Section 18
Chapter 17,298

The S-layer homology domain as a means for anchoring heterologous proteins on the cell surface of Bacillus anthracis

Mesnage, S.; Tosi-Couture, E.; Mock, M.; Fouet, A.

Journal of Applied Microbiology 87(2): 256-260


ISSN/ISBN: 1364-5072
PMID: 10475961
DOI: 10.1046/j.1365-2672.1999.00880.x
Accession: 017297772

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Bacillus anthracis synthesizes two S-layer proteins, each containing three S-layer homology (SLH) motifs towards their amino-terminus. In vitro experiments suggested that the three motifs of each protein were organized as a structural domain sufficient to bind purified cell walls. Chimeric genes encoding the SLH domains fused to the levansucrase of Bacillus subtilis were constructed and integrated on the chromosome. Cell fractionation and electron microscopy studies showed that both heterologous polypeptides were targeted to the cell surface. In addition, surface-exposed levansucrase retained its enzymatic and antigenic properties. Preliminary results concerning applications of this work are presented.

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