BCS-GH811-4 - Herbicide-tolerant cotton | BCH-LMO-SCBD-113966 | Living Modified Organism | Biosafety Clearing-House

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Living Modified Organism (LMO)

Decisions on the LMO Risk Assessments  
last updated: 01 Dec 2022
Living Modified Organism identity
The image below identifies the LMO through its unique identifier, trade name and a link to this page of the BCH. Click on it to download a larger image on your computer. For help on how to use it go to the LMO quick-links page.
Herbicide-tolerant cotton
EN
GHB811
Yes
BCS-GH811-4
  • - Organization: Bayer CropScience () | BCH-CON-NZ-8329-1
    Organization:
    Bayer CropScience ()
    Phone:
    Fax:
    Email:
    Website:
Cotton (Gossypium hirsutum) modified to confer tolerance to herbicides  and glyphosate via Agrobacterium-mediated transformation. To confer resistance to isoxaflutole, the cotton expresses Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase (HPPD) W336, which contains a point mutation that confers reduced binding affinity to HPPD inhibitors. For tolerance to glyphosate, the cotton expresses the Zea mays double mutant 5-enol pyruvylshikimate-3-phosphate synthase, which has a reduced binding affinity to the herbicide. 
EN
The term “Recipient organism” refers to an organism (either already modified or non-modified) that was subjected to genetic modification, whereas “Parental organisms” refers to those that were involved in cross breeding or cell fusion.
Coker 312
EN
Characteristics of the modification process
pTSIH09
EN
  • Agrobacterium-mediated DNA transfer
Some of these genetic elements may be present as fragments or truncated forms. Please see notes below, where applicable.
  • BCH-GENE-SCBD-104647-3 Histone H4 gene Promoter | Arabidopsis thaliana (Thale cress, Mouse-ear cress, Arabidopsis, ARATH)
    Promoter
  • BCH-GENE-SCBD-46333-8 5-enolpyruvylshikimate-3-phosphate synthase | Zea mays (Maize, Corn, MAIZE)
    Protein coding sequence | Resistance to herbicides (Glyphosate)
  • BCH-GENE-SCBD-104648-2 Histone H3 Gene II intron 1 | Arabidopsis thaliana (Thale cress, Mouse-ear cress, Arabidopsis, ARATH)
    Intron
  • BCH-GENE-SCBD-101419-4 Optimized Transit Peptide
    Transit signal
  • BCH-GENE-SCBD-104646-4 Histone H4 gene 3' UTR | Arabidopsis thaliana (Thale cress, Mouse-ear cress, Arabidopsis, ARATH)
    Terminator
  • BCH-GENE-SCBD-101900-6 CsVMV promoter | Cassava vein mosaic virus (Cassava vein mosaic virus, CVMV, CsVMV)
    Promoter
  • BCH-GENE-SCBD-104793-3 4-hydroxyphenylpyruvate dioxygenase | Pseudomonas fluorescens (PSEFL)
    Protein coding sequence | Resistance to herbicides
The GHB811 genome contains two gene cassettes: Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase (hppd) and Zea mays 5-enolpyruvylshikimate-3-phosphate synthase (2mepsps).

The hppd coding sequence is under control of a Cassava vein mosaic virus promoter and Arabidopsis thaliana histone H4 terminator. A synthetic optimized (N-terminal) transit peptide was included to target the translated HPPD W336 protein to the chloroplast. High levels of expression are expected due to the nature of the viral promoter.

The 2mepsps coding sequence is under control of an A. thaliana histone H4 promoter and 3'untranslated region. An A. thaliana histone H3 intron was included to enhance the expression of 2mepsps and a synthetic optimized (N-terminal) transit peptide is also present to direct the protein to the chloroplasts.

Note:
  • Molecular characterization of the event indicated that a single copy of the T-DNA was inserted into the genome without the integration of vector backbone sequences.
  • The hppd sequence contains an amino acid substitution (glycine replacement for tryptophan) at position 336. The sequence was then codon-optimized for expression in plants.
  • The 2mepsps sequence contains two point mutations:  at position102 (substitution of threonine by isoleucine) and position 106 (substitution of proline by serine).
  • The optimized transit protein contains the sequence of the RuBisCO small subunit genes of Zea mays and Helianthus annuus with a tyrosine substitution at position 55 and cotton codon optimization. 
EN
LMO characteristics
EN
  • Feed
  • Food
Detection method(s)
EN
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