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The S‐layer homology domain as a means for anchoring heterologous proteins on the cell surface of Bacillus anthracis
Author(s) -
Mesnage S.,
TosiCouture E.,
Mock M.,
Fouet A.
Publication year - 1999
Publication title -
journal of applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 1364-5072
DOI - 10.1046/j.1365-2672.1999.00880.x
Subject(s) - bacillus anthracis , heterologous , homology (biology) , anchoring , sequence homology , biology , s layer , microbiology and biotechnology , bacillaceae , genetics , peptide sequence , bacteria , bacillus subtilis , gene , structural engineering , engineering
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.