Production of bioactive, post-translationally modified, heterotrimeric, human recombinant type-I collagen in transgenic tobacco

Hanan Stein, Michal Wilensky, Yehuda Tsafrir, Michal Rosenthal, Rachel Amir, Tal Avraham, Keren Ofir, Or Dgany, Avner Yayon, Oded Shoseyov*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

115 Scopus citations

Abstract

Collagen's biocompatibility, biodegradability and low immunogenicity render it advantageous for extensive application in pharmaceutical or biotechnological disciplines. However, typical collagen extraction from animal or cadaver sources harbors risks including allergenicity and potential sample contamination with pathogens. In this work, 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 ∼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. Through a simple, safe and scalable method of rhCOL1 production and purification from tobacco plants, this work broadens the potential applications of human recombinant collagen in regenerative medicine.

Original languageAmerican English
Pages (from-to)2640-2645
Number of pages6
JournalBiomacromolecules
Volume10
Issue number9
DOIs
StatePublished - 14 Sep 2009

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