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Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens ‐mediated transient expression and in transgenic tobacco plant
Author(s) -
Merle C,
Perret S,
Lacour T,
Jonval V,
Hudaverdian S,
Garrone R,
Ruggiero F,
Theisen M
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02452-3
Subject(s) - recombinant dna , agrobacterium tumefaciens , transgene , genetically modified crops , chemistry , agrobacterium , enzyme , biochemistry , microbiology and biotechnology , biology , gene
Potential contamination of animal‐derived collagen with pathogens has led to the demand for safe recombinant sources of this complex molecule. In continuation of our previous work [Ruggiero et al. (2000) FEBS Lett. 469, 132–136], here we show that it is possible to produce recombinant hydroxylated homotrimeric collagen in tobacco plants that are co‐transformed with a human type I collagen and a chimeric proline‐4‐hydroxylase (P4H). This is to our knowledge the first time that transient expression in tobacco was used to improve the quality of a recombinant protein produced in plants through co‐expression with an animal cell‐derived modifying enzyme. We demonstrated the functionality of the new chimeric P4H and thus improved the thermal stability of recombinant collagen I from plants to 37°C.