Benoît Arragain
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View article: Polymerase trapping as mechanism of H5 highly pathogenic avian influenza virus genesis
Polymerase trapping as mechanism of H5 highly pathogenic avian influenza virus genesis Open
Highly pathogenic avian influenza viruses (HPAIVs) derive from H5 and H7 low pathogenic avian influenza viruses (LPAIVs). Although insertion of a furin-cleavable multibasic cleavage site (MBCS) in the hemagglutinin gene was identified deca…
View article: Structure of the tilapia lake virus nucleoprotein bound to RNA
Structure of the tilapia lake virus nucleoprotein bound to RNA Open
Tilapia Lake virus (TiLV) belongs to the Amnoonviridae family within the Articulavirales order of segmented negative-strand RNA viruses and is highly diverged from more familiar orthomyxoviruses, such as influenza. The viral nucleoprotein …
View article: Structure of the Tilapia lake virus nucleoprotein bound to RNA
Structure of the Tilapia lake virus nucleoprotein bound to RNA Open
Tilapia Lake virus (TiLV) belongs to the Amnoonviridae family within the Articulavirales order of segmented negative-strand RNA viruses and is highly diverged from more familiar orthomyxoviruses, such as influenza. The viral nucleoprotein …
View article: The RBPome of influenza A virus NP-mRNA reveals a role for TDP-43 in viral replication
The RBPome of influenza A virus NP-mRNA reveals a role for TDP-43 in viral replication Open
Genome-wide approaches have significantly advanced our knowledge of the repertoire of RNA-binding proteins (RBPs) that associate with cellular polyadenylated mRNAs within eukaryotic cells. Recent studies focusing on the RBP interactomes of…
View article: Structures of influenza A and B replication complexes explain avian to human host adaption and reveal a role of ANP32 as an electrostatic chaperone for the apo-polymerase
Structures of influenza A and B replication complexes explain avian to human host adaption and reveal a role of ANP32 as an electrostatic chaperone for the apo-polymerase Open
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…
View article: Structural characterization of the oligomerization of full-length Hantaan virus polymerase into symmetric dimers and hexamers
Structural characterization of the oligomerization of full-length Hantaan virus polymerase into symmetric dimers and hexamers Open
Hantaan virus is a dangerous human pathogen whose segmented negative-stranded RNA genome is replicated and transcribed by a virally-encoded multi-functional polymerase. Here we describe the complete cryo-electron microscopy structure of Ha…
View article: Structural and functional analysis of the minimal orthomyxovirus-like polymerase of Tilapia Lake Virus from the highly diverged<i>Amnoonviridae</i>family
Structural and functional analysis of the minimal orthomyxovirus-like polymerase of Tilapia Lake Virus from the highly diverged<i>Amnoonviridae</i>family Open
Tilapia Lake Virus (TiLV), a recently discovered pathogen of tilapia fish, belongs to the Amnoonviridae family from the Articulavirales order. Its ten genome segments have characteristic conserved ends and encode proteins with no known hom…
View article: The host RNA polymerase II C-terminal domain is the anchor for replication of the influenza virus genome
The host RNA polymerase II C-terminal domain is the anchor for replication of the influenza virus genome Open
Summary The current model is that the influenza virus polymerase (FluPol) binds either to host RNA polymerase II (RNAP II) or to the acidic nuclear phosphoprotein 32 (ANP32), which drives its conformation and activity towards transcription…
View article: Structures of active Hantaan virus polymerase uncover the mechanisms of Hantaviridae genome replication
Structures of active Hantaan virus polymerase uncover the mechanisms of Hantaviridae genome replication Open
Hantaviruses are causing life-threatening zoonotic infections in humans. Their tripartite negative-stranded RNA genome is replicated by the multi-functional viral RNA-dependent RNA-polymerase. Here we describe the structure of the Hantaan …
View article: Oxygen-Sensitive Metalloprotein Structure Determination by Cryo-Electron Microscopy
Oxygen-Sensitive Metalloprotein Structure Determination by Cryo-Electron Microscopy Open
Metalloproteins are involved in key cell processes such as photosynthesis, respiration, and oxygen transport. However, the presence of transition metals (notably iron as a component of [Fe-S] clusters) often makes these proteins sensitive …
View article: Analyse structurale et fonctionnelle de la réplication et de la transcription des Bunyavirales
Analyse structurale et fonctionnelle de la réplication et de la transcription des Bunyavirales Open
The Bunyavirales order encompasses over 500 species of segmented negative stranded RNA viruses (sNSV). Widespread throughout the world and considered as emerging viruses, the infection of humans by bunyaviruses can lead to serious diseases…
View article: Structural snapshots of La Crosse virus polymerase reveal the mechanisms underlying <i>Peribunyaviridae</i> replication and transcription
Structural snapshots of La Crosse virus polymerase reveal the mechanisms underlying <i>Peribunyaviridae</i> replication and transcription Open
Segmented negative-strand RNA bunyaviruses encode a multi-functional polymerase that performs genome replication and transcription. Here, we establish conditions for in vitro activity of La Crosse virus polymerase and visualize by cryo-ele…
View article: Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes
Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes Open
Bunyavirales is an order of segmented negative-strand RNA viruses comprising several life-threatening pathogens against which no effective treatment is currently available. Replication and transcription of the RNA genome constitute essenti…
View article: High resolution cryo-EM structure of the helical RNA-bound Hantaan virus nucleocapsid reveals its assembly mechanisms
High resolution cryo-EM structure of the helical RNA-bound Hantaan virus nucleocapsid reveals its assembly mechanisms Open
Negative-strand RNA viruses condense their genome into helical nucleocapsids that constitute essential templates for viral replication and transcription. The intrinsic flexibility of nucleocapsids usually prevents their full-length structu…
View article: Author response: High resolution cryo-EM structure of the helical RNA-bound Hantaan virus nucleocapsid reveals its assembly mechanisms
Author response: High resolution cryo-EM structure of the helical RNA-bound Hantaan virus nucleocapsid reveals its assembly mechanisms Open
Article Figures and data Abstract eLife digest Introduction Results Discussion Materials and methods Data availability References Decision letter Author response Article and author information Metrics Abstract Negative-strand RNA viruses c…
View article: Helical RNA-bound Hantaan virus nucleocapsid
Helical RNA-bound Hantaan virus nucleocapsid Open
Negative-strand RNA viruses condense their genome into helical nucleocapsids that constitute essential templates for viral replication and transcription. The intrinsic flexibility of nucleocapsids usually prevents their full-length structu…