Structure and function of the EA1 surface layer of Bacillus anthracis
Abstract The Gram-positive spore-forming bacterium Bacillus anthracis is the causative agent of anthrax, a deadly disease mostly affecting wildlife and livestock, as well as representing a bioterrorism threat. Its cell surface is covered by the mutually exclusive S-layers Sap and EA1, found in early...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2023-11-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-023-42826-x |
| _version_ | 1797636811534630912 |
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| author | Adrià Sogues Antonella Fioravanti Wim Jonckheere Els Pardon Jan Steyaert Han Remaut |
| author_facet | Adrià Sogues Antonella Fioravanti Wim Jonckheere Els Pardon Jan Steyaert Han Remaut |
| author_sort | Adrià Sogues |
| collection | DOAJ |
| description | Abstract The Gram-positive spore-forming bacterium Bacillus anthracis is the causative agent of anthrax, a deadly disease mostly affecting wildlife and livestock, as well as representing a bioterrorism threat. Its cell surface is covered by the mutually exclusive S-layers Sap and EA1, found in early and late growth phases, respectively. Here we report the nanobody-based structural characterization of EA1 and its native lattice contacts. The EA1 assembly domain consists of 6 immunoglobulin-like domains, where three calcium-binding sites structure interdomain contacts that allow monomers to adopt their assembly-competent conformation. Nanobody-induced depolymerization of EA1 S-layers results in surface defects, membrane blebbing and cell lysis under hypotonic conditions, indicating that S-layers provide additional mechanical stability to the cell wall. Taken together, we report a complete model of the EA1 S-layer and present a set of nanobodies that may have therapeutic potential against Bacillus anthracis. |
| first_indexed | 2024-03-11T12:39:32Z |
| format | Article |
| id | doaj.art-4644f6336e76474b9d2d70945a0c3c06 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-03-11T12:39:32Z |
| publishDate | 2023-11-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-4644f6336e76474b9d2d70945a0c3c062023-11-05T12:22:17ZengNature PortfolioNature Communications2041-17232023-11-0114111310.1038/s41467-023-42826-xStructure and function of the EA1 surface layer of Bacillus anthracisAdrià Sogues0Antonella Fioravanti1Wim Jonckheere2Els Pardon3Jan Steyaert4Han Remaut5Structural and Molecular Microbiology, VIB-VUB Center for Structural Biology, VIBStructural and Molecular Microbiology, VIB-VUB Center for Structural Biology, VIBStructural and Molecular Microbiology, VIB-VUB Center for Structural Biology, VIBStructural Biology Brussels, Vrije Universiteit Brussel, VUBStructural Biology Brussels, Vrije Universiteit Brussel, VUBStructural and Molecular Microbiology, VIB-VUB Center for Structural Biology, VIBAbstract The Gram-positive spore-forming bacterium Bacillus anthracis is the causative agent of anthrax, a deadly disease mostly affecting wildlife and livestock, as well as representing a bioterrorism threat. Its cell surface is covered by the mutually exclusive S-layers Sap and EA1, found in early and late growth phases, respectively. Here we report the nanobody-based structural characterization of EA1 and its native lattice contacts. The EA1 assembly domain consists of 6 immunoglobulin-like domains, where three calcium-binding sites structure interdomain contacts that allow monomers to adopt their assembly-competent conformation. Nanobody-induced depolymerization of EA1 S-layers results in surface defects, membrane blebbing and cell lysis under hypotonic conditions, indicating that S-layers provide additional mechanical stability to the cell wall. Taken together, we report a complete model of the EA1 S-layer and present a set of nanobodies that may have therapeutic potential against Bacillus anthracis.https://doi.org/10.1038/s41467-023-42826-x |
| spellingShingle | Adrià Sogues Antonella Fioravanti Wim Jonckheere Els Pardon Jan Steyaert Han Remaut Structure and function of the EA1 surface layer of Bacillus anthracis Nature Communications |
| title | Structure and function of the EA1 surface layer of Bacillus anthracis |
| title_full | Structure and function of the EA1 surface layer of Bacillus anthracis |
| title_fullStr | Structure and function of the EA1 surface layer of Bacillus anthracis |
| title_full_unstemmed | Structure and function of the EA1 surface layer of Bacillus anthracis |
| title_short | Structure and function of the EA1 surface layer of Bacillus anthracis |
| title_sort | structure and function of the ea1 surface layer of bacillus anthracis |
| url | https://doi.org/10.1038/s41467-023-42826-x |
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