Trimeric autotransporter adhesins (TAAs) are located on the surface of many pathogenic Gram-negative bacteria. TAAs belong to the autotransporter protein family and consist of three identical monomers. These obligate homotrimeric proteins are secreted through the bacterial type Vc secretion system and share a common molecular organization that each monomer consists of a N-terminal "passenger" domain and a C-terminal translocation domain. TAAs are important virulence factors that are involved in bacterial life cycle and participate in mediating infection, invasion, dissemination and evasion of host immune responses. TAAs have also proved to be useful for many applications, such as vaccines and disease biomarkers. We here mainly focused on new findings on bio-function and application of TAAs in addition to their common structure and secretion mechanisms.