Bacteria in the oral cavity must interact with salivary proteins if they are to survive. Such interactions can take several forms, either providing nutrients, a means of adhesion to surfaces, or resulting in aggregation or killing and, therefore, clearance of organisms. Recent work has provided an insight into the mechanisms of some of these bacterial-protein interactions, revealing complexity and diversity. For example, the interaction between a putative Streptococcus mutans adhesin, P1 (B, I/II, etc.), and a parotid glycoprotein results in adhesion when it occurs at a surface or aggregation when in solution, and different domains of P1 appear to be involved in the two processes. An alternative strategy is employed by Actinomyces viscosus, which interacts, via its type-1 fimbriae, with a proline-rich salivary protein; however, this interaction occurs only when the PRP is adsorbed to a surface. A. viscosus takes advantage of a conformational change in the PRP when it becomes surface-bound, which exposes a cryptic part of the molecule. A third, and intriguing, type of interaction is seen between various streptococci and salivary amylase. This does not result in either adherence or aggregation but provides organisms with the ability to utilize starch breakdown products for metabolism. An understanding of the mechanisms involved in bacterial-protein interactions could conceivably lead to novel methods for controlling specific pathogens, but the systems operating in the mouth are numerous, complex, and diverse.