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  1. Article: Les machineries réplicatives virales : synthèse en famille(s).

    Canard, Bruno

    Virologie (Montrouge, France)

    2020  Volume 16, Issue 4, Page(s) 183–184

    Title translation Les machineries réplicatives virales : synthèse en famille(s).
    Language English
    Publishing date 2020-09-11
    Publishing country France
    Document type Journal Article
    ZDB-ID 2118387-9
    ISSN 1950-6961 ; 1267-8694
    ISSN (online) 1950-6961
    ISSN 1267-8694
    DOI 10.1684/vir.2012.0453
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Kill or corrupt: Mechanisms of action and drug-resistance of nucleotide analogues against SARS-CoV-2.

    Shannon, Ashleigh / Canard, Bruno

    Antiviral research

    2022  Volume 210, Page(s) 105501

    Abstract: Nucleoside/tide analogues (NAs) have long been used in the fight against viral diseases, and now present a promising option for the treatment of COVID-19. Once activated to the 5'-triphosphate state, NAs act by targeting the viral RNA-dependent RNA- ... ...

    Abstract Nucleoside/tide analogues (NAs) have long been used in the fight against viral diseases, and now present a promising option for the treatment of COVID-19. Once activated to the 5'-triphosphate state, NAs act by targeting the viral RNA-dependent RNA-polymerase for incorporation into the viral RNA genome. Incorporated analogues can either 'kill' (terminate) synthesis, or 'corrupt' (genetically or chemically) the RNA. Against coronaviruses, the use of NAs has been further complicated by the presence of a virally encoded exonuclease domain (nsp14) with proofreading and repair capacities. Here, we describe the mechanism of action of four promising anti-COVID-19 NAs; remdesivir, molnupiravir, favipiravir and bemnifosbuvir. Their distinct mechanisms of action best exemplify the concept of 'killers' and 'corruptors'. We review available data regarding their ability to be incorporated and excised, and discuss the specific structural features that dictate their overall potency, toxicity, and mutagenic potential. This should guide the synthesis of novel analogues, lend insight into the potential for resistance mutations, and provide a rational basis for upcoming combinations therapies.
    MeSH term(s) Humans ; SARS-CoV-2 ; Nucleotides/pharmacology ; Nucleotides/chemistry ; Antiviral Agents/therapeutic use ; COVID-19 ; RNA, Viral/genetics
    Chemical Substances Nucleotides ; Antiviral Agents ; RNA, Viral
    Language English
    Publishing date 2022-12-22
    Publishing country Netherlands
    Document type Review ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 306628-9
    ISSN 1872-9096 ; 0166-3542
    ISSN (online) 1872-9096
    ISSN 0166-3542
    DOI 10.1016/j.antiviral.2022.105501
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1627: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Viral Instant Mutation Viewer: A Tool to Speed Up the Identification and Analysis of New SARS-CoV-2 Emerging Variants and Beyond.

    Wilde, Vincent / Canard, Bruno / Ferron, François

    Viruses

    2023  Volume 15, Issue 8

    Abstract: The appearance of genetic variants impacts vaccination efficiency and therapeutic options, generating a need to map and relate mutations observed in the proteome and the genome. We develop an user-friendly web service software (Viral Instant Mutation ... ...

    Abstract The appearance of genetic variants impacts vaccination efficiency and therapeutic options, generating a need to map and relate mutations observed in the proteome and the genome. We develop an user-friendly web service software (Viral Instant Mutation Viewer or VIMVer) which allows a direct identification of mutations in the genome and its counterpart in the viral proteome. Since its emergence in 2019, the severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), responsible for the COVID-19 pandemic, has generated an overwhelming amount of data while becoming one of the most studied viruses of the Nidovirales order. We originally developed this tool during the COVID pandemic; thus, for any SARS-CoV-2 nucleotide sequence, the web service gives a fast identification, mapping, and display of new mutations simultaneously at the nucleotide and amino acid level in comparison to a reference sequence (Wuhan-1). Furthermore, the lineage or the relative position to the known lineage of the variant of interest is available on the link to Phylogenetic Assignment of Named Global Outbreak LINeages (PANGOLIN COVID-19). The workflow presented here is available online. The source code is released under public license and can be easily adapted for further development to other viruses.
    MeSH term(s) Humans ; Animals ; SARS-CoV-2/genetics ; COVID-19 ; Pandemics ; Phylogeny ; Proteome ; Mutation ; Pangolins
    Chemical Substances Proteome
    Language English
    Publishing date 2023-07-26
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v15081628
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Structural flexibility of Toscana virus nucleoprotein in the presence of a single-chain camelid antibody.

