Structural conservation in a membrane-enveloped filamentous virus infecting a hyperthermophilic acidophile
| العنوان: | Structural conservation in a membrane-enveloped filamentous virus infecting a hyperthermophilic acidophile |
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| المؤلفون: | Liu, Ying, Osinski, Tomasz, Wang, Fengbin, Krupovic, Mart, Schouten, Stefan, Kasson, Peter, Prangishvili, David, Egelman, Edward H., non-UU output of UU-AW members |
| المساهمون: | Biologie Moléculaire du Gène chez les Extrêmophiles (BMGE), Institut Pasteur [Paris], University of Virginia [Charlottesville], Royal Netherlands Institute for Sea Research (NIOZ), Utrecht University [Utrecht], This work was supported by NIH R35GM122510 (to E.H.E.), the European Union’s Horizon 2020 research and innovation program under grant agreement 685778, project VIRUS‑X (to D.P.) and l’Agence Nationale de la Recherche (France) project ENVIRA (to M.K.). The cryo-EM imaging was conducted at the Molecular Electron Microscopy Core facility at the University of Virginia, which is supported by the School of Medicine and built with NIH grant G20-RR31199. The Titan Krios and Falcon II direct electron detector were obtained with NIH S10-RR025067 and S10-OD018149, respectively. Ellen Hopmans and Caglar Yildiz (NIOZ) are thanked for analytical support., ANR-17-CE15-0005,ENVIRA,Remodelage de la membrane cytoplasmique par les virus enveloppés d'archées(2017), European Project: 685778,H2020,H2020-LEIT-BIO-2015-1,Virus-X(2016), Institut Pasteur [Paris] (IP), University of Virginia, non-UU output of UU-AW members |
| المصدر: | Nature Communications Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018) Nature Communications, 9(1). Nature Publishing Group Nature Communications, Nature Publishing Group, 2018, 9 (1), pp.3360. ⟨10.1038/s41467-018-05684-6⟩ Nature Communications, 2018, 9 (1), pp.3360. ⟨10.1038/s41467-018-05684-6⟩ |
| بيانات النشر: | Nature Publishing Group UK, 2018. |
| سنة النشر: | 2018 |
| مصطلحات موضوعية: | 0301 basic medicine, Chemistry(all), [SDV]Life Sciences [q-bio], viruses, ved/biology.organism_classification_rank.species, General Physics and Astronomy, MESH: Protein Structure, Secondary, Biochemistry, Protein Structure, Secondary, chemistry.chemical_compound, Extreme environment, lcsh:Science, Genetics, Sulfolobus shibatae, Multidisciplinary, biology, MESH: DNA Viruses, Sulfolobus, MESH: Sulfolobus, Acidophile, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, MESH: Virion, MESH: Cryoelectron Microscopy, MESH: Genome, Viral, Science, macromolecular substances, Genome, Viral, Physics and Astronomy(all), General Biochemistry, Genetics and Molecular Biology, Virus, Article, 03 medical and health sciences, Viral Proteins, Archaeol, 030102 biochemistry & molecular biology, ved/biology, Biochemistry, Genetics and Molecular Biology(all), Cryoelectron Microscopy, DNA Viruses, Virion, General Chemistry, biology.organism_classification, MESH: Viral Proteins, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, 030104 developmental biology, chemistry, lcsh:Q, DNA, Archaea, Genetics and Molecular Biology(all) |
| الوصف: | Different forms of viruses that infect archaea inhabiting extreme environments continue to be discovered at a surprising rate, suggesting that the current sampling of these viruses is sparse. We describe here Sulfolobus filamentous virus 1 (SFV1), a membrane-enveloped virus infecting Sulfolobus shibatae. The virus encodes two major coat proteins which display no apparent sequence similarity with each other or with any other proteins in databases. We have used cryo-electron microscopy at 3.7 Å resolution to show that these two proteins form a nearly symmetrical heterodimer, which wraps around A-form DNA, similar to what has been shown for SIRV2 and AFV1, two other archaeal filamentous viruses. The thin (∼ 20 Å) membrane of SFV1 is mainly archaeol, a lipid species that accounts for only 1% of the host lipids. Our results show how relatively conserved structural features can be maintained across evolution by both proteins and lipids that have diverged considerably. Only a few archaeal filamentous viruses have been structurally characterized. Here the authors describe the membrane-enveloped Sulfolobus filamentous virus 1 that infects Sulfolobus shibatae and present its 3.7 Å resolution cryo-EM structure, which reveals that major coat proteins are structurally conserved among archaeal filamentous viruses. |
| وصف الملف: | application/pdf; image/pdf |
| اللغة: | English |
| تدمد: | 2041-1723 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d6c3ddbb2f86a54d0eadc205e62bb72 http://europepmc.org/articles/PMC6105669 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....3d6c3ddbb2f86a54d0eadc205e62bb72 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 20411723 |
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