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Phosphomannose Isomerase, a Novel Plant Selection System
Author(s) -
PRIVALLE LAURA S.
Publication year - 2002
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2002.tb04138.x
Subject(s) - mannose , isomerase , biochemistry , glycoprotein , glycosylation , enzyme , chemistry , transgene , biology , gene
A bstract : 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.