Recognition and invasion of host cells is a key step in the life-cycle of all apicomplexan parasites. The thrombospondin-related anonymous protein (TRAP) of Plasmodium sporozoites is directly involved in both processes and shares conserved adhesive domains with micronemal transmembrane proteins of other apicomplexans. Here, we report the cloning and characterization of a Babesia bovis TRAP homologue (BbTRAP). It was predicted to be a type 1 transmembrane protein containing a von Willebrand Factor A domain (vWFA), a thrombospondin type 1 domain (TSP1), a conserved transmembrane region and a conserved cytoplasmic C-terminus, thus resembling the domain arrangement of Plasmodium TRAP. In contrast to Plasmodium TRAP, BbTRAP was shown to be present during the asexual erythrocytic cycle, being located mainly at the apical side of merozoites. Polyclonal rabbit antisera directed against synthetic peptides derived from the TSP1 domain or the C-terminal end of the ectodomain were shown to inhibit erythrocyte invasion in vitro. Both antisera recognized a 75 kDa protein in merozoite extracts as well as in a protein fraction that was secreted into the extracellular milieu during in vitro invasion of erythrocytes.