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Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases

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2010
Authors
Radosavljević, Jelena
Dobrijevic, Dragana
Jadranin, Milka
Blanusa, Milan
Vukmirica, Jelena
Ćirković Veličković, Tanja
Article (Published version)
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Abstract
BACKGROUND: The major peanut allergens are Ara h 1, Ara h 2 and Ara h 6. Proteolytic processing has been shown to be required for the maturation process of Ara h 6. The aim of this study was to examine whether Ara h 2 undergoes proteolytic processing and, if so, whether proteolytic processing influences its ability to bind human immunoglobulin E (IgE). RESULTS: Ara h 2 isolated from peanut extract under conditions of protease inhibition revealed a single additional peak for its two known isoforms (Ara h 2.01 and Ara h 2.02), corresponding to a C-terminally truncated form lacking a dipeptide (RY). Ara h 2 isolated in the absence of protease inhibition, however, yielded two additional peaks, identified as C-terminally truncated forms lacking either a dipeptide (RY) or a single tyrosine residue. The IgE-binding capacity of the Ara h 2 truncated forms was not altered. CONCLUSION: Ara h 2 undergoes proteolytic processing by peanut proteases that involves C-terminal removal of a dipeptide. H...ence Ara h 2 isolated from peanut extract is a complex mixture of two isoforms expressed by different genes, Ara h 2.01 and Ara h 2.02, as well as truncated forms generated by the proteolytic processing of these isoforms.

Keywords:
Ara h 2 / Ara h 6 / proteolysis / IgE binding / food allergy
Source:
Journal of the Science of Food and Agriculture, 2010, 90, 10, 1702-1708
Publisher:
  • John Wiley & Sons Ltd, Chichester
Projects:
  • Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima (RS-142020)

DOI: 10.1002/jsfa.4005

ISSN: 0022-5142

PubMed: 20564442

WoS: 000280121600018

Scopus: 2-s2.0-77954404613
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URI
http://cer.ihtm.bg.ac.rs/handle/123456789/709
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IHTM

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