Protein quality in bacterial inclusion bodies

S Ventura, A Villaverde - TRENDS in Biotechnology, 2006 - cell.com
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 …

Polyionic tags as enhancers of protein solubility in recombinant protein expression

V Paraskevopoulou, FH Falcone - Microorganisms, 2018 - mdpi.com
Since the introduction of recombinant protein expression in the second half of the 1970s, the
growth of the biopharmaceutical field has been rapid and protein therapeutics has come to …

The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures

A Vera, N González‐Montalbán, A Arís… - Biotechnology and …, 2007 - Wiley Online Library
Protein aggregation is a major bottleneck during the bacterial production of recombinant
proteins. In general, the induction of gene expression at sub‐optimal growth temperatures …

Bacterial inclusion bodies are industrially exploitable amyloids

A De Marco, N Ferrer-Miralles… - FEMS microbiology …, 2019 - academic.oup.com
Understanding the structure, functionalities and biology of functional amyloids is an issue of
emerging interest. Inclusion bodies, namely protein clusters formed in recombinant bacteria …

[HTML][HTML] Effect of temperature on protein quality in bacterial inclusion bodies

NS de Groot, S Ventura - FEBS letters, 2006 - Elsevier
Increasing evidence indicates that protein aggregation in bacteria does not necessarily
imply loss of biological activity. Here, we have investigated the effect of growth-temperature …

Engineering inclusion bodies for non denaturing extraction of functional proteins

Š Peternel, J Grdadolnik, V Gaberc-Porekar… - Microbial cell …, 2008 - Springer
Background For a long time IBs were considered to be inactive deposits of accumulated
target proteins. In our previous studies, we discovered IBs containing a high percentage of …

Analysis of type I and IV collagens by FT-IR spectroscopy and imaging for a molecular investigation of skeletal muscle connective tissue

C Petibois, G Gouspillou, K Wehbe, JP Delage… - Analytical and …, 2006 - Springer
Many muscular diseases result from abnormal organization of connective tissue and/or
collagen network formation. Only a few molecular imaging techniques are able to analyze …

Active protein aggregates induced by terminally attached self-assembling peptide ELK16 in Escherichia coli

W Wu, L Xing, B Zhou, Z Lin - Microbial cell factories, 2011 - Springer
Background In recent years, it has been gradually realized that bacterial inclusion bodies
(IBs) could be biologically active. In particular, several proteins including green fluorescent …

[HTML][HTML] Inclusion bodies: specificity in their aggregation process and amyloid-like structure

M Morell, R Bravo, A Espargaró, X Sisquella… - … et Biophysica Acta (BBA …, 2008 - Elsevier
The accumulation of aggregated protein in the cell is associated with the pathology of many
diseases and constitutes a major concern in protein production. Intracellular aggregates …

In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study

D Ami, F Lavatelli, P Rognoni, G Palladini… - Scientific Reports, 2016 - nature.com
Light chain (AL) amyloidosis, caused by deposition of amyloidogenic immunoglobulin light
chains (LCs), is the most common systemic form in industrialized countries. Still open …