Résumés
Résumé
La production de protéines recombinantes est une biotechnologie qui entre dans une phase de maturité, entraînant ainsi un essor de la production industrielle. Cependant, le processus de conversion systématique de l'information génétique en protéine biologiquement active se heurte au problème fondamental du repliement cellulaire des protéines : de nombreuses protéines recombinantes ne sont pas produites dans leur état natif, et s'agrègent dans un état biologiquement inactif. Bien que ce phénomène d'agrégation présente certains avantages pratiques, la renaturation in vitro des protéines recombinantes, après solubilisation des agrégats cellulaires, revêt toujours un caractère empirique et aléatoire. Aussi est-il préférable d'intervenir en amont en optimisant les conditions d'expression de la protéine, afin de minimiser ce problème au sein des cellules. Dans ce domaine, l'alternative la plus prometteuse est certainement le développement des méthodes génétiques permettant le criblage à haut débit des protéines correctement repliées dans la cellule.
Summary
The biotechnology of recombinant protein production is now entering its most advanced stage, and the growth of indusrial protein pharmaceuticals provides solid proof of this evolution. However, the sytematic conversion of genetic information into a biologically active protein is constantly confronted by the fundamental problem of protein folding in cells, and many recombinant proteins are not produced in their native state. Instead, they aggregate into a biologically inactive state. Although this aggregation reaction has some pratical advantages, in vitro renaturation of recombinant proteins, after solubilization of cellular aggregates, is still an empiric and random process. Thus, it is better to control cellular expression conditions to minimize this problem inside the cells. The most attractive approach is certainly the development of high throughput genetic screens to monitor efficient protein folding.
Parties annexes
Références
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