During infection of the urogenital tract, the parasite Trichomonas vaginalis is challenged by factors such as nutrient limitation, the host immune response and coexistence with other members of the microbial fauna. Thus establishment of trichomonad infection depends on multifactorial host-parasite interactions, that involve both contact-dependent mechanisms, such as adherence to vaginal epithelial cells, contact-dependent extracellular killing of host cells, and active phagocytosis of host cells and bacteria, as well as contact independent mechanisms that include secretion of soluble biologically active molecules. To get more insight into the secreted proteome of T. vaginalis we detected and quantified released proteins at consecutive time points. Out of 2072 detected proteins, 89 were estimated to significantly increase in time. These include leishmaniolysin-like metallopeptidases, cathepsin-like cystein peptidases and a number of proteins involved in sugar metabolism, most notably beta-amylases, which may be significant in utilization of host-cell derived glycogen. We further discovered a large group of secreted hypothetical proteins with predicted triple tyrosine domain that may facilitate interaction with the extracellular matrix of the host epithelium.