    Papageorgiou, Nicolas / Baklouti, Amal / Lichière, Julie / Desmyter, Aline / Canard, Bruno / Coutard, Bruno / Ferron, François

    Acta crystallographica. Section D, Structural biology

    2024  Volume 80, Issue Pt 2, Page(s) 113–122

    Abstract: Phenuiviridae nucleoprotein is the main structural and functional component of the viral cycle, protecting the viral RNA and mediating the essential replication/transcription processes. The nucleoprotein (N) binds the RNA using its globular core and ... ...

    Abstract Phenuiviridae nucleoprotein is the main structural and functional component of the viral cycle, protecting the viral RNA and mediating the essential replication/transcription processes. The nucleoprotein (N) binds the RNA using its globular core and polymerizes through the N-terminus, which is presented as a highly flexible arm, as demonstrated in this article. The nucleoprotein exists in an `open' or a `closed' conformation. In the case of the closed conformation the flexible N-terminal arm folds over the RNA-binding cleft, preventing RNA adsorption. In the open conformation the arm is extended in such a way that both RNA adsorption and N polymerization are possible. In this article, single-crystal X-ray diffraction and small-angle X-ray scattering were used to study the N protein of Toscana virus complexed with a single-chain camelid antibody (VHH) and it is shown that in the presence of the antibody the nucleoprotein is unable to achieve a functional assembly to form a ribonucleoprotein complex.
    MeSH term(s) Nucleoproteins/chemistry ; Sandfly fever Naples virus/genetics ; Sandfly fever Naples virus/metabolism ; Nucleocapsid Proteins/chemistry ; Models, Molecular ; RNA, Viral/chemistry ; RNA, Viral/metabolism
    Chemical Substances Nucleoproteins ; Nucleocapsid Proteins ; RNA, Viral
    Language English
    Publishing date 2024-01-24
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2968623-4
    ISSN 2059-7983 ; 0907-4449
    ISSN (online) 2059-7983
    ISSN 0907-4449
    DOI 10.1107/S2059798324000196
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: The WHO mission report struggles to trace the origins of the SARS-CoV-2 epidemic.

    Decroly, Etienne / Claverie, Jean-Michel / Canard, Bruno

    Virologie (Montrouge, France)

    2021  Volume 25, Issue 3, Page(s) 42–46

    MeSH term(s) COVID-19 ; Epidemics ; Humans ; SARS-CoV-2 ; World Health Organization
    Language English
    Publishing date 2021-05-25
    Publishing country France
    Document type Journal Article
    ZDB-ID 2118387-9
    ISSN 1950-6961 ; 1267-8694
    ISSN (online) 1950-6961
    ISSN 1267-8694
    DOI 10.1684/vir.2021.0902
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Le rapport de la mission OMS peine à retracer les origines de l’épidémie de SARS-CoV-2.

    Decroly, Etienne / Claverie, Jean-Michel / Canard, Bruno

    Virologie (Montrouge, France)

    2021  Volume 25, Issue 3, Page(s) 148–152

    Title translation The WHO mission report struggles to trace the origins of the SARS-CoV-2 epidemic.
    MeSH term(s) COVID-19 ; Epidemics ; Humans ; SARS-CoV-2 ; World Health Organization
    Language French
    Publishing date 2021-05-21
    Publishing country France
    Document type Journal Article
    ZDB-ID 2118387-9
    ISSN 1950-6961 ; 1267-8694
    ISSN (online) 1950-6961
    ISSN 1267-8694
    DOI 10.1684/vir.2021.0901
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: The enzymes for genome size increase and maintenance of large (+)RNA viruses.

    Ferron, François / Sama, Bhawna / Decroly, Etienne / Canard, Bruno

    Trends in biochemical sciences

    2021  Volume 46, Issue 11, Page(s) 866–877

    Abstract: With sizes <50 kb, viral RNA genomes are at the crossroads of genetic, biophysical, and biochemical stability in their host cell. Here, we analyze the enzymatic assets accompanying large RNA genome viruses, mostly based on recent scientific advances in ... ...

    Abstract With sizes <50 kb, viral RNA genomes are at the crossroads of genetic, biophysical, and biochemical stability in their host cell. Here, we analyze the enzymatic assets accompanying large RNA genome viruses, mostly based on recent scientific advances in Coronaviridae. We argue that, in addition to the presence of an RNA exonuclease (ExoN), two markers for the large size of viral RNA genomes are (i) the presence of one or more RNA methyltransferases (MTases) and (ii) a specific architecture of the RNA-dependent RNA polymerase active site. We propose that RNA genome expansion and maintenance are driven by an evolutionary ménage-à-trois made of fast and processive RNA polymerases, RNA repair ExoNs, and RNA MTases that relates to the transition between RNA- to DNA-based life.
    MeSH term(s) Amino Acid Sequence ; Genome Size ; Methyltransferases ; RNA Viruses/genetics ; RNA, Viral/genetics
    Chemical Substances RNA, Viral ; Methyltransferases (EC 2.1.1.-)
    Language English
    Publishing date 2021-06-23
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 194216-5
    ISSN 1362-4326 ; 0968-0004 ; 0376-5067
    ISSN (online) 1362-4326
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2021.05.006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1207: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  8. Article ; Online: N

