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J. Bacteriol., 01 1998, 52-58, Vol 180, No. 1
Copyright © 1998, American Society for Microbiology

The capsule and S-layer: two independent and yet compatible macromolecular structures in Bacillus anthracis [In Process Citation]

S Mesnage, E Tosi-Couture, P Gounon, M Mock and A Fouet
Toxines et Pathogenie Bacteriennes (CNRS URA 1858), Institut Pasteur, Paris, France.

Bacillus anthracis, the etiological agent of anthrax, is a gram- positive spore-forming bacterium. Fully virulent bacilli are toxinogenic and capsulated. Two abundant surface proteins, including the major antigen, are components of the B. anthracis surface layer (S- layer). The B. anthracis paracrystalline S-layer has previously only been found in noncapsulated vegetative cells. Here we report that the S- layer proteins are also synthesized under conditions where the poly- gamma-D-glutamic acid capsule is present. Structural and immunological analyses show that the capsule is exterior to and completely covers the S-layer proteins. Nevertheless, analysis of single and double S-layer protein mutants shows that the presence of these proteins is not required for normal capsulation of the bacilli. Similarly, the S-layer proteins assemble as a two-dimensional crystal, even in the presence of the capsule. Thus, both structures are compatible, and yet neither is required for the correct formation of the other.


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