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  1. Article ; Online: Cryo-electron tomography of viral infection - from applications to biosafety.

    Zimmermann, Liv / Chlanda, Petr

    Current opinion in virology

    2023  Volume 61, Page(s) 101338

    Abstract: Cellular cryo-electron tomography (cryo-ET) offers 3D snapshots at molecular resolution capturing pivotal steps during viral infection. However, tomogram quality depends on the vitrification level of the sample and its thickness. In addition, mandatory ... ...

    Abstract Cellular cryo-electron tomography (cryo-ET) offers 3D snapshots at molecular resolution capturing pivotal steps during viral infection. However, tomogram quality depends on the vitrification level of the sample and its thickness. In addition, mandatory inactivation protocols to assure biosafety when handling highly pathogenic viruses during cryo-ET can compromise sample preservation. Here, we focus on different strategies applied in cryo-ET and discuss their advantages and limitations with reference to severe acute respiratory syndrome coronavirus 2 studies. We highlight the importance of virus-like particle (VLP) and replicon systems to study virus assembly and replication in a cellular context without inactivation protocols. We discuss the application of chemical fixation and different irradiation methods in cryo-ET sample preparation and acquisition workflows.
    MeSH term(s) Humans ; Electron Microscope Tomography/methods ; Containment of Biohazards ; Cryoelectron Microscopy/methods ; COVID-19 ; Virus Diseases
    Language English
    Publishing date 2023-06-20
    Publishing country Netherlands
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 2611378-8
    ISSN 1879-6265 ; 1879-6257
    ISSN (online) 1879-6265
    ISSN 1879-6257
    DOI 10.1016/j.coviro.2023.101338
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: The Art of Viral Membrane Fusion and Penetration.

    Winter, Sophie L / Chlanda, Petr

    Sub-cellular biochemistry

    2023  Volume 106, Page(s) 113–152

    Abstract: As obligate pathogens, viruses have developed diverse mechanisms to deliver their genome across host cell membranes to sites of virus replication. While enveloped viruses utilize viral fusion proteins to accomplish fusion of their envelope with the ... ...

    Abstract As obligate pathogens, viruses have developed diverse mechanisms to deliver their genome across host cell membranes to sites of virus replication. While enveloped viruses utilize viral fusion proteins to accomplish fusion of their envelope with the cellular membrane, non-enveloped viruses rely on machinery that causes local membrane ruptures and creates an opening through which the capsid or viral genome is released. Both membrane fusion and membrane penetration take place at the plasma membrane or in intracellular compartments, often involving the engagement of the cellular machinery and antagonism of host restriction factors. Enveloped and non-enveloped viruses have evolved intricate mechanisms to enable virus uncoating and modulation of membrane fusion in a spatiotemporally controlled manner. This chapter summarizes and discusses the current state of understanding of the mechanisms of viral membrane fusion and penetration. The focus is on the role of lipids, viral scaffold uncoating, viral membrane fusion inhibitors, and host restriction factors as physicochemical modulators. In addition, recent advances in visualizing and detecting viral membrane fusion and penetration using cryo-electron microscopy methods are presented.
    MeSH term(s) Virus Internalization ; Cryoelectron Microscopy/methods ; Viruses/genetics ; Viruses/metabolism ; Cell Membrane/metabolism ; Membrane Fusion
    Language English
    Publishing date 2023-12-30
    Publishing country United States
    Document type Journal Article
    ISSN 0306-0225 ; 0096-8757
    ISSN 0306-0225 ; 0096-8757
    DOI 10.1007/978-3-031-40086-5_4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Influenza Hemagglutinin and M2 ion channel priming by trypsin: Killing two birds with one stone.

    Chlanda, Petr

    Virology

    2017  Volume 509, Page(s) 131–132

    Abstract: Influenza A virus membrane fusion and disassembly, prerequisite processes for viral infectivity, depend on acidic pH. In a recent study, Zhirnov et al. reported an important finding-that influenza virions are not permeable to protons unless the ... ...

    Abstract Influenza A virus membrane fusion and disassembly, prerequisite processes for viral infectivity, depend on acidic pH. In a recent study, Zhirnov et al. reported an important finding-that influenza virions are not permeable to protons unless the hemagglutinin (HA) fusion protein is primed by trypsin cleavage. This raises the question of whether in the viral context the M2 ion channel requires priming prior to its activation by low pH. Here, it is hypothesized that both HA and M2 ion channel direct priming by trypsin is required for their sensitization by low pH.
    MeSH term(s) Hemagglutinin Glycoproteins, Influenza Virus/metabolism ; Host-Pathogen Interactions ; Hydrogen-Ion Concentration ; Trypsin/metabolism ; Viral Matrix Proteins/metabolism
    Chemical Substances Hemagglutinin Glycoproteins, Influenza Virus ; Viral Matrix Proteins ; Trypsin (EC 3.4.21.4)
    Language English
    Publishing date 2017-06-21
    Publishing country United States
    Document type Letter ; Comment
    ZDB-ID 200425-2
    ISSN 1096-0341 ; 0042-6822
    ISSN (online) 1096-0341
    ISSN 0042-6822
    DOI 10.1016/j.virol.2017.06.011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.172: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: Dual-axis Volta phase plate cryo-electron tomography of Ebola virus-like particles reveals actin-VP40 interactions.

