The structures of two archaeal type IV pili illuminate evolutionary relationships
We have determined the cryo-electron microscopic (cryo-EM) structures of two archaeal type IV pili (T4P), from Pyrobaculum arsenaticum and Saccharolobus solfataricus, at 3.8 Å and 3.4 Å resolution, respectively. This triples the number of high resolution archaeal T4P structures, and allows us to pinpoint the evolutionary divergence of bacterial T4P, archaeal T4P and archaeal flagellar filaments. We suggest that extensive glycosylation previously observed in T4P of Sulfolobus islandicus is a response to an acidic environment, as at even higher temperatures in a neutral environment much less glycosylation is present for Pyrobaculum than for Sulfolobus and Saccharolobus pili. Consequently, the Pyrobaculum filaments do not display the remarkable stability of the Sulfolobus filaments in vitro. We identify the Saccharolobus and Pyrobaculum T4P as host receptors recognized by rudivirus SSRV1 and tristromavirus PFV2, respectively. Our results illuminate the evolutionary relationships among bacterial and archaeal T4P filaments and provide insights into archaeal virus-host interactions.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2020 |
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| Erschienen: |
2020 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:11 |
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| Enthalten in: |
Nature communications - 11(2020), 1 vom: 09. Juli, Seite 3424 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Wang, Fengbin [VerfasserIn] |
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| Links: |
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| Themen: |
Archaeal Proteins |
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| Anmerkungen: |
Date Completed 31.08.2020 Date Revised 09.07.2021 published: Electronic Citation Status MEDLINE |
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| doi: |
10.1038/s41467-020-17268-4 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM312239769 |
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| 245 | 1 | 4 | |a The structures of two archaeal type IV pili illuminate evolutionary relationships |
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| 500 | |a Citation Status MEDLINE | ||
| 520 | |a We have determined the cryo-electron microscopic (cryo-EM) structures of two archaeal type IV pili (T4P), from Pyrobaculum arsenaticum and Saccharolobus solfataricus, at 3.8 Å and 3.4 Å resolution, respectively. This triples the number of high resolution archaeal T4P structures, and allows us to pinpoint the evolutionary divergence of bacterial T4P, archaeal T4P and archaeal flagellar filaments. We suggest that extensive glycosylation previously observed in T4P of Sulfolobus islandicus is a response to an acidic environment, as at even higher temperatures in a neutral environment much less glycosylation is present for Pyrobaculum than for Sulfolobus and Saccharolobus pili. Consequently, the Pyrobaculum filaments do not display the remarkable stability of the Sulfolobus filaments in vitro. We identify the Saccharolobus and Pyrobaculum T4P as host receptors recognized by rudivirus SSRV1 and tristromavirus PFV2, respectively. Our results illuminate the evolutionary relationships among bacterial and archaeal T4P filaments and provide insights into archaeal virus-host interactions | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, N.I.H., Extramural | |
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| 700 | 1 | |a Baquero, Diana P |e verfasserin |4 aut | |
| 700 | 1 | |a Su, Zhangli |e verfasserin |4 aut | |
| 700 | 1 | |a Beltran, Leticia C |e verfasserin |4 aut | |
| 700 | 1 | |a Prangishvili, David |e verfasserin |4 aut | |
| 700 | 1 | |a Krupovic, Mart |e verfasserin |4 aut | |
| 700 | 1 | |a Egelman, Edward H |e verfasserin |4 aut | |
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