Genetically Engineered Tobacco Plants Produce Human Collagen

In either case, the process is time consuming and costly, and the end product is likely to contain viral or bacterial contaminants or even prions.

An advanced genetic engineering method for collagen production, which demands the coexpression of five separate genes, was originally published in the August 14, 2009, online edition of the journal Biomacromolecules. In this paper investigators at the Hebrew University of Jerusalem (Rehovoth, Israel) described how two human genes encoding recombinant heterotrimeric collagen type I (rhCOL1) were successfully coexpressed in tobacco plants with the human prolyl-4-hydroxylase (P4H) and lysyl hydroxylase 3 (LH3) enzymes, responsible for key posttranslational modifications of collagen. Plants coexpressing all five vacuole-targeted proteins generated intact procollagen yields of nearly 2% of the extracted total soluble proteins. Plant-extracted rhCOL1 formed thermally stable triple helical structures and demonstrated biofunctionality similar to human tissue-derived collagen supporting binding and proliferation of adult peripheral blood-derived endothelial progenitor-like cells.

For this groundbreaking work senior author Dr. Oded Shoseyov, professor of plant sciences at the Hebrew University of Jerusalem, was recently awarded the prestigious Kaye Innovation Award, presented to outstanding researchers who have developed innovative methods and inventions with good commercial potential that will benefit the university and society.

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Hebrew University of Jerusalem