Web Release Date: October 15,
Transgenic Expression of Bean 
-Amylase Inhibitor in Peas
Results in Altered Structure and Immunogenicity
and
Division of Molecular Bioscience, The John Curtin School of Medical Research, Australian National University, Canberra, ACT, Australia, Division of Allergy and Immunology, Department of Pediatrics, Cincinnati Children's Hospital Medical Center, University of Cincinnati College of Medicine, Cincinnati, Ohio 45229, and Divisions of Entomology and Plant Industry, Commonwealth Scientific and Industrial Research Organization, Canberra, ACT, Australia
Received for review March 16, 2005. Revised manuscript received August 26, 2005. Accepted September 6, 2005. This work was supported in part by National Health Medical Research Council (Australia) Program Grant 224207.
Abstract:
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 (-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 AI and not the native form predisposed to antigen-specific
CD4+ Th2-type inflammation. Furthermore, consumption of the modified AI concurrently with other
heterogeneous proteins promoted immunological cross priming, which then elicited specific immunoreactivity of these proteins. Thus, transgenic expression of non-native proteins in plants may lead to
the synthesis of structural variants possessing altered immunogenicity.
Keywords: -Amylase inhibitor; transgenic plant; animal model; Th2 inflammation; mass spectrophotometry
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