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J Bacteriol. 2011 Oct;193(19):5098-104. doi: 10.1128/JB.05658-11. Epub 2011 Aug 5.

Localization and assembly of the novel exosporium protein BetA of Bacillus anthracis.

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1
Department of Biochemistry, 471E Bond Life Sciences Center, 1201 E. Rollins Street, University of Missouri, Columbia, MO 65211, USA.

Abstract

The exosporium of Bacillus anthracis is comprised of two distinct layers: a basal layer and a hair-like nap that covers the basal layer. The hair-like nap contains the glycoproteins BclA and, most likely, BclB. BclA and BclB are directed to assemble into the exosporium by motifs in their N-terminal domains. Here, we identify a previously uncharacterized putative gene encoding this motif, which we have named betA (Bacillus exosporium-targeted protein of B. anthracis). Like bclA, betA encodes a putative collagenlike repeat region. betA is present in several genomes of exosporium-producing Bacillus species but, so far, not in any others. Using fluorescence microscopic localization of a BetA-enhanced green fluorescent protein (eGFP) fusion protein and immunofluorescence microscopy with anti-BetA antibodies, we showed that BetA resides in the exosporium basal layer, likely underneath BclA. BetA assembles at the spore surface at around hour 5 of sporulation and under the control of BxpB, similar to the control of deposition of BclA. We suggest a model in which BclA and BetA are incorporated into the exosporium by a mechanism that depends on their similar N termini. These data suggest that BetA is a member of a growing family of exosporium proteins that assemble under the control of targeting sequences in their N termini.

PMID:
21821770
PMCID:
PMC3187373
DOI:
10.1128/JB.05658-11
[Indexed for MEDLINE]
Free PMC Article
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