    Winter, Sophie L / Chlanda, Petr

    Journal of structural biology

    2021  Volume 213, Issue 2, Page(s) 107742

    Abstract: Cryo-electron tomography (cryo-ET) is a pivotal imaging technique for studying the structure of pleomorphic enveloped viruses and their interactions with the host at native conditions. Owing to the limited tilting range of samples with a slab geometry, ... ...

    Abstract Cryo-electron tomography (cryo-ET) is a pivotal imaging technique for studying the structure of pleomorphic enveloped viruses and their interactions with the host at native conditions. Owing to the limited tilting range of samples with a slab geometry, electron tomograms suffer from so-called missing wedge information in Fourier space. In dual-axis cryo-ET, two tomograms reconstructed from orthogonally oriented tilt series are combined into a tomogram with improved resolution as the missing wedge information is reduced to a pyramid. Volta phase plate (VPP) allows to perform in-focus cryo-ET with high contrast transfer at low-resolution frequencies and thus its application may improve the quality of dual-axis tomograms. Here, we compare dual-axis cryo-ET with and without VPP on Ebola virus-like particles to visualize and segment viral and host cell proteins within the membrane-enveloped filamentous particles. Dual-axis VPP cryo-ET reduces the missing wedge information and ray artifacts arising from the weighted back-projection during tomogram reconstruction, thereby minimizing ambiguity in the analysis of crowded environments and facilitating 3D segmentation. We show that dual-axis VPP tomograms provide a comprehensive description of macromolecular organizations such as nucleocapsid assembly states, the distribution of glycoproteins on the viral envelope and asymmetric arrangements of the VP40 layer in non-filamentous regions of virus-like particles. Our data reveal actin filaments within virus-like particles in close proximity to the viral VP40 scaffold, suggesting a direct interaction between VP40 and actin filaments. Dual-axis VPP cryo-ET provides more complete 3D information at high contrast and allows for better interpretation of macromolecule interactions and pleomorphic organizations.
    MeSH term(s) Actins/chemistry ; Actins/metabolism ; Cell Membrane ; Cryoelectron Microscopy/methods ; Ebolavirus/chemistry ; Ebolavirus/metabolism ; Ebolavirus/ultrastructure ; Electron Microscope Tomography/methods ; HEK293 Cells ; Hemorrhagic Fever, Ebola/pathology ; Hemorrhagic Fever, Ebola/virology ; Host-Pathogen Interactions ; Humans ; Imaging, Three-Dimensional ; Nucleocapsid/chemistry ; Viral Matrix Proteins/chemistry ; Viral Matrix Proteins/metabolism
    Chemical Substances Actins ; VP40 protein, virus ; Viral Matrix Proteins
    Language English
    Publishing date 2021-05-08
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1032718-6
    ISSN 1095-8657 ; 1047-8477
    ISSN (online) 1095-8657
    ISSN 1047-8477
    DOI 10.1016/j.jsb.2021.107742
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1428: 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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  5. Book ; Online ; Thesis: Structural characterization of Ebola virus uncoating

    Winter, Sophie L. [Verfasser] / Chlanda, Petr [Akademischer Betreuer]

    2023  

    Author's details Sophie Luise Winter ; Betreuer: Petr Chlanda
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Language English
    Publisher Universitätsbibliothek Heidelberg
    Publishing place Heidelberg
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

    Full text online

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  6. Article ; Online: Ebola virus inclusion bodies are liquid organelles whose formation is facilitated by nucleoprotein oligomerization.

    Bodmer, Bianca S / Vallbracht, Melina / Ushakov, Dmitry S / Wendt, Lisa / Chlanda, Petr / Hoenen, Thomas

    Emerging microbes & infections

    2023  Volume 12, Issue 2, Page(s) 2223727

    Abstract: Viral RNA synthesis of several non-segmented, negative-sense RNA viruses (NNSVs) takes place in inclusion bodies (IBs) that show properties of liquid organelles, which are formed by liquid-liquid phase separation of scaffold proteins. It is believed that ...

