Movatterモバイル変換

[0]ホーム
URL:

Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
Thehttps:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

NIH NLM Logo
Log inShow account info
Access keysNCBI HomepageMyNCBI HomepageMain ContentMain Navigation
pubmed logo
Advanced Clipboard
User Guide

Full text links

Public Library of Science full text link Public Library of Science Free PMC article
Full text links

Actions

Share

.2016 Jun 16;11(6):e0157849.
doi: 10.1371/journal.pone.0157849. eCollection 2016.

Boiling and Frying Peanuts Decreases Soluble Peanut (Arachis Hypogaea) Allergens Ara h 1 and Ara h 2 But Does Not Generate Hypoallergenic Peanuts

Affiliations

Boiling and Frying Peanuts Decreases Soluble Peanut (Arachis Hypogaea) Allergens Ara h 1 and Ara h 2 But Does Not Generate Hypoallergenic Peanuts

Sarah S Comstock et al. PLoS One..

Abstract

Peanut allergy continues to be a problem in most developed countries of the world. We sought a processing method that would alter allergenic peanut proteins, such that allergen recognition by IgE from allergic individuals would be significantly reduced or eliminated. Such a method would render accidental exposures to trace amounts of peanuts safer. A combination of boiling and frying decreased recovery of Ara h 1 and Ara h 2 at their expected MWs. In contrast, treatment with high pressures under varying temperatures had no effect on protein extraction profiles. Antibodies specific for Ara h 1, Ara h 2, and Ara h 6 bound proteins extracted from raw samples but not in boiled/fried samples. However, pre-incubation of serum with boiled/fried extract removed most raw peanut-reactive IgE from solution, including IgE directed to Ara h 1 and 2. Thus, this method of processing is unlikely to generate a peanut product tolerated by peanut allergic patients. Importantly, variability in individual patients' IgE repertoires may mean that some patients' IgE would bind fewer polypeptides in the sequentially processed seed.

PubMed Disclaimer

Conflict of interest statement

Competing Interests:The authors have desclared that no competing interests exist.

Figures

Fig 1
Fig 1. Comparison of chloroform/methanol defatted (df) and non-defatted (ndf), buffer D extracted raw and boiled/fried peanut samples.
50μg protein (as determined using the Bradford assay on extracts prior to centrifugation) was loaded per lane on a 14% reducing SDS-PAGE. Lane labeled “spun” was loaded with non-defatted samples that had been centrifuged for one minute at 15,000 rpm in a benchtop eppendorf centrifuge. Arrows indicate differentially detected proteins.
Fig 2
Fig 2. 12% reducing SDS-PAGE of all 38 defatted, buffer D extracted peanut extracts.
A raw peanut extract (Raw) from defatted peanut was included on each gel as an internal control. Lanes are labeled with extract number (Table 1). Each lane was loaded with 65μg of protein.
Fig 3
Fig 3. Dot blot of all 38 defatted, buffer D extracted peanut samples (1μg/dot).
(A) Dot blot layout. Samples were blotted with serum from an atopic (mold sensitive), non-food allergic patient with presumably no peanut-specific IgE (B) and a peanut allergic individual (C).
Fig 4
Fig 4. Immunoblots of defatted, buffer D extracted peanut samples (numbers match Table 1) blotted with serum from peanut allergic individuals.
Serum was from individuals with a broad IgE repertoire (A, B), individuals with a more limited IgE repertoire (C, D), or an atopic (mold sensitive), non-food allergic patient with presumably no peanut-specific IgE (E). Extracts were run on 14% SDS-PAGE, 50μg per lane, and transferred to 0.22μm NC before blotting.
Fig 5
Fig 5. Immunoblots of defatted, buffer D extracted peanut samples (numbers match Table 1) blotted with polyclonal galline anti-Ara antibodies.
A) anti-Ara h 1, B) anti-Ara h 2, C) anti-Ara h 6 and D) anti-Ara h 3. Extracts were run on 14% reducing SDS-PAGE, 50μg per lane, and transferred to 0.22μm NC before blotting.
Fig 6
Fig 6. Inhibition immunoblots.
A) Inhibition immunoblot of raw peanut (sample 38) with sera from peanut allergic individuals presorbed with boiled/fried peanut (sample 37). B) Inhibition immunoblot of boiled/fried peanut (sample 37) with sera from peanut allergic individuals presorbed with purified Ara h 2 protein (h2) or not presorbed (0). C) Inhibition immunoblot of raw peanut (sample 38) with sera 4 presorbed with purified Ara h 2 (5μg or 10μg) or Ara h 6 (5μg or 10μg). “P” indicates a sample was presorbed with pollen extract.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Burbank AJ, Sood P, Vickery BP, Wood RA (2016) Oral Immunotherapy for Food Allergy. Immunol Allergy Clin North Am 36: 55–69. 10.1016/j.iac.2015.08.007 - DOI - PubMed
    1. Du Toit G, Roberts G, Sayre PH, Bahnson HT, Radulovic S, Santos AF, et al. (2015) Randomized trial of peanut consumption in infants at risk for peanut allergy. N Engl J Med 372: 803–813. 10.1056/NEJMoa1414850 - DOI - PMC - PubMed
    1. Blom WM, Vlieg-Boerstra BJ, Kruizinga AG, van der Heide S, Houben GF, Dubois AE (2013) Threshold dose distributions for 5 major allergenic foods in children. J Allergy Clin Immunol 131: 172–179. 10.1016/j.jaci.2012.10.034 - DOI - PubMed
    1. Taylor SL, Baumert JL, Kruizinga AG, Remington BC, Crevel RW, Brooke-Taylor S, et al. (2014) Establishment of Reference Doses for residues of allergenic foods: report of the VITAL Expert Panel. Food Chem Toxicol 63: 9–17. 10.1016/j.fct.2013.10.032 - DOI - PubMed
    1. Burks AW, Williams LW, Helm RM, Connaughton C, Cockrell G, O'Brien T (1991) Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges. J Allergy Clin Immunol 88: 172–179. - PubMed

MeSH terms

Substances

Related information

Grants and funding

This research was partially supported by Masterfoods Inc. (SST). The remaining funding was provided by the University of California, Davis. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.

LinkOut - more resources

Full text links
Public Library of Science full text link Public Library of Science Free PMC article
Cite
Send To

NCBI Literature Resources

MeSHPMCBookshelfDisclaimer

The PubMed wordmark and PubMed logo are registered trademarks of the U.S. Department of Health and Human Services (HHS). Unauthorized use of these marks is strictly prohibited.

[8]ページ先頭
©2009-2025 Movatter.jp