    Ahmed-Belkacem, Rostom / Troussier, Joris / Delpal, Adrien / Canard, Bruno / Vasseur, Jean-Jacques / Decroly, Etienne / Debart, Françoise

    RSC medicinal chemistry

    2024  Volume 15, Issue 3, Page(s) 839–847

    Abstract: RNA cap methylations have been shown to be crucial for the life cycle, replication, and infection of ssRNA viruses, as well as for evading the host's innate immune system. Viral methyltransferases (MTases) therefore represent an attractive target for the ...

    Abstract RNA cap methylations have been shown to be crucial for the life cycle, replication, and infection of ssRNA viruses, as well as for evading the host's innate immune system. Viral methyltransferases (MTases) therefore represent an attractive target for the development of compounds as tools and inhibitors. In coronaviruses,
    Language English
    Publishing date 2024-01-26
    Publishing country England
    Document type Journal Article
    ISSN 2632-8682
    ISSN (online) 2632-8682
    DOI 10.1039/d3md00737e
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Biophysical and structural study of La Crosse virus endonuclease inhibition for the development of new antiviral options.

    Feracci, Mikael / Hernandez, Sergio / Garlatti, Laura / Mondielli, Clemence / Vincentelli, Renaud / Canard, Bruno / Reguera, Juan / Ferron, François / Alvarez, Karine

    IUCrJ

    2024  

    Abstract: The large Bunyavirales order includes several families of viruses with a segmented ambisense (-) RNA genome and a cytoplasmic life cycle that starts by synthesizing viral mRNA. The initiation of transcription, which is common to all members, relies on an ...

    Abstract The large Bunyavirales order includes several families of viruses with a segmented ambisense (-) RNA genome and a cytoplasmic life cycle that starts by synthesizing viral mRNA. The initiation of transcription, which is common to all members, relies on an endonuclease activity that is responsible for cap-snatching. In La Crosse virus, an orthobunyavirus, it has previously been shown that the cap-snatching endonuclease resides in the N-terminal domain of the L protein. Orthobunyaviruses are transmitted by arthropods and cause diseases in cattle. However, California encephalitis virus, La Crosse virus and Jamestown Canyon virus are North American species that can cause encephalitis in humans. No vaccines or antiviral drugs are available. In this study, three known Influenza virus endonuclease inhibitors (DPBA, L-742,001 and baloxavir) were repurposed on the La Crosse virus endonuclease. Their inhibition was evaluated by fluorescence resonance energy transfer and their mode of binding was then assessed by differential scanning fluorimetry and microscale thermophoresis. Finally, two crystallographic structures were obtained in complex with L-742,001 and baloxavir, providing access to the structural determinants of inhibition and offering key information for the further development of Bunyavirales endonuclease inhibitors.
    Language English
    Publishing date 2024-05-01
    Publishing country England
    Document type Journal Article
    ZDB-ID 2754953-7
    ISSN 2052-2525 ; 2052-2525
    ISSN (online) 2052-2525
    ISSN 2052-2525
    DOI 10.1107/S205225252400304X
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: The enzymes for genome size increase and maintenance of large (+)RNA viruses

    Ferron, François / Sama, Bhawna / Decroly, Etienne / Canard, Bruno

    Trends in biochemical sciences. 2021 Nov., v. 46, no. 11

    2021  

    Abstract: With sizes <50 kb, viral RNA genomes are at the crossroads of genetic, biophysical, and biochemical stability in their host cell. Here, we analyze the enzymatic assets accompanying large RNA genome viruses, mostly based on recent scientific advances in ... ...

    Abstract With sizes <50 kb, viral RNA genomes are at the crossroads of genetic, biophysical, and biochemical stability in their host cell. Here, we analyze the enzymatic assets accompanying large RNA genome viruses, mostly based on recent scientific advances in Coronaviridae. We argue that, in addition to the presence of an RNA exonuclease (ExoN), two markers for the large size of viral RNA genomes are (i) the presence of one or more RNA methyltransferases (MTases) and (ii) a specific architecture of the RNA-dependent RNA polymerase active site. We propose that RNA genome expansion and maintenance are driven by an evolutionary ménage-à-trois made of fast and processive RNA polymerases, RNA repair ExoNs, and RNA MTases that relates to the transition between RNA- to DNA-based life.
    Keywords Coronaviridae ; RNA ; RNA-directed RNA polymerase ; active sites ; exons ; genome expansion ; methyltransferases
    Language English
    Dates of publication 2021-11
    Size p. 866-877.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 194220-7
    ISSN 0968-0004 ; 0376-5067
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2021.05.006
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 78/716: Show issues

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