Premium
Triple helix assembly and processing of human collagen produced in transgenic tobacco plants
Author(s) -
Ruggiero F,
Exposito J.-Y,
Bournat P,
Gruber V,
Perret S,
Comte J,
Olagnier B,
Garrone R,
Theisen M
Publication year - 2000
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(00)01259-x
Subject(s) - recombinant dna , triple helix , transgene , complementary dna , procollagen peptidase , genetically modified crops , chemistry , biochemistry , helix (gastropod) , collagen helix , microbiology and biotechnology , biology , gene , stereochemistry , ecology , snail
The use of tobacco plants as a novel expression system for the production of human homotrimeric collagen I is presented in this report. Constructs were engineered from cDNA encoding the human proα1(I) chain to generate transgenic tobacco plants expressing collagen I. The recombinant proα1(I) chains were expressed as disulfide‐bonded trimers and were shown to fold into a stable homotrimeric triple helix. Moreover, the recombinant procollagen was subsequently processed to collagen as it occurs in animals. Large amounts of recombinant collagen were purified from field grown plant material. The data suggest that plants are a valuable alternative for the recombinant production of collagen for various medical and scientific purposes.