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Phosphomannose Isomerase, a Novel Plant Selection System

Potential Allergenicity Assessment

Authors

  • LAURA S. PRIVALLE

    Corresponding author
    1. Syngenta Seeds, Inc., Research Triangle Park, North Carolina 27705, USA
      Address for correspondence: Dr. Laura S. Privalle, Senior Manager, Regulatory Science, Syngenta Seeds, Inc., P.O. Box 12257, 3054 Cornwallis Road, Research Triangle Park, NC 27705. Voice: 919-541-8594; fax: 919-541-8585; Laura.privalle@syngenta.com.
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Address for correspondence: Dr. Laura S. Privalle, Senior Manager, Regulatory Science, Syngenta Seeds, Inc., P.O. Box 12257, 3054 Cornwallis Road, Research Triangle Park, NC 27705. Voice: 919-541-8594; fax: 919-541-8585; Laura.privalle@syngenta.com.

Abstract

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.

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