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Showing 1–13 of 13 results
Advanced filters: Author: David Prangishvili Clear advanced filters

  • In this Essay, Alberset al. discuss the remarkable achievements of two leaders of the archaeal research field: the late Carl Woese and the late Wolfram Zillig. They highlight how the discoveries of these two researchers have inspired the current and upcoming generations of microbiologists.

    • Sonja-Verena Albers
    • Patrick Forterre
    • Christa Schleper
    Comments & Opinion
    Nature Reviews Microbiology
    Volume: 11, P: 713-719

  • The rod-shaped virus APBV1 is among the most thermostable viruses known. Here, Ptchelkine et al. determine its structure at near-atomic resolution, show that the DNA is packed as left-handed superhelix and identify extended hydrophobic interfaces that likely contribute to the extreme thermostability of the capsid.

    • Denis Ptchelkine
    • Ashley Gillum
    • Juha T. Huiskonen
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-6

  • One of the most prominent features of archaea is the extraordinary diversity of their viruses. In this Review, Prangishviliet al. summarize their morphological diversity, the molecular biology of their life cycles and virus–host interactions, and discuss their evolution and their role in the global virosphere.

    • David Prangishvili
    • Dennis H. Bamford
    • Mart Krupovic
    Reviews
    Nature Reviews Microbiology
    Volume: 15, P: 724-739

  • Cultured archaeal viruses, which so far all have double-stranded DNA genomes, come in all shapes and sizes, with the range of virion morphotypes surpassing that found in the viruses of the Bacteria. The authors present a unifying view of this fascinating viral group.

    • David Prangishvili
    • Patrick Forterre
    • Roger A. Garrett
    Reviews
    Nature Reviews Microbiology
    Volume: 4, P: 837-848

  • Growing two long filamentous tails may help an archaeal virus to survive in a hostile environment.

    • Monika Häring
    • Gisle Vestergaard
    • David Prangishvili
    Research
    Nature
    Volume: 436, P: 1101-1102

  • 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.

    • Ying Liu
    • Tomasz Osinski
    • Edward H. Egelman
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-10

  • Understanding the structural basis for the inhibition of archaeal eukaryotic-like RNA polymerases (RNAPs) during virus infection is of interest for drug design. Here, the authors present the cryo-EM structures of apo Sulfolobus acidocaldarius RNAP and the RNAP complex structures with two regulatory factors, RIP and TFS4 that inhibit transcription and discuss their inhibitory mechanisms.

    • Simona Pilotto
    • Thomas Fouqueau
    • Finn Werner
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-15

  • Here, the authors investigate the diversity and dynamics of the CRISPRome in the hyperthermophilic archaea of the order Sulfolobales, and find the most abundant spacers to come from mini-CRISPR arrays of archaeal viruses, which might represent a strategy for superinfection exclusion and promotion of archaeal virus speciation.

    • Sofia Medvedeva
    • Ying Liu
    • Mart Krupovic
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-10

  • Certain bacterial enzymes are packaged within protein chambers that provide a confined environment for their reactions to take place. Ban and colleagues now identify a family of proteins that form nanocompartments, similar to bacterial microcompartments such as the carboxysome, and show that the enzymes within are anchored by their C-terminal extensions to binding sites on the inner surface of the chamber.

    • Markus Sutter
    • Daniel Boehringer
    • Nenad Ban
    Research
    Nature Structural & Molecular Biology
    Volume: 15, P: 939-947

  • Archaeal type IV pili (T4P) mediate adhesion to surfaces and are receptors for hyperthermophilic archaeal viruses. Here, the authors present the cryo-EM structures of two archaeal T4P from Pyrobaculum arsenaticum and Saccharolobus solfataricus and discuss evolutionary relationships between bacterial T4P, archaeal T4P and archaeal flagellar filaments.

    • Fengbin Wang
    • Diana P. Baquero
    • Edward H. Egelman
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-10

  • The electron cryo-microscopy structure of Sulfolobus islandicus pili enabled the identification of SiL_2606 as the main pilin in these filaments and revealed that the pili are glycosylated, which probably explains how these structures remain soluble and stable even when cells grow at pH 3 and 80 °C.

    • Fengbin Wang
    • Virginija Cvirkaite-Krupovic
    • Edward H. Egelman
    Research
    Nature Microbiology
    Volume: 4, P: 1401-1410