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  1. Article ; Online: Disruption of influenza virus packaging signals results in various misassembled genome complexes.

    Girard, Justine / Jakob, Celia / Toews, Lina Kathrin / Fuchs, Jonas / Pohlmann, Anne / Franzke, Kati / Kolesnikova, Larissa / Jeney, Csaba / Beer, Martin / Bron, Patrick / Schwemmle, Martin / Bolte, Hardin

    Journal of virology

    2023  Volume 97, Issue 10, Page(s) e0107623

    Abstract: Importance: The influenza A virus genome consists of eight distinct viral RNAs (vRNAs) that are typically packaged into a single virion as an octameric complex. How this genome complex is assembled and incorporated into the virion is poorly understood, ... ...

    Abstract Importance: The influenza A virus genome consists of eight distinct viral RNAs (vRNAs) that are typically packaged into a single virion as an octameric complex. How this genome complex is assembled and incorporated into the virion is poorly understood, but previous research suggests a coordinative role for packaging signals present in all vRNAs. Here, we show that disruption of two packaging signals in a model H7N7 influenza A virus results in a mixture of virions with unusual vRNA content, including empty virions, virions with one to four vRNAs, and virions with octameric complexes composed of vRNA duplicates. Our results suggest that (i) the assembly of error-free octameric complexes proceeds through a series of defined vRNA sub-complexes and (ii) virions can bud without incorporating complete octameric complexes.
    MeSH term(s) Genome, Viral ; Influenza A virus/genetics ; Influenza A Virus, H7N7 Subtype/genetics ; RNA, Viral/genetics ; Viral Genome Packaging ; Virion/genetics ; Virus Assembly
    Chemical Substances RNA, Viral
    Language English
    Publishing date 2023-10-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/jvi.01076-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Evolutionarily conserved amino acids in MHC-II mediate bat influenza A virus entry into human cells.

    Olajide, Okikiola M / Osman, Maria Kaukab / Robert, Jonathan / Kessler, Susanne / Toews, Lina Kathrin / Thamamongood, Thiprampai / Neefjes, Jacques / Wrobel, Antoni G / Schwemmle, Martin / Ciminski, Kevin / Reuther, Peter

    PLoS biology

    2023  Volume 21, Issue 7, Page(s) e3002182

    Abstract: The viral hemagglutinins of conventional influenza A viruses (IAVs) bind to sialylated glycans on host cell surfaces for attachment and subsequent infection. In contrast, hemagglutinins of bat-derived IAVs target major histocompatibility complex class II ...

    Abstract The viral hemagglutinins of conventional influenza A viruses (IAVs) bind to sialylated glycans on host cell surfaces for attachment and subsequent infection. In contrast, hemagglutinins of bat-derived IAVs target major histocompatibility complex class II (MHC-II) for cell entry. MHC-II proteins from various vertebrate species can facilitate infection with the bat IAV H18N11. Yet, it has been difficult to biochemically determine the H18:MHC-II binding. Here, we followed a different approach and generated MHC-II chimeras from the human leukocyte antigen DR (HLA-DR), which supports H18-mediated entry, and the nonclassical MHC-II molecule HLA-DM, which does not. In this context, viral entry was supported only by a chimera containing the HLA-DR α1, α2, and β1 domains. Subsequent modeling of the H18:HLA-DR interaction identified the α2 domain as central for this interaction. Further mutational analyses revealed highly conserved amino acids within loop 4 (N149) and β-sheet 6 (V190) of the α2 domain as critical for virus entry. This suggests that conserved residues in the α1, α2, and β1 domains of MHC-II mediate H18-binding and virus propagation. The conservation of MHC-II amino acids, which are critical for H18N11 binding, may explain the broad species specificity of this virus.
    MeSH term(s) Animals ; Humans ; Influenza A virus ; Chiroptera ; Amino Acids ; Histocompatibility Antigens Class II ; HLA-DR Antigens/metabolism ; HLA Antigens
    Chemical Substances Amino Acids ; Histocompatibility Antigens Class II ; HLA-DR Antigens ; HLA Antigens
    Language English
    Publishing date 2023-07-06
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2126776-5
    ISSN 1545-7885 ; 1544-9173
    ISSN (online) 1545-7885
    ISSN 1544-9173
    DOI 10.1371/journal.pbio.3002182
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6193: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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  3. Article ; Online: Disruption of influenza virus packaging signals results in various misassembled genome complexes ; Gestörte Verpackungssignale des Influenzavirus - falsch zusammengesetzte Genomkomplexe

    Girard, Justine / Jakob, Celia / Toews, Lina Kathrin / Fuchs, Jonas / Pohlmann, Anne / Franzke, Kati / Kolesnikova, Larissa / Jeney, Csaba / Beer, Martin / Bron, Patrick / Schwemmle, Martin / Bolte, Hardin

    2023  

    Abstract: The eight different genomic viral RNAs (vRNAs) of influenza A virus are typically packaged into virions as a (7 + 1) complex of seven viral ribonucleoproteins (vRNPs) around a central vRNP. Mutations in the packaging signals of these vRNAs are predicted ... ...

    Abstract The eight different genomic viral RNAs (vRNAs) of influenza A virus are typically packaged into virions as a (7 + 1) complex of seven viral ribonucleoproteins (vRNPs) around a central vRNP. Mutations in the packaging signals of these vRNAs are predicted to result in virions lacking specific vRNPs. However, whether these vRNPs are then replaced by vRNP-like host RNAs is an open question. Here, we report that mutations in two packaging signals of influenza A/SC35M virus, which cause the near-complete loss of four vRNAs from the total virion population, result in several distinct virion subpopulations with unusual vRNP content. Half of the virions analyzed are empty or contain incomplete genome complexes with one to four vRNPs. Unexpectedly, most other virions contain atypical (7 + 1) complexes consisting of multiple copies of the four efficiently packaged vRNAs, but no host RNAs. The reported set of misassembled genome complexes suggests that packaging signals coordinate a modular genome assembly process. IMPORTANCE The influenza A virus genome consists of eight distinct viral RNAs (vRNAs) that are typically packaged into a single virion as an octameric complex. How this genome complex is assembled and incorporated into the virion is poorly understood, but previous research suggests a coordinative role for packaging signals present in all vRNAs. Here, we show that disruption of two packaging signals in a model H7N7 influenza A virus results in a mixture of virions with unusual vRNA content, including empty virions, virions with one to four vRNAs, and virions with octameric complexes composed of vRNA duplicates. Our results suggest that (i) the assembly of error-free octameric complexes proceeds through a series of defined vRNA sub-complexes and (ii) virions can bud without incorporating complete octameric complexes.
    Keywords article ; Text ; ddc:570 ; RNA sequencing -- electron tomography -- genome packaging -- packaging mutant -- ribonucleoproteins -- self-assembly
    Subject code 612
    Language English
    Publishing date 2023-10-09
    Publisher American Society for Microbiology
    Publishing country de
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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