ArticleJournal of bacteriology2010
Sequence motifs and proteolytic cleavage of the collagen-like glycoprotein BclA required for its attachment to the exosporium of Bacillus anthracis.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 30 citations in OpenAlex.
- Phylogenomic analysis of the collagen-like BclA proteins inApplied and environmental microbiology · 2026Article
- Helical ultrastructure of the L-ENA spore aggregation factor of a Bacillus paranthracis foodborne outbreak strain.Nature communications · 2024Article
- Ectopical expression of bacterial collagen-like protein supports its role as adhesin in host-parasite coevolution.Royal Society open science · 2024Article
- Article
- Roles and Organization of BxpB (ExsFA) and ExsFB in the Exosporium Outer Basal Layer of Bacillus anthracis.Journal of bacteriology · 2022Article
- Prokaryotic Collagen-Like Proteins as Novel Biomaterials.Frontiers in bioengineering and biotechnology · 2022Review
- When Appearance Misleads: The Role of the Entomopathogen Surface in the Relationship with Its Host.Insects · 2020Review
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- Surviving Between Hosts: Sporulation and Transmission.Microbiology spectrum · 2016Review
- Bacillus anthracis Spore Surface Protein BclA Mediates Complement Factor H Binding to Spores and Promotes Spore Persistence.PLoS pathogens · 2016Article
- The Regulation of Exosporium-Related Genes in Bacillus thuringiensis.Scientific reports · 2016Article
- The Exosporium Layer of Bacterial Spores: a Connection to the Environment and the Infected Host.Microbiology and molecular biology reviews : MMBR · 2015Review
- Plasmid-encoded genes influence exosporium assembly and morphology in Bacillus megaterium QM B1551 spores.FEMS microbiology letters · 2015Article
- Bacterial collagen-like proteins that form triple-helical structures.Journal of structural biology · 2014Article
- Cryo-EM analysis of the organization of BclA and BxpB in the Bacillus anthracis exosporium.Journal of structural biology · 2014Article
- Surface display of recombinant proteins on Escherichia coli by BclA exosporium of Bacillus anthracis.Microbial cell factories · 2013Article
- A genetic approach for the identification of exosporium assembly determinants of Bacillus anthracis.Journal of microbiological methods · 2013Article
- Assembly of the BclB glycoprotein into the exosporium and evidence for its role in the formation of the exosporium 'cap' structure in Bacillus anthracis.Molecular microbiology · 2012Article
- Localization and assembly of the novel exosporium protein BetA of Bacillus anthracis.Journal of bacteriology · 2011Article
- The co-dependence of BxpB/ExsFA and BclA for proper incorporation into the exosporium of Bacillus anthracis.Molecular microbiology · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Bacillus anthracis spores are enclosed by an exosporium comprised of a basal layer and an external hair-like nap. The filaments of the nap are composed of trimers of the collagen-like glycoprotein BclA. The attachment of essentially all BclA trimers to the exosporium requires the basal layer protein BxpB, and both proteins are included in stable high-molecular-mass exosporium complexes. BclA contains a proteolytically processed 38-residue amino-terminal domain (NTD) that is essential for basal-layer attachment. In this report, we identify three NTD submotifs (SM1a, SM1b, and SM2, located within residues 21 to 33) that are important for BclA attachment and demonstrate that residue A20, the amino-terminal residue of processed BclA, is not required for attachment. We show that the shortest NTD of BclA-or of a recombinant protein-sufficient for high-level basal-layer attachment is a 10-residue motif consisting of an initiating methionine, an apparently arbitrary second residue, SM1a or SM1b, and SM2. We also demonstrate that cleavage of the BclA NTD is necessary for efficient attachment to the basal layer and that the site of cleavage is somewhat flexible, at least in certain mutant NTDs. Finally, we propose a mechanism for BclA attachment and discuss the possibility that analogous mechanisms are involved in the attachment of many different collagen-like proteins of B. anthracis and closely related Bacillus species.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.