Protein folding and conformational stress in microbial cells producing recombinant proteins: A host comparative overview

Brigitte Gasser, Markku Saloheimo, Ursula Rinas, Martin Dragosits, Escarlata Rodríguez-Carmona, Kristin Baumann, Maria Giuliani, Ermenegilda Parrilli, Paola Branduardi, Christine Lang, Danilo Porro, Pau Ferrer, Maria Tutino, Diethard Mattanovich, Antonio Villaverde

Research output: Contribution to journalReview articleResearchpeer-review

219 Citations (Scopus)

Abstract

Different species of microorganisms including yeasts, filamentous fungi and bacteria have been used in the past 25 years for the controlled production of foreign proteins of scientific, pharmacological or industrial interest. A major obstacle for protein production processes and a limit to overall success has been the abundance of misfolded polypeptides, which fail to reach their native conformation. The presence of misfolded or folding-reluctant protein species causes considerable stress in host cells. The characterization of such adverse conditions and the elicited cell responses have permitted to better understand the physiology and molecular biology of conformational stress. Therefore, microbial cell factories for recombinant protein production are depicted here as a source of knowledge that has considerably helped to picture the extremely rich landscape of in vivo protein folding, and the main cellular players of this complex process are described for the most important cell factories used for biotechnological purposes. © 2008 Gasser et al; licensee BioMed Central Ltd.
Original languageEnglish
Article number11
Pages (from-to)11-
JournalMicrobial Cell Factories
Volume7
DOIs
Publication statusPublished - 4 Apr 2008

Fingerprint

Dive into the research topics of 'Protein folding and conformational stress in microbial cells producing recombinant proteins: A host comparative overview'. Together they form a unique fingerprint.

Cite this