YwdL in Bacillus cereus: its role in germination and exosporium structure.

In members of the Bacillus cereus group the outermost layer of the spore is the exosporium, which interacts with hosts and the environment. Efforts have been made to identify proteins of the exosporium but only a few have so far been characterised and their role in determining spore architecture and...

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Main Authors: Cassandra Terry, Andrew Shepherd, David S Radford, Anne Moir, Per A Bullough
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2011-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3161080?pdf=render
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spelling doaj-0fe75b4391204a3287185554b1002a1f2020-11-25T01:52:51ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-0168e2380110.1371/journal.pone.0023801YwdL in Bacillus cereus: its role in germination and exosporium structure.Cassandra TerryAndrew ShepherdDavid S RadfordAnne MoirPer A BulloughIn members of the Bacillus cereus group the outermost layer of the spore is the exosporium, which interacts with hosts and the environment. Efforts have been made to identify proteins of the exosporium but only a few have so far been characterised and their role in determining spore architecture and spore function is still poorly understood. We have characterised the exosporium protein, YwdL. ΔywdL spores have a more fragile exosporium, subject to damage on repeated freeze-thawing, although there is no evidence of altered resistance properties, and coats appear intact. Immunogold labelling and Western blotting with anti-YwdL antibodies identified YwdL to be located exclusively on the inner surface of the exosporium of B. cereus and B. thuringiensis. We conclude that YwdL is important for formation of a robust exosporium but is not required to maintain the crystalline assembly within the basal layer or for attachment of the hairy nap structure. ΔywdL spores are unable to germinate in response to CaDPA, and have altered germination properties, a phenotype that confirms the expected defect in localization of the cortex lytic enzyme CwlJ in the coat.http://europepmc.org/articles/PMC3161080?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Cassandra Terry
Andrew Shepherd
David S Radford
Anne Moir
Per A Bullough
spellingShingle Cassandra Terry
Andrew Shepherd
David S Radford
Anne Moir
Per A Bullough
YwdL in Bacillus cereus: its role in germination and exosporium structure.
PLoS ONE
author_facet Cassandra Terry
Andrew Shepherd
David S Radford
Anne Moir
Per A Bullough
author_sort Cassandra Terry
title YwdL in Bacillus cereus: its role in germination and exosporium structure.
title_short YwdL in Bacillus cereus: its role in germination and exosporium structure.
title_full YwdL in Bacillus cereus: its role in germination and exosporium structure.
title_fullStr YwdL in Bacillus cereus: its role in germination and exosporium structure.
title_full_unstemmed YwdL in Bacillus cereus: its role in germination and exosporium structure.
title_sort ywdl in bacillus cereus: its role in germination and exosporium structure.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2011-01-01
description In members of the Bacillus cereus group the outermost layer of the spore is the exosporium, which interacts with hosts and the environment. Efforts have been made to identify proteins of the exosporium but only a few have so far been characterised and their role in determining spore architecture and spore function is still poorly understood. We have characterised the exosporium protein, YwdL. ΔywdL spores have a more fragile exosporium, subject to damage on repeated freeze-thawing, although there is no evidence of altered resistance properties, and coats appear intact. Immunogold labelling and Western blotting with anti-YwdL antibodies identified YwdL to be located exclusively on the inner surface of the exosporium of B. cereus and B. thuringiensis. We conclude that YwdL is important for formation of a robust exosporium but is not required to maintain the crystalline assembly within the basal layer or for attachment of the hairy nap structure. ΔywdL spores are unable to germinate in response to CaDPA, and have altered germination properties, a phenotype that confirms the expected defect in localization of the cortex lytic enzyme CwlJ in the coat.
url http://europepmc.org/articles/PMC3161080?pdf=render
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