Isolation of a thiol-dependent serine protease in peanut and investigation of its role in the complement and the allergic reaction

Publication date: July 2016
Source:Molecular Immunology, Volume 75
Author(s): Cédric Javaux, Patrick Stordeur, Mohamed Azarkan, Françoise Mascart, Danielle Baeyens-Volant
A serine protease activity was detected in aqueous peanuts seeds extracts, partially purified and characterized as a thiol-dependent serine protease. The potential role of this proteolytic activity on allergic reaction to peanuts was prospected through complement activation studies in human plasma and serum, and MDCK cells to investigate a possible occludin degradation in tight junctions. The peanut protease activity induced the production of anaphylatoxins C3a and C5a, and of the terminal membrane attack complex SC5b-9 whatever the complement activation pathway. The protease activity was also involved in the partial digestion of occludin within tight junctions, with for result, an increase of the epithelial permeability to antigen absorption.



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