Protein quality in bacterial inclusion bodies

Trends in Biotechnology
Salvador Ventura, Antonio Villaverde

Abstract

A common limitation of recombinant protein production in bacteria is the formation of insoluble protein aggregates known as inclusion bodies. The propensity of a given protein to aggregate is unpredictable, and the goal of a properly folded, soluble species has been pursued using four main approaches: modification of the protein sequence; increasing the availability of folding assistant proteins; increasing the performance of the translation machinery; and minimizing physicochemical conditions favoring conformational stress and aggregation. From a molecular point of view, inclusion bodies are considered to be formed by unspecific hydrophobic interactions between disorderly deposited polypeptides, and are observed as "molecular dust-balls" in productive cells. However, recent data suggest that these protein aggregates might be a reservoir of alternative conformational states, their formation being no less specific than the acquisition of the native-state structure.

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Citations

Feb 12, 2013·Nanomedicine·Joaquin Seras-FranzosoAntonio Villaverde
Feb 18, 2014·Molecular Biotechnology·Monika PodoliankaitėElena Servienė
Apr 2, 2010·Cellular and Molecular Life Sciences : CMLS·Raimon SabateSalvador Ventura
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