Proteolysis of the peanut allergen Ara h 1 by an endogenous aspartic protease

Copyright © 2015 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 96(2015) vom: 27. Nov., Seite 301-10
1. Verfasser: Wilson, Karl A (VerfasserIn)
Weitere Verfasser: Tan-Wilson, Anna
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2015
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. 7S globulin storage protein Allergen Ara h 1 Aspartic protease Germination Peanut Proteolysis mehr... Antigens, Plant Ara h 1 protein, Arachis hypogaea Glycoproteins Membrane Proteins Plant Proteins Aspartic Acid Proteases EC 3.4.-
Beschreibung
Zusammenfassung:Copyright © 2015 Elsevier Masson SAS. All rights reserved.
The 7S and 11S globulins of peanuts are subjected to proteolysis two days after seed imbibition, with Ara h 1 and the arachin acidic chains being among the first storage proteins to be mobilized. Proteolytic activity was greatest at pH 2.6-3 and is inhibited by pepstatin A, characteristic of an aspartic protease. This activity persists in seedling cotyledons up to at least 8 days after imbibition. In vitro proteolysis of Ara h 1 at pH 2.6 by extracts of cotyledons from seedlings harvested 24 h after seed imbibition generates newly appearing bands on SDS-PAGE. Partial sequences of Ara h 1 that were obtained through LC-MS/MS analysis of in-gel trypsin digests of those bands, combined with information on fragment size, suggest that proteolysis begins in the region that links the two cupin domains to produce two 33/34 kD fragments, each one encompassing an intact cupin domain. The later appearance of two 18 and 10/11 kD fragments can be explained by proteolysis within an exposed site in the cupin domains of each of the 33/34 kD fragments. The same or similar proteolytic activity was observed in developing seeds, but Ara h 1 remains intact through seed maturation. This is partly explained by the observation that acidification of the protein storage vacuoles, demonstrated by vacuolar accumulation of acridine orange that was dissipated by a membrane-permeable base, occurs only after germination. These findings suggest a method for use of the seed aspartic protease in reducing peanut allergy due to Ara h 1
Beschreibung:Date Completed 02.09.2016
Date Revised 30.09.2020
published: Print-Electronic
Citation Status MEDLINE
ISSN:1873-2690
DOI:10.1016/j.plaphy.2015.08.008