The immunoglobulin (Ig) protein domain is widespread in nature having a well-recognized role in proteins of the immune system. In this review, we describe the proteins containing Ig-like domains in
Escherichia coli and entero-bacteria, reporting their structural and functional properties, protein folding, and diverse biological roles. In addition, we cover the expression of heterolo-gous Ig domains in E. coli owing to its biotechnological application for expression and selection of antibody fragments and full-length IgG molecules. Ig-like domains in E. coli and enterobacteria are frequently found in cell surface proteins and fimbrial organelles playing important functions during host cell
adhesion and invasion of pathogenic strains, being structural components of pilus and nonpilus fimbrial systems and members of the intimin/invasin family of outer membrane (OM) adhesins. Ig-like domains are also found in periplasmic chaperones and OM usher proteins assembling fimbriae, in oxidoreductases and hydrolytic enzymes, ATP-binding cassette transporters, sugar-binding and metal-resistance proteins. The folding of most E. coli Ig-like domains is
assisted by periplasmic chaperones, peptidyl
prolylcis/transisomerases and disulfide bond catalysts that also participate in the folding of antibodies expressed in this bacterium. The technologies for expression and selection of recombinant antibodies in
E. coli are described along with their biotechnological potential.This work has been supported by Grants of the Spanish Ministry of Science and Innovation (BIO2008-05201; BIO2011-26689), the Autonomous Community of Madrid
(S-BIO-236-2006; S2010-BMD-2312), CSIC (PIE 2011 20E049), ‘la Caixa’ Foundation, and the VI Framework Program from the European Union (FP6-LSHB-CT-2005-512061 NoE ‘EuroPathogenomics’).Peer reviewe
