The goal of this study was to characterize salivary components of titanium pellicles and to determine how experimental pellicles affect adhesion of several strains of streptococci to titanium surfaces. Titanium experimental pellicles were formed by incubation of fresh human parotid or human submandibular-sublingual saliva on pure titanium beads. Pellicle was recovered from the beads using sodium dodecyl sulfate buffer and was subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting to identify adsorbed salivary components. Streptococcus anginosus, S. oralis, and S. salivarius recovered from in vivo titanium plaque and five reference strains of streptococci were used in adhesion assays to titanium beads with and without experimental salivary pellicles. The experimental pellicle formed on titanium was found to be composed of selected proteins from human parotid and human submandibular-sublingual saliva. Salivary alpha-amylase and proline-rich proteins were found in all experimental pellicles, while sIgA, high-molecular weight mucin, and proline-rich glycoproteins were detected in one of the experimental pellicles examined. Adhesion of fresh isolates and reference stains of S. anginosus, S. oralis, and S. salivarius to saliva-coated titanium was reduced compared to that of titanium without saliva coating. However, adhesion of laboratory strains of S. gordonii and S. sanguis was found to be significantly greater to experimental pellicles of human submandibular-sublingual saliva than was the adhesion of the fresh isolates, suggesting that streptococci-colonizing implant surfaces may be inherently less adhesive than other bacterial strains. This study found that salivary pellicles are selectively formed on titanium and mediate in vitro adhesion of streptococci.