Structure and biology of trimeric autotransporter adhesins

Abstract

Trimeric autotransporter adhesins (TAAs) are a family of secreted Gram-negative bacterial outer membrane (OM) proteins. These obligate homotrimeric proteins share a common molecular organisation, consisting of a N-terminal "passenger" domain followed by a C-terminal translocation unit/membrane anchor. All described TAAs act as adhesins. The passenger domain is responsible for specific adhesive and other activities of the protein and has a modular architecture. Its globular head domain(s), where ligands often bind, are projected away from the bacterial surface by an extended triple α-helical coiled coil stalk attached to the β-barrel anchor. The head domains appear to be constructed from a limited set of subdomains. The β-barrel anchor is the only part of the protein strictly conserved between family members. It appears that the extracellular export of the passenger does not require an external energy source or auxiliary proteins, though recent data indicate that an OM complex (the Bam complex) is involved in passenger domain secretion. The ability to bind to a variety of host molecules such as collagen, fibronectin, laminin or cell surface receptors via a structurally diverse elements suggests that TAAs have evolved a unique mechanism which closely links structure to folding and function.