Institution
Unit of Virus Host Cell Interactions
Facility•Grenoble, France•
About: Unit of Virus Host Cell Interactions is a facility organization based out in Grenoble, France. It is known for research contribution in the topics: RNA & Binding site. The organization has 199 authors who have published 248 publications receiving 14467 citations.
Topics: RNA, Binding site, Polymerase, Viral replication, ESCRT
Papers
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TL;DR: Both oligomerization routes the authors characterized could be exploited by cellular or viral factors to modulate or control viral RNA encapsidation by NP and bind directly as oligomers to RNA with a higher affinity than that of the monomers.
42 citations
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TL;DR: The HpDnaB double-hexamer architecture supports an alternative strategy to load bacterial helicases onto forks in the absence of helicase loaders.
42 citations
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TL;DR: Through a targeted regulation of surface BST2, Vpu promotes HIV-1 release and limits pDC antiviral responses upon sensing of infected cells, likely to be important for an efficient early viral dissemination during acute HIV infection.
Abstract: Plasmacytoid dendritic cells (pDCs) constitute a major source of type-I interferon (IFN-I) production during acute HIV infection. Their activation results primarily from TLR7-mediated sensing of HIV-infected cells. However, the interactions between HIV-infected T cells and pDCs that modulate this sensing process remain poorly understood. BST2/Tetherin is a restriction factor that inhibits HIV release by cross-linking virions onto infected cell surface. BST2 was also shown to engage the ILT7 pDC-specific inhibitory receptor and repress TLR7/9-mediated IFN-I production by activated pDCs. Here, we show that Vpu, the HIV-1 antagonist of BST2, suppresses TLR7-mediated IFN-I production by pDC through a mechanism that relies on the interaction of BST2 on HIV-producing cells with ILT7. Even though Vpu downregulates surface BST2 as a mean to counteract the restriction on HIV-1 release, we also find that the viral protein re-locates remaining BST2 molecules outside viral assembly sites where they are free to bind and activate ILT7 upon cell-to-cell contact. This study shows that through a targeted regulation of surface BST2, Vpu promotes HIV-1 release and limits pDC antiviral responses upon sensing of infected cells. This mechanism of innate immune evasion is likely to be important for an efficient early viral dissemination during acute infection.
40 citations
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TL;DR: It is shown that Agrocin 84 requires tRNA(Leu) for tight binding to the LeuRS synthetic active site, unlike any previously reported inhibitors.
Abstract: Agrobacterium radiobacter strain K84 generates an antibiotic targeting pathogenic strains of Agrobacterium tumefaciens, enabling its use as a biocontrol to prevent infection of crops. Here the authors show that this antibiotic inhibits leucyl-tRNA synthetases via an unusual mechanism that depends on binding of tRNALeu.
40 citations
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TL;DR: The structure represents a snapshot of an assembled Vps4 conformation and provides insight into the molecular motions the ring structure undergoes in a concerted action to couple ATP hydrolysis to ESCRT-III substrate disassembly.
Abstract: The vacuolar protein sorting 4 AAA-ATPase (Vps4) recycles endosomal sorting complexes required for transport (ESCRT-III) polymers from cellular membranes. Here we present a 3.6-A X-ray structure of ring-shaped Vps4 from Metallosphera sedula (MsVps4), seen as an asymmetric pseudohexamer. Conserved key interface residues are shown to be important for MsVps4 assembly, ATPase activity in vitro, ESCRT-III disassembly in vitro and HIV-1 budding. ADP binding leads to conformational changes within the protomer, which might propagate within the ring structure. All ATP-binding sites are accessible and the pseudohexamer binds six ATP with micromolar affinity in vitro. In contrast, ADP occupies one high-affinity and five low-affinity binding sites in vitro, consistent with conformational asymmetry induced on ATP hydrolysis. The structure represents a snapshot of an assembled Vps4 conformation and provides insight into the molecular motions the ring structure undergoes in a concerted action to couple ATP hydrolysis to ESCRT-III substrate disassembly.
40 citations
Authors
Showing all 202 results
Name | H-index | Papers | Citations |
---|---|---|---|
Stephen Cusack | 81 | 290 | 21552 |
Rob W.H. Ruigrok | 70 | 166 | 13831 |
Guy Schoehn | 51 | 180 | 8348 |
Christoph W. Müller | 51 | 137 | 10240 |
Winfried Weissenhorn | 51 | 121 | 10142 |
Imre Berger | 43 | 145 | 6501 |
Annelies S. Zinkernagel | 39 | 142 | 11109 |
Marc Jamin | 37 | 77 | 3878 |
Andrew A. McCarthy | 35 | 75 | 5275 |
Niels H. Gehring | 35 | 65 | 4217 |
Ramesh S. Pillai | 35 | 60 | 10255 |
Christiane Schaffitzel | 34 | 86 | 5055 |
Patrice Morand | 34 | 138 | 4374 |
Adam Round | 34 | 66 | 3659 |
Matthew W. Bowler | 31 | 84 | 2705 |