Detoxifying Escherichia coli for endotoxin-free production of recombinant proteins.

ABSTRACT:

Background

Lipopolysaccharide (LPS), also referred to as endotoxin, is the major constituent of the outer leaflet of the outer membrane of virtually all Gram-negative bacteria. The lipid A moiety, which anchors the LPS molecule to the outer membrane, acts as a potent agonist for Toll-like receptor 4/myeloid differentiation factor 2-mediated pro-inflammatory activity in mammals and, thus, represents the endotoxic principle of LPS. Recombinant proteins, commonly manufactured in Escherichia coli, are generally contaminated with endotoxin. Removal of bacterial endotoxin from recombinant therapeutic proteins is a challenging and expensive process that has been necessary to ensure the safety of the final product.

Results

As an alternative strategy for common endotoxin removal meth

SUBMITTER: Mamat U 

PROVIDER: S-EPMC4404585 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature