Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases.
J Sci Food Agric
; 90(10): 1702-8, 2010 Aug 15.
Article
in En
| MEDLINE
| ID: mdl-20564442
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. Hence 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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Arachis
/
Peptide Hydrolases
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Plant Proteins
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Allergens
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Glycoproteins
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Antigens, Plant
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2S Albumins, Plant
Language:
En
Journal:
J Sci Food Agric
Year:
2010
Type:
Article