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. 2018 Jul 25;16(7):e05349. doi: 10.2903/j.efsa.2018.5349

Table 3.

Characteristics and intended effects of the events stacked in cotton GHB614 × T304‐40 × GHB119

Event Protein Donor organism and function Intended effects in GM plant
GHB614 2mEPSPS Based on a gene from Zea mays, 5‐enolpyruvyl‐shikimate‐3‐phosphate synthase (EPSPS) is an enzyme involved in the shikimic acid pathway for aromatic amino acid biosynthesis in plants and microorganisms (Lebrun et al., 2003) The amino acid sequence of the maize EPSPS enzyme was modified by two substitutions to render it tolerant to glyphosate. Expression of 2mEPSPS confers tolerance to glyphosate‐containing herbicides
T304‐40

Cry1Ab

PAT

Based on genes from Bacillus thuringiensis, subsp berliner 1715, Cry1Ab confers resistance to insect pests of the leptidopteran family; its insecticidal activity is attributed to the expression of crystal protein (cry) genes (Schnepf et al., 1998).

Based on the bar gene from Streptomyces hygroscopicus, Phosphinothricin‐acetyl‐transferase (PAT) enzyme confers resistance to the antibiotic bialaphos (Eckes et al., 1989)

Cotton T304‐40 expresses a chimeric, truncated cry1Ab gene. Cry1Ab is a chimeric protein toxic to certain lepidopteran larvae feeding on cotton.

Cotton T304‐40 expresses the PAT protein, which acetylates L‐glufosinate‐ammonium and thereby confers tolerance to glufosinate ammonium‐based herbicides

GHB119

Cry2Ae

PAT

Based on genes from Bacillus thuringiensis subsp. dakota 1715, Cry1Ae confers resistance to insect pests of the leptidopteran family; its insecticidal activity is attributed to the expression of crystal protein (cry) genes (Schnepf et al., 1998).

Based on the bar gene from Streptomyces hygroscopicus strain ATCC21705, Phosphinothricin‐acetyl‐transferase (PAT) enzyme confers resistance to the antibiotic bialaphos (Eckes et al., 1989)

Cotton GHB119 expresses a cry2Ae gene. Cry2Ae is a chimeric protein toxic to certain lepidopteran larvae feeding on cotton.

Cotton GHB119 expresses the PAT protein, which acetylates L‐glufosinate‐ammonium and thereby confers tolerance to glufosinate ammonium‐based herbicides