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Structures of influenza A and B replication complexes give insight into avian to human host adaptation and reveal a role of ANP32 as an electrostatic chaperone for the apo-polymerase

Replication of influenza viral RNA depends on at least two viral polymerases, a parental replicase and an encapsidase, and cellular factor ANP32. ANP32 comprises an LRR domain and a long C-terminal low complexity acidic region (LCAR). Here we present evidence suggesting that ANP32 is recruited to th...

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Main Authors: Arragain, Benoit (Author) , Krischuns, Tim (Author) , Pelosse, Martin (Author) , Drncova, Petra (Author) , Blackledge, Martin (Author) , Naffakh, Nadia (Author) , Cusack, Stephen (Author)
Format: Article (Journal)
Language:English
Published: 19 August 2024
In: Nature Communications
Year: 2024, Volume: 15, Pages: 1-20
ISSN:2041-1723
DOI:10.1038/s41467-024-51007-3
Online Access:Verlag, kostenfrei, Volltext: https://doi.org/10.1038/s41467-024-51007-3
Verlag, kostenfrei, Volltext: https://www.nature.com/articles/s41467-024-51007-3
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Author Notes:Benoît Arragain, Tim Krischuns, Martin Pelosse, Petra Drncova, Martin Blackledge, Nadia Naffakh & Stephen Cusack
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Summary:Replication of influenza viral RNA depends on at least two viral polymerases, a parental replicase and an encapsidase, and cellular factor ANP32. ANP32 comprises an LRR domain and a long C-terminal low complexity acidic region (LCAR). Here we present evidence suggesting that ANP32 is recruited to the replication complex as an electrostatic chaperone that stabilises the encapsidase moiety within apo-polymerase symmetric dimers that are distinct for influenza A and B polymerases. The ANP32 bound encapsidase, then forms the asymmetric replication complex with the replicase, which is embedded in a parental ribonucleoprotein particle (RNP). Cryo-EM structures reveal the architecture of the influenza A and B replication complexes and the likely trajectory of the nascent RNA product into the encapsidase. The cryo-EM map of the FluB replication complex shows extra density attributable to the ANP32 LCAR wrapping around and stabilising the apo-encapsidase conformation. These structures give new insight into the various mutations that adapt avian strain polymerases to use the distinct ANP32 in mammalian cells.
Item Description:Gesehen am 18.07.2025
Physical Description:Online Resource
ISSN:2041-1723
DOI:10.1038/s41467-024-51007-3

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