Preferences help
enabled [disable] Abstract
Number of results
2004 | 53 | 2 | 201-206
Article title

Wykorzystanie roślin do wytwarzania biofarmaceutyków

Title variants
The production of biopharmaceuticals in plants
Languages of publication
Summary The use of plants for medicinal purposes dates back thousands years but genetic engineering of plants to produce desired biopharmaceuticals is much more recent. "Molecular farming" is the production of recombinant proteins in plants. It is intended to increase the power of agriculture to cultivate and harvest transgenic plants producing recombinant therapeutics. Molecular farming has the potential to provide diagnostic and therapeutic tools in both health care and the life science. In the past decade, plants have been actively considered as an important expression system and a number of recombinant proteins such as hepatitis B (HbsAg) or cholera toxin B were produced in this system. Plant expression system may be useful for producing pharmaceuticals, as large amount of protein can be produced at a relatively low cost. In addition, plants are capable of complex post-traslationalmodification as that in Eukaryota. Preliminary clinical trials using transgenic lettuce plants expressing hepatitis B virus surface antigen showed encouraging immune response in human volunteers, thus suggesting that humanmay be immunised orally against HBV with plants expressing the viral antigen. Plant - derived biopharmaceuticals are cheap to produce and store, easy to scale up for mass production and safer than those derived from animals. Positive sides as well as possible negative concerns connected with molecular farming are discussed in the article.
Physical description
  • IV Liceum Ogólnokształcące, Pomorska 16, 91-416 Łódź, Polska
  • ARNTZEN C. J., 1997. High-tech herbal medicine: plant-based vaccines. Nature Biotechnol. 15, 221-223.
  • CARTRAIN M., SALMON P. M., ROBINSON D. K., BUCKLAND B. C., 2000. Metabolic engineering and directed evolution for the production of pharmaceuticals. Curr. Opin. Biotechnol. 11, 209-214.
  • CRAMER C. L., WEISSENBORN D. L., OISHI K. K., GRABAU E. A., BENNETT S. P., GRABOWSKI G. A., RADIN D. N., 1996. Bioproduction of human enzymes in transgenic tobacco. Ann. NY Acad. Sci. 25, 62-71.
  • DANIEL H., STREATFIELD S. J., WYCOFF K., 2001. Medical molecular farming: production of antibodies, biopharmaceuticals and edible vaccines in plants. Trends Plant Sci. 6, 219-226.
  • DIERYCK W., PAGNIER J., POYART C., MARDEN M. C., GRUBER V., BOURNAT I., BAUDINO S., MEROT B., 1997. Human haemoglobin from transgenic tobacco. Nature 386, 29-30.
  • DORAN P. M., 2000. Foreign protein production in plant tissue cultures. Curr. Opin. Biotechnol. 11, 199-204.
  • FISCHER R., DROSSARD J., COMMANDEUR U., SCHILLBERG S., EMANS N., 1999a. Towards molecular farming in the future: moving from diagnostic protein and antibody production in microbes to plants. Biotechnol. Appl. Biochem. 30, 101-108.
  • FISCHER R. L., LIAO Y. C., HOFFMANN K., SCHILLBERG S., EMANS N., 1999b. Molecular farming of recombinant antibodies in plants. Biol. Chem. 380, 825-839.
  • GIDDINGS G., 2000. Transgenic plants as factories for biopharmauceuticals. Nat. Biotechnol. 18, 1151-1155.
  • GIDDINGS G., 2001. Transgenic plants as protein factories. Curr. Opin. Biotechnol. 12, 450-454.
  • HIATT A., CAFFERKEY R., BOWDISH K., 1989. Production of antibodies produced in plants. Nature 342, 76-78.
  • JORGENSEN R., SNYDER C., JONES J. D. G., 1987. T-DNA is organized predominantly in inverted repeat structures in plants transformed with Agrobacterium tumefaciens C58 derivatives. Mol. Gen. Genet. 207, 471-477.
  • KAPUSTA J., MODELSKA A., FIGLEROWICZ M., PNIEWSKI T., LETELLIER M., LISOWA O., YUSIBOV V., KOPROWSKI H., PŁUCIENNICZAK A., LEGOCKI A. B., 1999. A plant-derived edible vaccine against hepatitis B virus. FASEB J. 13, 1796-1799.
  • LARRICK J. W., YU L., CHEN J., JAISWAL S., WYCOFF K., 1998. Production of antibodies in transgenic plants. In vivo and in vitro production of mAbs. 7th Forum in Immunology.
  • MA J. K., HIKMAT B. Y., WYCOFF K., VINE N. D., WANG F., STABILA P., VAN DOLLEWEERD C., MOSTOW K., LEHNER T., 1998. Generation and assembly of secretory antibodies in plants. Science 268, 716-719.
  • MAGNUSON N. S., LINZMAIER P. M., REEVES R., AN G., HAYGLASS K., LEE J. M., 1998. Secretion of biologically active human interleukin-2 and interleukin-4 from genetically modified tobacco cells in suspension culture. Protein Expr. Purif. 13, 45-52.
  • MATSUMOTO S., IKURA K., UEDA M., SASAKI R., 1995. Characterization of human glycoprotein (erythroprotein) produced in cultured tobacco cells. Plant. Mol. Biol. 27, 1163-1172.
  • PERMENTER D. L., BOOTHE J.G., VAN ROOIJEN G. J., YEUNG E. C., MOLONEY M. M., 1995. Production of biologically active hirudin in plant seeds using oleosin partitioning. Plant Mol. Biol. 29, 1167-1180.
  • SIJMONS P. C., DEKKER B. M., SCHRAMMEIJER B., VERWOERD T. C., VAN DEN P. J., HOEKEMA A., 1990. Production of correctly processed human serum albumin in transgenic plants. Biotechnology 8, 217-221.
  • STAUB J. M., 2000. High-yield production of a human therapeutic protein in tobacco chloroplast. Nature Biotechnol. 18, 333-338.
  • STOGER E., 2000. Cereal crops as viable production and storage system for pharmaceutical scFv antibodies. Plant Mol. Biol. 42, 583-590.
  • TERASHIMA M., MURAI Y., KAWAMURA M., NAKANISHI S., STOLTZ T., CHEN L., DROHAN W., RODRIGUEZ R. L., KATOH S., 1999. Production of functional human alpha 1-antitripsin by plant cell culture. Appl. Microbiol. Biotechnolol. 52, 516-523.
  • WALMSLEY A., ARNTZEN C., 2000. Plants for delivery of edible vaccines. Curr. Opin. Biotechnol. 11, 126-129.
  • WASSENEGGER M., PELISSIER T., 1998. A model for RNA-mediated gene silencing in higher plants. Plant Mol. Biol. 37, 349-362.
  • ZIEGLER M., THOMAS S., DANNA K., 2000. Accumulation of a thermostable endo-1,4-b-D-glukose in the apoplast of Arabidopsis thaliana leaves. Mol. Breed. 6, 37-46.
Document Type
Publication order reference
YADDA identifier
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.