Immunogenicity of therapeutic proteins: influence of aggregation

KD Ratanji, JP Derrick, RJ Dearman… - Journal of …, 2014 - Taylor & Francis
The elicitation of anti-drug antibodies (ADA) against biotherapeutics can have detrimental
effects on drug safety, efficacy, and pharmacokinetics. The immunogenicity of …

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 …

Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins

E García-Fruitós, N González-Montalbán, M Morell… - Microbial cell …, 2005 - Springer
Background Many enzymes of industrial interest are not in the market since they are bio-
produced as bacterial inclusion bodies, believed to be biologically inert aggregates of …

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 …

Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli

A de Marco, E Deuerling, A Mogk, T Tomoyasu… - BMC …, 2007 - Springer
Background The overproduction of recombinant proteins in host cells often leads to their
misfolding and aggregation. Previous attempts to increase the solubility of recombinant …

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 …

To fuse or not to fuse: what is your purpose?

MR Bell, MJ Engleka, A Malik, JE Strickler - Protein Science, 2013 - Wiley Online Library
Since the dawn of time, or at least the dawn of recombinant DNA technology (which for many
of today's scientists is the same thing), investigators have been cloning and expressing …

[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 …

[HTML][HTML] Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid-or benzyl alcohol–overexpressed molecular chaperones

A De Marco, L Vigh, S Diamant… - Cell stress & …, 2005 - ncbi.nlm.nih.gov
When massively expressed in bacteria, recombinant proteins often tend to misfold and
accumulate as soluble and insoluble nonfunctional aggregates. A general strategy to …

Simplified screening for the detection of soluble fusion constructs expressed in E. coli using a modular set of vectors

A Dümmler, AM Lawrence, A De Marco - Microbial cell factories, 2005 - Springer
Background The solubility of recombinant proteins expressed in bacteria is often
disappointingly low. Several strategies have been developed to improve the yield and one …