Transgenic Expression of Bean -Amylase Inhibitor in Peas Results in Altered Structure and Immunogenicity
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- 作者：Vanessa E. Prescott ; Peter M. Campbell ; Andrew Moore ; Joerg Mattes ; Marc E. Rothenberg ; Paul S. Foster ; T. J. V. Higgins ; and Simon P. Hogan
- 刊名：Journal of Agricultural and Food Chemistry
- 出版年：2005
- 出版时间：November 16, 2005
- 年：2005
- 卷：53
- 期：23
- 页码：9023 - 9030
- 全文大小：450K
- 年卷期：v.53,no.23(November 16, 2005)
- ISSN：1520-5118
文摘
The development of modern gene technologies allows for the expression of recombinant proteins innon-native hosts. Diversity in translational and post-translational modification pathways betweenspecies could potentially lead to discrete changes in the molecular architecture of the expressedprotein and subsequent cellular function and antigenicity. Here, we show that transgenic expressionof a plant protein (
fchars/alpha.gif" BORDER=0>-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 astructurally modified form of this inhibitor. Employing models of inflammation, we demonstrated inmice that consumption of the modified fchars/alpha.gif" BORDER=0>AI and not the native form predisposed to antigen-specificCD4+ Th2-type inflammation. Furthermore, consumption of the modified fchars/alpha.gif" BORDER=0>AI concurrently with otherheterogeneous proteins promoted immunological cross priming, which then elicited specific immunoreactivity of these proteins. Thus, transgenic expression of non-native proteins in plants may lead tothe synthesis of structural variants possessing altered immunogenicity.Keywords: fchars/alpha.gif" BORDER=0>-Amylase inhibitor; transgenic plant; animal model; Th2 inflammation; mass spectrophotometry
fchars/alpha.gif" BORDER=0>-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 astructurally modified form of this inhibitor. Employing models of inflammation, we demonstrated inmice that consumption of the modified fchars/alpha.gif" BORDER=0>AI and not the native form predisposed to antigen-specificCD4+ Th2-type inflammation. Furthermore, consumption of the modified fchars/alpha.gif" BORDER=0>AI concurrently with otherheterogeneous proteins promoted immunological cross priming, which then elicited specific immunoreactivity of these proteins. Thus, transgenic expression of non-native proteins in plants may lead tothe synthesis of structural variants possessing altered immunogenicity.Keywords: fchars/alpha.gif" BORDER=0>-Amylase inhibitor; transgenic plant; animal model; Th2 inflammation; mass spectrophotometry