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Modified Organism
Potato modified to synthesise fusion spider silk fragment/ elastin protein
Record information and status
Record ID
100316
Status
Published
Date of creation
2009-07-21 08:21 UTC (german_bch@bvl.bund.de)
Date of last update
2013-05-07 19:59 UTC (dina.abdelhakim@cbd.int)
Date of publication
2013-05-07 19:59 UTC (dina.abdelhakim@cbd.int)

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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.

LMO name
Potato modified to synthesise fusion spider silk fragment/ elastin protein
Transformation event
7 lines: pCB301-Kan-So1-100xELP-31, -33, -37, -38, -39, -44 and -50
Developer(s)
Institut für Pflanzengenetik und Kulturpflanzenforschung
Corrensstrasse 3 
Gatersleben
Germany, 06466
Phone:+49 (0)39482 5-0
Fax:+49 (0) 39482 5139
Email:info@ipk-gatersleben.de
Url:IPK Gatersleben
Description
Potatoes pCB301-Kan-SO1-100xELP produce a fusion protein consisting of the repetitive part of the spider silk protein MaSPI and an artificial elastin which is mainly observed in tubers. Female golden silk orbweaver spiders Nephila clavipes incorporate MaSpI protein within the very strong and elastic silk of the main threads of the spider net which is of high industrial interest. The artificial elastin 100xELP has high similarity to human elastin and consists of oligomeric repeats of the pentapeptide Val-Pro-Gly-Xaa-Gly (Xaa - any amino acid but proline). 100xELP exhibits a good ability to be solved in aqueous solution depending on salt concentration and temperature. It can undergo an inverse transition, i.e. the protein is soluble in an aqueous solution below its transition temperature but insoluble above this critical value. This characteristic is delegated to its fusion partner SO1 resulting in easy isolation and purification of spider silk protein from the biomass of potato tubers.
Recipient Organism or Parental Organisms
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.
Solanum tuberosum - Potato, SOLTU
Related LMOs
Potato modified to synthesise fusion spider silk/ elastin protein
Production of medical or pharmaceutical compounds (human or animal) Resistance to antibiotics - Kanamycin Use in industrial applications
Characteristics of the transformation process
Vector
pCB301-Kan-SO1-100xELP (derivate of pCB301-Kan from pBIN19)
Techniques used for the modification
  • Agrobacterium-mediated DNA transfer
Genetic elements construct
 
CaMV 35S promoter
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LeB4 Signal peptide
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Synthetic spider silk protein coding sequence
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c-myc-tag
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Synthetic elastin-like protein
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KDEL ER retention signal
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CaMV 35S terminator
0.00 Kb
 
 
Nopaline Synthase Gene Promoter
0.00 Kb
 
 
Neomycin Phosphotransferase II
0.00 Kb
 
 
Nopaline Synthase Gene Terminator
0.00 Kb
 
Further details
Notes regarding the genetic elements introduced or modified in this LMO
The introduced recombinant DNA includes two gene cassettes.

First, the fusion protein consisting of the synthetic spider silk protein SO1 and the elastin-like protein 100xELP carries the signal peptide LeB4 for translocation to the endoplasmic reticulum (ER) at the N-terminus and the KDEL signal peptide for retention in the ER at the C-terminus. The expression of this construct is controlled by the CaMV 35S promoter and -terminator.  The coding sequence SO1 represents the repetitive part of the spider silk protein MaSpI; approx. 180 bp of the MaSpI gene was removed form the 3´-end. The c-myc tag serves as immunochemical evidence of the fusion protein in Western blot analyses using antibodies.

Second, a nptII gene cassette consisting of the nos promoter, the nptII gene and nos terminator serves as a selection marker system via aminoglycosid antibiotics.
LMO characteristics
Modified traits
  • Use in industrial applications
Common use(s)
  • Research

Records referencing this document (3)
IDDescription
3record(s) found
Country's Decision or any other Communication1 record
Modified Organism1 record
Risk Assessment1 record