AI Article Synopsis
- Bacillus subtilis coat assembly provides a useful model for studying biological structure self-assembly, with promising applications in nanobiotechnology.
- The morphology of B. subtilis spores was analyzed using advanced microscopy techniques, revealing prolate shapes measuring 0.6-3 micrometers in length and 0.5-2 micrometers in width, featuring surface bumps of 8 to 70 nm in diameter.
- Single molecule recognition force spectroscopy (SMRFS) showed that the spore coat protein CotA, which is found on the outer surface of the spores, has a binding force of about 55 pN when interacting with a specific polyclonal antibody.
Article Abstract
Coat assembly in Bacillus subtilis serves as a tractable model for the study of the self-assembly process of biological structures and has a significant potential for use in nano-biotechnological applications. In the present study, the morphology of B. subtilis spores was investigated by magnetically driven dynamic force microscopy (MAC mode atomic force microscopy) under physiological conditions. B. subtilis spores appeared as prolate structures, with a length of 0.6-3 microm and a width of about 0.5-2 microm. The spore surface was mainly covered with bump-like structures with diameters ranging from 8 to 70 nm. Besides topographical explorations, single molecule recognition force spectroscopy (SMRFS) was used to characterize the spore coat protein CotA. This protein was specifically recognized by a polyclonal antibody directed against CotA (anti-CotA), the antibody being covalently tethered to the AFM tip via a polyethylene glycol linker. The unbinding force between CotA and anti-CotA was determined as 55 +/- 2 pN. From the high-binding probability of more than 20% in force-distance cycles it is concluded that CotA locates in the outer surface of B. subtilis spores.
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