major allergens. In our study, we focused on peanut extracts from Indonesia that apparently contain lower levels of the major Arachis hypogaea allergen 1 (Ara h 1). Basic extracts of Virginia-type and Indonesian peanuts were compared by 1- and 2-DE. We identified more than hundred individual components in these extracts by MS and provide a high-resolution allergen map that also includes so far unknown fragments of major peanut allergens. The reduced level of Ara h 1 associated with a significantly lower abundance of the most potent peanut allergen Ara h 2 in various Indonesian peanuts was also confirmed by Western blotting with monoclonal antibodies and sera of allergic patients.

Entities:  

Mesh:

Substances:

Year:  2009        PMID: 19609960     DOI: 10.1002/pmic.200800938

Source DB:  PubMed          Journal:  Proteomics        ISSN: 1615-9853            Impact factor:   3.984


  4 in total

1.  The 2S albumin allergens of Arachis hypogaea, Ara h 2 and Ara h 6, are the major elicitors of anaphylaxis and can effectively desensitize peanut-allergic mice.

Authors:  M Kulis; X Chen; J Lew; Q Wang; O P Patel; Y Zhuang; K S Murray; M W Duncan; H S Porterfield; A W Burks; S C Dreskin
Journal:  Clin Exp Allergy       Date:  2012-02       Impact factor: 5.018

2.  Primary sequence and site-selective hydroxylation of prolines in isoforms of a major peanut allergen protein Ara h 2.

Authors:  Jinxi Li; Kevin Shefcheck; John Callahan; Catherine Fenselau
Journal:  Protein Sci       Date:  2010-01       Impact factor: 6.725

3.  Analysis of common bean expressed sequence tags identifies sulfur metabolic pathways active in seed and sulfur-rich proteins highly expressed in the absence of phaseolin and major lectins.

Authors:  Fuqiang Yin; Agnieszka Pajak; Ralph Chapman; Andrew Sharpe; Shangzhi Huang; Frédéric Marsolais
Journal:  BMC Genomics       Date:  2011-05-26       Impact factor: 3.969

Review 4.  Peanut allergens.

Authors:  Chiara Palladino; Heimo Breiteneder
Journal:  Mol Immunol       Date:  2018-04-19       Impact factor: 4.407

  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.