Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals.
Biofilms are communities of bacteria that grow encased in an extracellular matrix that often contains proteins. The spatial organization and the molecular interactions between matrix scaffold proteins remain in most cases largely unknown. Here, we report that Bap protein of Staphylococcus aureus sel...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2016-06-01
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| Series: | PLoS Pathogens |
| Online Access: | https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1005711&type=printable |
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| _version_ | 1849435457537966080 |
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| author | Agustina Taglialegna Susanna Navarro Salvador Ventura James A Garnett Steve Matthews José R Penades Iñigo Lasa Jaione Valle |
| author_facet | Agustina Taglialegna Susanna Navarro Salvador Ventura James A Garnett Steve Matthews José R Penades Iñigo Lasa Jaione Valle |
| author_sort | Agustina Taglialegna |
| collection | DOAJ |
| description | Biofilms are communities of bacteria that grow encased in an extracellular matrix that often contains proteins. The spatial organization and the molecular interactions between matrix scaffold proteins remain in most cases largely unknown. Here, we report that Bap protein of Staphylococcus aureus self-assembles into functional amyloid aggregates to build the biofilm matrix in response to environmental conditions. Specifically, Bap is processed and fragments containing at least the N-terminus of the protein become aggregation-prone and self-assemble into amyloid-like structures under acidic pHs and low concentrations of calcium. The molten globule-like state of Bap fragments is stabilized upon binding of the cation, hindering its self-assembly into amyloid fibers. These findings define a dual function for Bap, first as a sensor and then as a scaffold protein to promote biofilm development under specific environmental conditions. Since the pH-driven multicellular behavior mediated by Bap occurs in coagulase-negative staphylococci and many other bacteria exploit Bap-like proteins to build a biofilm matrix, the mechanism of amyloid-like aggregation described here may be widespread among pathogenic bacteria. |
| format | Article |
| id | doaj-art-5a927ce032ed46a7996413f65abdf3c0 |
| institution | Kabale University |
| issn | 1553-7366 1553-7374 |
| language | English |
| publishDate | 2016-06-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj-art-5a927ce032ed46a7996413f65abdf3c02025-08-20T03:26:16ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742016-06-01126e100571110.1371/journal.ppat.1005711Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals.Agustina TaglialegnaSusanna NavarroSalvador VenturaJames A GarnettSteve MatthewsJosé R PenadesIñigo LasaJaione ValleBiofilms are communities of bacteria that grow encased in an extracellular matrix that often contains proteins. The spatial organization and the molecular interactions between matrix scaffold proteins remain in most cases largely unknown. Here, we report that Bap protein of Staphylococcus aureus self-assembles into functional amyloid aggregates to build the biofilm matrix in response to environmental conditions. Specifically, Bap is processed and fragments containing at least the N-terminus of the protein become aggregation-prone and self-assemble into amyloid-like structures under acidic pHs and low concentrations of calcium. The molten globule-like state of Bap fragments is stabilized upon binding of the cation, hindering its self-assembly into amyloid fibers. These findings define a dual function for Bap, first as a sensor and then as a scaffold protein to promote biofilm development under specific environmental conditions. Since the pH-driven multicellular behavior mediated by Bap occurs in coagulase-negative staphylococci and many other bacteria exploit Bap-like proteins to build a biofilm matrix, the mechanism of amyloid-like aggregation described here may be widespread among pathogenic bacteria.https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1005711&type=printable |
| spellingShingle | Agustina Taglialegna Susanna Navarro Salvador Ventura James A Garnett Steve Matthews José R Penades Iñigo Lasa Jaione Valle Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals. PLoS Pathogens |
| title | Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals. |
| title_full | Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals. |
| title_fullStr | Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals. |
| title_full_unstemmed | Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals. |
| title_short | Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals. |
| title_sort | staphylococcal bap proteins build amyloid scaffold biofilm matrices in response to environmental signals |
| url | https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1005711&type=printable |
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