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Two Putative Polysaccharide Deacetylases Are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus anthracis

Authors :
Waldemar Vollmer
Elias Eliopoulos
Sofia Arnaouteli
Petros Giastas
Christine Aldridge
Vassilis Bouriotis
Socrates J. Tzartos
Athina Andreou
Mary Tzanodaskalaki
Source :
The Journal of Biological Chemistry
Publication Year :
2015

Abstract

Background: BA0330 and BA0331 are the only two lipoproteins among 11 known or putative polysaccharide deacetylases from Bacillus anthracis. Results: Both proteins lack deacetylase activity and are important for cell shape maintenance (BA0331) or high salt stress adaptation of the bacterium (BA0330). Conclusion: BA0330 and BA0331 stabilize the cell wall of B. anthracis. Significance: Understanding the mechanisms by which lipoproteins maintain cell wall integrity.<br />Membrane-anchored lipoproteins have a broad range of functions and play key roles in several cellular processes in Gram-positive bacteria. BA0330 and BA0331 are the only lipoproteins among the 11 known or putative polysaccharide deacetylases of Bacillus anthracis. We found that both lipoproteins exhibit unique characteristics. BA0330 and BA0331 interact with peptidoglycan, and BA0330 is important for the adaptation of the bacterium to grow in the presence of a high concentration of salt, whereas BA0331 contributes to the maintenance of a uniform cell shape. They appear not to alter the peptidoglycan structure and do not contribute to lysozyme resistance. The high resolution x-ray structure of BA0330 revealed a C-terminal domain with the typical fold of a carbohydrate esterase 4 and an N-terminal domain unique for this family, composed of a two-layered (4 + 3) β-sandwich with structural similarity to fibronectin type 3 domains. Our data suggest that BA0330 and BA0331 have a structural role in stabilizing the cell wall of B. anthracis.

Details

ISSN :
1083351X
Volume :
290
Issue :
21
Database :
OpenAIRE
Journal :
The Journal of biological chemistry
Accession number :
edsair.doi.dedup.....975500c48ee4cfce3a9bf3bcfcc7d18b