Crystal structure of the transport unit of the autotransporter adhesin involved in diffuse adherence from Escherichia coli

Abstract

Several serious gastrointestinal diseases, which are widespread all over the world, are caused by enteropathogenic Escherichia coli. The monomeric autotransporter AIDA-I (adhesin involved in diffuse adherence) represents an important virulence factor of these strains and is involved in adhesion, biofilm formation, aggregation and invasion into host cells. Here, we present the crystal structure of the transport unit of AIDA-I at 3.0Å resolution, which forms a 12-stranded β-barrel harboring the linker domain in its pore. Mutagenesis studies of the C-terminal amino acid demonstrated the great impact of this terminal residue on membrane integration of AIDA-I and passenger translocation.

Keywords: AIDA-I; Autotransporter; Escherichia coli; Membrane proteins; Outer membrane (OM); Protein secretion; Protein structure; Structural biology; Type V secretion; X-ray crystallography.