Triple helix assembly and processing of human collagen produced in transgenic tobacco plants

• Published in: FEBS letters Vol. 469; no. 1; pp. 132 - 136
• Main Authors: Ruggiero, F, Exposito, J.-Y, Bournat, P, Gruber, V, Perret, S, Comte, J, Olagnier, B, Garrone, R, Theisen, M
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 03-03-2000
• Subjects: Amino Acid Sequence; Circular Dichroism; Electrophoresis, Polyacrylamide Gel; Humans; Microscopy, Electron; Molecular Sequence Data; Nicotiana - genetics; Plants, Genetically Modified; Plants, Toxic; Procollagen - chemistry; Procollagen - genetics; Protein Conformation; Protein Denaturation; Protein Folding; Recombinant collagen; Recombinant Proteins - chemistry; Recombinant Proteins - ultrastructure; Transgenic plant; Triple helix assembly; Trypsin; Triple helix assembly; Recombinant collagen; Transgenic plant
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(00)01259-X

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.