Species-specific cell wall binding affinity of the S-layer proteins of mosquitocidal bacterium Bacillus sphaericus C3-41.

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 Microbiol

authors

Li J,Hu X,Yan J,Yuan Z

doi

10.1128/AEM.00356-09

subject

Has Abstract

pub_date

2009-06-01 00:00:00

pages

3891-5

issue

12

eissn

0099-2240

issn

1098-5336

pii

AEM.00356-09

journal_volume

75

pub_type

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