Peanut varieties with reduced Ara h 1 content indicating no reduced allergenicity

Molecular Nutrition and Food Research

Volumn 54, Issue 3, 2010, Pages 381-387

  Krause, Susanne ^a   Latendorf, Ties ^b   Schmidt, Hendrik ^b   Darcan Nicolaisen, Yasemin ^a   Reese, Gerald ^c   Petersen, Arnd ^a   Janssen, Ottmar ^b   Becker, Wolf Meinhard ^a  

^a RESEARCH CENTER BORSTEL   (Germany)

^b UNIVERSITY HOSPITAL SCHLESWIG HOLSTEIN   (Germany)

^c PAUL EHRLICH INSTITUT   (Germany)

Author keywords

Allergenicity; Ara h 1; Hypoallergenic peanuts; Peanut allergy; Seed storage protein

Indexed keywords

ALLERGEN; ARA H 1 PROTEIN, ARACHIS HYPOGAEA; GLYCOPROTEIN; PLANT ANTIGEN; PLANT EXTRACT; VEGETABLE PROTEIN;

ANIMAL; ARTICLE; BASOPHIL; BASOPHIL DEGRANULATION TEST; CELL LINE; CHEMISTRY; COMPARATIVE STUDY; DOSE RESPONSE; ENZYME LINKED IMMUNOSORBENT ASSAY; HUMAN; IMMUNOLOGY; ISOLATION AND PURIFICATION; NUT; PATHOPHYSIOLOGY; PEANUT; PEANUT ALLERGY; PHYSIOLOGY; PROTEIN INTAKE; RAT; SOUTHEAST ASIA; SPECIES DIFFERENCE; TWO DIMENSIONAL GEL ELECTROPHORESIS;

ALLERGENS; ANIMALS; ANTIGENS, PLANT; ARACHIS HYPOGAEA; ASIA, SOUTHEASTERN; BASOPHIL DEGRANULATION TEST; BASOPHILS; CELL LINE; DIETARY PROTEINS; DOSE-RESPONSE RELATIONSHIP, IMMUNOLOGIC; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; ENZYME-LINKED IMMUNOSORBENT ASSAY; GLYCOPROTEINS; HUMANS; NUTS; PEANUT HYPERSENSITIVITY; PLANT EXTRACTS; PLANT PROTEINS; RATS; SPECIES SPECIFICITY;

ARA; ARACHIS HYPOGAEA;

EID: 77649276125     PISSN: 16134125     EISSN: 16134133     Source Type: Journal    
DOI: 10.1002/mnfr.200900072     Document Type: Article

References (18)

1. European Union. Directive 2003/89/EC, 2003.
2. Hourihane, J. B., Kilburn, S. A., Nordlee, J. A., Hefle, S. L., et al., An evaluation of the sensitivity of subjects with peanut allergy to very low doses of peanut protein: a randomized, double-blind, placebo-controlled food challenge study. J. Allergy Clin. Immunol. 1997, 100, 596-600.
3. Dodo, H. W., Konan, K. N., Chen, F. C., Egnin, M., Viquez, O. M., Alleviating peanut allergy using genetic engineering: the silencing of the immunodominant allergen Ara h 2 leads to its significant reduction and a decrease in peanut allergenicity. Plant Biotechnol. J. 2008, 6, 135-145.
4. Maleki, S. J., Viquez, O., Jacks, T., Dodo, H. et al., The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function. J. Allergy Clin. Immunol. 2003, 112, 190-195.
5. Kleber-Janke, T., Crameri, R., Appenzeller, U., Schlaak, M., Becker, W. M., Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology. Int. Arch. Allergy Immunol. 1999, 119, 265-274.
6. Suhr, M., Wicklein, D., Lepp, U., Becker, W. M., Isolation and characterization of natural Ara h 6: evidence for a further peanut allergen with putative clinical relevance based on resistance to pepsin digestion and heat. Mol. Nutr. Food Res. 2004, 48, 390-399.
7. Boldt, A., Fortunato, D., Conti, A., Petersen, A. et al., Analysis of the composition of an immunoglobulin E reactive high molecular weight protein complex of peanut extract containing Ara h 1 and Ara h 3/4. Proteomics 2005, 5, 675-686.
8. Becker, W. M., in: Holgate S., Marone G., Ring J. (Eds.), Cellular and Molecular Targets in Allergy and Clinical Immunology, Hogrefe, Göttingen 2007, pp. 70-72.
9. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227,680-685.
10. Kyhse-Andersen, J., Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J. Biochem. Biophys. Methods 1984, 10, 203-209.
11. Blake, M. S., Johnston, K. H., Jones, G. J., Gotschlich, E. C., A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots. Anal. Biochem. 1984, 136, 175-179.
12. Hoffmann, A., Vieths, S., Haustein, D., Biologic allergen assay for in vivo test allergens with an in vitro model of the murine type I reaction. J. Allergy Clin. Immunol. 1997, 99, 227-232.
13. Beaven, M. A., Rogers, J., Moore, J. P., Hesketh, T. R. et al., The mechanism of the calcium signal and correlation with histamine release in 2H3 cells. J. Biol. Chem. 1984, 259, 7129-7136.
14. Schmidt, H., Gelhaus, C., Latendorf, T., Nebendahl, M. et al., 2D-DIGE analysis of the proteome of extracts from peanut variants reveals striking differences in major allergen contents. Proteomics 2009, 9, 3507-3521.
15. Nogueira, M. C., McDonald, R., Westphal, C., Maleki, S. J., Yeung, J. M., Can commercial peanut assay kits detect peanut allergens? J. AOAC Int. 2004, 87, 1480-1484.
16. Pomes, A., Helm, R. M., Bannon, G. A., Burks, A. W. et al., Monitoring peanut allergen in food products by measuring Ara h 1. J. Allergy Clin. Immunol. 2003, 111, 640-645.
17. Koppelman, S. J., Vlooswijk, R. A., Knippels, L. M., Hessing, M. et al., Quantification of major peanut allergens Ara h 1 and Ara h 2 in the peanut varieties Runner, Spanish, Virginia, and Valencia, bred in different parts of the world. Allergy 2001, 56, 132-137.
18. Hill, D. J., Hosking, C.S., The prevalence of allergens in foods and threshold levels for sensitization. Joint FAO/WHO Expert Consultation on Foods Derived from Biotechnology 2001, Topic 7, 1-11.