The S-layer homology domain as a means for anchoring heterologous proteins on the cell surface of Bacillus anthracis.
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.
Mesnage
S
S
Unité Toxines et Pathogénie Bactériennes (CNRS URA 1858), Institut Pasteur, Paris, France. smesnage@pasteur.fr
Tosi-Couture
E
E
Mock
M
M
Fouet
A
A
D000818:Animals; D000942:Antigens, Bacterial / Q000096:biosynthesis / Q000235:genetics; D001408:Bacillus anthracis / Q000235:genetics / Q000378:metabolism*; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics* / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D051379:Mice; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism
D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins