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Structure of Nora v...
Structure of Nora virus at 2.7 angstrom resolution and implications for receptor binding, capsid stability and taxonomy
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Laurinmäki, Pasi (författare)
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Shakeel, Shabih (författare)
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- Ekström, Jens-Ola (författare)
- Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten),Institute of Biosciences and Medical Technology, BioMediTech, University of Tampere, Finland
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Mohammadi, Pezhman (författare)
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- Hultmark, Dan, 1949- (författare)
- Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten),Institute of Biosciences and Medical Technology, BioMediTech, University of Tampere, Finland
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Butcher, Sarah J. (författare)
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(creator_code:org_t)
- 2020-11-12
- 2020
- Engelska.
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Ingår i: Scientific Reports. - : Nature Publishing Group. - 2045-2322. ; 10:1
- Relaterad länk:
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https://doi.org/10.1...
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https://umu.diva-por... (primary) (Raw object)
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https://www.nature.c...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Nora virus, a virus of Drosophila, encapsidates one of the largest single-stranded RNA virus genomes known. Its taxonomic affinity is uncertain as it has a picornavirus-like cassette of enzymes for virus replication, but the capsid structure was at the time for genome publication unknown. By solving the structure of the virus, and through sequence comparison, we clear up this taxonomic ambiguity in the invertebrate RNA virosphere. Despite the lack of detectable similarity in the amino acid sequences, the 2.7 angstrom resolution cryoEM map showed Nora virus to have T=1 symmetry with the characteristic capsid protein beta -barrels found in all the viruses in the Picornavirales order. Strikingly, alpha -helical bundles formed from the extended C-termini of capsid protein VP4B and VP4C protrude from the capsid surface. They are similar to signalling molecule folds and implicated in virus entry. Unlike other viruses of Picornavirales, no intra-pentamer stabilizing annulus was seen, instead the intra-pentamer stability comes from the interaction of VP4C and VP4B N-termini. Finally, intertwining of the N-termini of two-fold symmetry-related VP4A capsid proteins and RNA, provides inter-pentamer stability. Based on its distinct structural elements and the genetic distance to other picorna-like viruses we propose that Nora virus, and a small group of related viruses, should have its own family within the order Picornavirales.
Ämnesord
- NATURVETENSKAP -- Biologi -- Strukturbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Structural Biology (hsv//eng)
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