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transgenic glphosate resistance protein predicted to be allergen



The article below found that a glyphosate resistance transgene from rr ready
crops was a likely allergen. IgE is the family of proteins from the immune
system that activates the allergy response. Further clinical testing is
recommended and the finding certainly refutes the claim the rr ready crops are substantially equivalent. Such findings should have triggered a moratorium on growth and sale of the rr crops but incompetent bureaucrats are waiting for a
body count.

Screening of transgenic proteins expressed in transgenic food crops for the
presence of short amino acid sequences identical to potential, IgE – binding
linear epitopes of allergens
Gijs A Kleter  and Ad ACM Peijnenburg
BMC Structural Biology 2002 2:8 (published 12 December 2002)

Abstract
Background
Transgenic proteins expressed by genetically modified food crops are evaluated
for their potential allergenicity prior to marketing, among others by
identification of short identical amino acid sequences that occur both in the transgenic protein and allergenic proteins. A strategy is proposed, in which the positive outcomes of the sequence comparison with a minimal length of six
amino acids are further screened for the presence of potential linear IgE-
epitopes. This double track approach involves the use of literature data on IgE-
epitopes and an antigenicity prediction algorithm.
Results
Thirty-three transgenic proteins have been screened for identities of at least
six contiguous amino acids shared with allergenic proteins. Twenty-two
transgenic proteins showed positive results of six- or seven- contiguous amino acids length. Only a limited number of identical stretches shared by transgenic proteins (papaya ringspot virus coat protein, acetolactate synthase GH50, and glyphosate oxidoreductase) and allergenic proteins could be identified as (part
of) potential linear epitopes.
Conclusion
Many transgenic proteins have identical stretches of six or seven amino acids in common with allergenic proteins. Most identical stretches are likely to be
false positives. As shown in this study, identical stretches can be further
screened for relevance by comparison with linear IgE-binding epitopes described
in literature. In the absence of literature data on epitopes, antigenicity
prediction by computer aids to select potential antibody binding sites that
will need verification of IgE binding by sera binding tests. Finally, the
positive outcomes of this approach warrant further clinical testing for
potential allergenicity.

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