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

Authorized Users Only
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
Funding / 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
[ Google Scholar ]
14
11
URI
https://cer.ihtm.bg.ac.rs/handle/123456789/709
Collections
  • Radovi istraživača / Researchers' publications
Institution/Community
IHTM
TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Dobrijevic, Dragana
AU  - Jadranin, Milka
AU  - Blanusa, Milan
AU  - Vukmirica, Jelena
AU  - Ćirković Veličković, Tanja
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/709
AB  - 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.
PB  - John Wiley & Sons Ltd, Chichester
T2  - Journal of the Science of Food and Agriculture
T1  - Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases
VL  - 90
IS  - 10
SP  - 1702
EP  - 1708
DO  - 10.1002/jsfa.4005
ER  - 
@article{
author = "Radosavljević, Jelena and Dobrijevic, Dragana and Jadranin, Milka and Blanusa, Milan and Vukmirica, Jelena and Ćirković Veličković, Tanja",
year = "2010",
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.",
publisher = "John Wiley & Sons Ltd, Chichester",
journal = "Journal of the Science of Food and Agriculture",
title = "Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases",
volume = "90",
number = "10",
pages = "1702-1708",
doi = "10.1002/jsfa.4005"
}
Radosavljević, J., Dobrijevic, D., Jadranin, M., Blanusa, M., Vukmirica, J.,& Ćirković Veličković, T.. (2010). Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases. in Journal of the Science of Food and Agriculture
John Wiley & Sons Ltd, Chichester., 90(10), 1702-1708.
https://doi.org/10.1002/jsfa.4005
Radosavljević J, Dobrijevic D, Jadranin M, Blanusa M, Vukmirica J, Ćirković Veličković T. Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases. in Journal of the Science of Food and Agriculture. 2010;90(10):1702-1708.
doi:10.1002/jsfa.4005 .
Radosavljević, Jelena, Dobrijevic, Dragana, Jadranin, Milka, Blanusa, Milan, Vukmirica, Jelena, Ćirković Veličković, Tanja, "Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases" in Journal of the Science of Food and Agriculture, 90, no. 10 (2010):1702-1708,
https://doi.org/10.1002/jsfa.4005 . .

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