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The production of human serum albumin in transgenic Hevea brasiliensis

Arokiaraj P., Rueker Florian, Jaafar H., Bahri Shamsul, Yeang Hoong Yeet. 2001. The production of human serum albumin in transgenic Hevea brasiliensis. In : Biotechnology and rubber tree : Proceedings of IRRDB symposium, 25-28 September 2001, Montpellier, France. Sainte-Beuve Jérôme (ed.). IRRDB, CIRAD-CP-HEVEA. Montpellier : CIRAD IRRDB Symposium, Montpellier, France, 25 Septembre 2001/28 Septembre 2001.

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Résumé : One of the goals in the Hevea genetic transformation programme at the RRIM is the production of recombinant proteins in the latex of transgenic Hevea, so that it can be extracted continually and nondestructively by tapping the rubber tree. Gene transfer in Hevea has become routine, facilitated by Agrobacterium. Recombinant proteins produced from plants is one of the most exciting and fastest developing areas in biology. This aspect becomes increasingly important in cases where large amounts of protein need to be produced. Hevea trees with their large volume of latex production capability, and easy scale-up of transgenics through vegetative propagation could be the choice. As the transgenic Hevea system does not depend on repeated success with genetic transformation, clonal copies could be vegetatively propagated form high expressing transformants. From a commercial standpoint, transgenic rubber trees have the highest potential as a safe production system for heterologous proteins in bulk quantities. The probability of health risks because of contamination with potential human pathogens and toxins in recombinant products derived from Hevea in minimized. To explore the potential to produce commercially interesting proteins, we set out to express the 68 kDa protein human serum albumin (HSA) in transgenic Hevea. HSA is initially synthesised in human liver as prepro-albumin and released after cleavage of the aminoterminal prepeptide consisting of 18 amino acids from the endoplasmic reticulum. The proalbumin is processed further in the Golgi complex by the removal of the propeptide (6 residues) by a serine proteinase. The mature polypeptide (585 amino acids) is thus secreted.

Classification Agris : F30 - Génétique et amélioration des plantes

Auteurs et affiliations

  • Arokiaraj P., MRB (MYS)
  • Rueker Florian, Agricultural University of Vienna (AUT)
  • Jaafar H., MRB (MYS)
  • Bahri Shamsul, MRB (MYS)
  • Yeang Hoong Yeet, MRB (MYS)

Autres liens de la publication

Source : Cirad - Agritrop (https://agritrop.cirad.fr/513751/)

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