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Phosphomannose Isomerase, a Novel Plant Selection System
Potential Allergenicity Assessment
Article first published online: 24 JAN 2006
DOI: 10.1111/j.1749-6632.2002.tb04138.x
Issue
1749-6632/asset/cover.gif?v=1&s=ab6276ce206ff2a11aab60a58914347cab6db545 "Annals of the New York Academy of Sciences")
Annals of the New York Academy of Sciences
Volume 964, GENETICALLY ENGINEERED FOODS: ASSESSING POTENTIAL ALLERGENICITY pages 129–138, May 2002
Additional Information
How to Cite
PRIVALLE, L. S. (2002), Phosphomannose Isomerase, a Novel Plant Selection System. Annals of the New York Academy of Sciences, 964: 129–138. doi: 10.1111/j.1749-6632.2002.tb04138.x
Publication History
- Issue published online: 24 JAN 2006
- Article first published online: 24 JAN 2006
- Abstract
- Article
- References
- Cited By
Keywords:
- allergenicity assessment;
- phosphomannose isomerase;
- transgenic plants;
- oral allergens
Abstract: Phosphomannose isomerase (PMI), an enzyme not present in many plants, catalyzes the reversible interconversion of mannose 6-phosphate and fructose 6-phosphate. Plant cells lacking this enzyme are incapable of surviving on synthetic medium containing mannose. Thus PMI/mannose selection has utility in the identification of transformed plant cells. As part of the safety assessment transgenic plants undergo before commercialization, PMI has been evaluated for its potential allergenicity. Purified PMI protein was readily digestible in a simulated gastric environment. PMI has no sequence homology to known allergens, does not contain multiple disulfide bonds, and has no N-glycosylation consensus sequences. No detectable changes in glycoprotein profiles were detected in PMI-transformed plants as compared to nontransgenic controls. These results indicate that PMI lacks many of the attributes associated with known oral allergens.