A variety of bioactive peptides and proteins have been successfully displayed on the surface of recombinant spores of Bacillus subtilis and other sporeformers. In most cases, spore display has been achieved by stably anchoring the foreign molecules to endogenous surface proteins or parts of them. Recombinant spores have been proposed for a large number of potential applications ranging from oral vaccine vehicles to bioremediation tools, and including biocatalysts, probiotics for animal or human use, as well as the generation and screening of mutagenesis libraries. In addition, a nonrecombinant approach has been recently developed to adsorb antigens and enzymes on the spore surface. This nonrecombinant approach appears particularly well suited for applications involving the delivery of active molecules to human or animal mucosal surfaces. Both the recombinant and nonrecombinant spore display systems have a number of advantages over cell- or phage-based systems. The stability, safety of spores of several bacterial species, and amenability to laboratory manipulations, together with the lack of some constraints limiting the use of other systems, make the spore a highly efficient platform to display heterologous proteins.