Escherichia coli strains are responsible for many cases of gastrointestinal disease and represent a serious health problem worldwide. An essential step in the pathogenesis of such strains involves recognition and attachment to host intestinal surfaces. TibA is a potent bacterial adhesin associated with a number of enterotoxigenic E. coli strains and mediates bacterial attachment to a variety of human cells; additionally, it promotes invasion of such cells. This adhesin is a surface-displayed autotransporter protein and belongs to the exclusive group of bacterial glycoproteins; only the glycosylated form confers binding to and invasion of mammalian cells. Here we characterized TibA and showed that it possesses self-association characteristics and can mediate autoaggregation of E. coli cells. We demonstrated that intercellular TibA-TibA interaction is responsible for bacterial autoaggregation. Also, TibA expression significantly enhances biofilm formation by E. coli on abiotic surfaces.