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Applied and Environmental Microbiology, June 2009, p. 3891-3895, Vol. 75, No. 12
0099-2240/09/$08.00+0 doi:10.1128/AEM.00356-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China,1 Graduate School of the Chinese Academy of Sciences, Beijing 100039, China2
Received 12 February 2009/ Accepted 21 April 2009
The binding affinities and specificities of six truncated S-layer homology domain (SLH) polypeptides of mosquitocidal Bacillus sphaericus strain C3-41 with the purified cell wall sacculi have been assayed. The results indicated that the SLH polypeptide comprised of amino acids 31 to 210 was responsible for anchoring the S-layer subunits to the rigid cell wall layer via a distinct type of secondary cell wall polymer and that a motif of the recombinant SLH polypeptide comprising amino acids 152 to 210 (rSLH152-210) was essential for the stable binding of the S-layer with the bacterial cell walls. The quantitative assays revealed that the KD (equilibrium dissociation constant) values of rSLH152-210 and rSLH31-210 with purified cell wall sacculi were 1.11 x 10–6 M and 1.40 x 10–6 M, respectively. The qualitative assays demonstrated that the SLH domain of strain C3-41 could bind only to the cell walls or the cells treated with 5 M guanidinium hydrochloride of both toxic and nontoxic B. sphaericus strains but not to those from other bacteria, indicating the species-specific binding of the SLH polypeptide of B. sphaericus with bacterial cell walls.
Published ahead of print on 24 April 2009.
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