Transgenic Expression of Bean alpha-Amylase Inhibitor in Peas Results in Altered Structure and Immunogenicity

摘要

The development of modern gene technologies allows for the expression of recombinant proteins in non-native hosts.Diversity in translational and post-translational modification pathways between species could potentially lead to discrete changes in the molecular architecture of the expressed protein and subsequent cellular function and antigenicity.Here,we show that transgenic expression of a plant protein(alpha-amylase inhibitor-1 from the common bean(Phaseolus vulgaris L.cv.Tendergreen))in a non-native host(transgenic pea(Pisum sativum L.))led to the synthesis of a structurally modified form of this inhibitor.Employing models of inflammation,we demonstrated in mice that consumption of the modified alphaAl and not the native form predisposed to antigen-specific CD4~+ Th_2-type inflammation.Furthermore,consumption of the modified alphaAlconcurrently with other heterogeneous proteins promoted immunological cross priming,which then elicited specific immuno-reactivity of these proteins.Thus,transgenic expression of non-native proteins in plants may lead to the synthesis of structural variants possessing altered immunogenicity.