Abstract:
: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 (rSLH(152-210)) was essential for the stable binding of the S-layer with the bacterial cell walls. The quantitative assays revealed that the K(D) (equilibrium dissociation constant) values of rSLH(152-210) and rSLH(31-210) 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.
journal_name
Appl Environ Microbioljournal_title
Applied and environmental microbiologyauthors
Li J,Hu X,Yan J,Yuan Zdoi
10.1128/AEM.00356-09subject
Has Abstractpub_date
2009-06-01 00:00:00pages
3891-5issue
12eissn
0099-2240issn
1098-5336pii
AEM.00356-09journal_volume
75pub_type
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