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Bacterial spores spontaneously interact and tightly bind heterologous proteins. A variety of antigens and enzymes have been efficiently displayed on spores of  Bacillus subtilis , the model system for spore formers. Adsorption on  B. subtilis  spores has then been proposed as a non-recombinant approach for the development of mucosal vaccine/drug delivery vehicles, biocatalysts, bioremediation, and diagnostic tools. We used spores of  B. megaterium  QM B1551 to evaluate their efficiency as an adsorption platform. Spores of  B. megaterium  are significantly larger than those of  B. subtilis  and of other  Bacillus  species and are surrounded by the exosporium, an outermost surface layer present only in some  Bacillus  species and lacking in  B. subtilis.  Strain QM B1551 of  B. megaterium  and a derivative strain totally lacking the exosporium were used to localize the adsorbed monomeric Red Fluorescent Protein (mRFP) of the coral  Discosoma  sp., used as a model heterologous protein. Our results indicate that spores of  B. megaterium  adsorb mRFP more efficiently than  B. subtilis  spores, that the exosporium is essential for mRFP adsorption, and that most of the adsorbed mRFP molecules are not exposed on the spore surface but rather localized in the space between the outer coat and the exosporium.

The Exosporium of Bacillus megaterium QM B1551 Is Permeable to the Red Fluorescence Protein of the Coral Discosoma sp.