    Abstract Viral RNA synthesis of several non-segmented, negative-sense RNA viruses (NNSVs) takes place in inclusion bodies (IBs) that show properties of liquid organelles, which are formed by liquid-liquid phase separation of scaffold proteins. It is believed that this is driven by intrinsically disordered regions (IDRs) and/or multiple copies of interaction domains, which for NNSVs are usually located in their nucleo - and phosphoproteins. In contrast to other NNSVs, the Ebola virus (EBOV) nucleoprotein NP alone is sufficient to form IBs without the need for a phosphoprotein, and to facilitate the recruitment of other viral proteins into these structures. While it has been proposed that also EBOV IBs are liquid organelles, this has so far not been formally demonstrated. Here we used a combination of live cell microscopy, fluorescence recovery after photobleaching assays, and mutagenesis approaches together with reverse genetics-based generation of recombinant viruses to study the formation of EBOV IBs. Our results demonstrate that EBOV IBs are indeed liquid organelles, and that oligomerization but not IDRs of the EBOV nucleoprotein plays a key role in their formation. Additionally, VP35 (often considered the phosphoprotein-equivalent of EBOV) is not essential for IB formation, but alters their liquid behaviour. These findings define the molecular mechanism for the formation of EBOV IBs, which play a central role in the life cycle of this deadly virus.
    MeSH term(s) Humans ; Ebolavirus/genetics ; Hemorrhagic Fever, Ebola ; Inclusion Bodies ; Nucleoproteins/genetics ; Phosphoproteins/genetics
    Chemical Substances Nucleoproteins ; Phosphoproteins
    Language English
    Publishing date 2023-06-12
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2681359-2
    ISSN 2222-1751 ; 2222-1751
    ISSN (online) 2222-1751
    ISSN 2222-1751
    DOI 10.1080/22221751.2023.2223727
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  7. Article ; Online: Cryo-electron tomography of influenza A and Ebola virus cell infection

    Amorim, Maria Joao / Vallbracht, Melina / Wachsmuth-Melm, Moritz / Chlanda, Petr* / Hoenen, Thomas

    2023  

    Keywords abstract_or_summary ; Text ; ddc:570
    Language English
    Publishing date 2023-10-09
    Publisher Cold Spring Harbor Laboratory
    Publishing country de
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: Structural insights into the Ebola virus nucleocapsid assembly cascade by in-cell cryoelectron tomography

    Vallbracht, Melina* / Bodmer, Bianca Susanne / Fischer, Konstantin / Winter, Sophie L. / Hoenen, Thomas / Chlanda, Petr

    [Vortrag]

    2023  

    Keywords abstract_or_summary ; Text ; ddc:570
    Language English
    Publishing date 2023-03-29
    Publisher Cold Spring Harbor Laboratory
    Publishing country de
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: Glucosylceramide in bunyavirus particles is essential for virus binding to host cells.

    Uckeley, Zina M / Duboeuf, Maëva / Gu, Yu / Erny, Alexandra / Mazelier, Magalie / Lüchtenborg, Christian / Winter, Sophie L / Schad, Paulina / Mathieu, Cyrille / Koch, Jana / Boulant, Steeve / Chlanda, Petr / Maisse, Carine / Brügger, Britta / Lozach, Pierre-Yves

    Cellular and molecular life sciences : CMLS

    2024  Volume 81, Issue 1, Page(s) 71

    Abstract: Hexosylceramides (HexCer) are implicated in the infection process of various pathogens. However, the molecular and cellular functions of HexCer in infectious cycles are poorly understood. Investigating the enveloped virus Uukuniemi (UUKV), a bunyavirus ... ...

    Abstract Hexosylceramides (HexCer) are implicated in the infection process of various pathogens. However, the molecular and cellular functions of HexCer in infectious cycles are poorly understood. Investigating the enveloped virus Uukuniemi (UUKV), a bunyavirus of the Phenuiviridae family, we performed a lipidomic analysis with mass spectrometry and determined the lipidome of both infected cells and derived virions. We found that UUKV alters the processing of HexCer to glycosphingolipids (GSL) in infected cells. The infection resulted in the overexpression of glucosylceramide (GlcCer) synthase (UGCG) and the specific accumulation of GlcCer and its subsequent incorporation into viral progeny. UUKV and several pathogenic bunyaviruses relied on GlcCer in the viral envelope for binding to various host cell types. Overall, our results indicate that GlcCer is a structural determinant of virions crucial for bunyavirus infectivity. This study also highlights the importance of glycolipids on virions in facilitating interactions with host cell receptors and infectious entry of enveloped viruses.
    MeSH term(s) Orthobunyavirus ; Glucosylceramides ; Virus Attachment ; Lipidomics ; Mass Spectrometry
    Chemical Substances Glucosylceramides
    Language English
    Publishing date 2024-02-01
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 1358415-7
    ISSN 1420-9071 ; 1420-682X
    ISSN (online) 1420-9071
    ISSN 1420-682X
    DOI 10.1007/s00018-023-05103-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 195: 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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  10. Article ; Online: SARS-CoV-2 nsp3 and nsp4 are minimal constituents of a pore spanning replication organelle.

    Zimmermann, Liv / Zhao, Xiaohan / Makroczyova, Jana / Wachsmuth-Melm, Moritz / Prasad, Vibhu / Hensel, Zach / Bartenschlager, Ralf / Chlanda, Petr

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 7894

    Abstract: Coronavirus replication is associated with the remodeling of cellular membranes, resulting in the formation of double-membrane vesicles (DMVs). A DMV-spanning pore was identified as a putative portal for viral RNA. However, the exact components and the ... ...

    Abstract Coronavirus replication is associated with the remodeling of cellular membranes, resulting in the formation of double-membrane vesicles (DMVs). A DMV-spanning pore was identified as a putative portal for viral RNA. However, the exact components and the structure of the SARS-CoV-2 DMV pore remain to be determined. Here, we investigate the structure of the DMV pore by in situ cryo-electron tomography combined with subtomogram averaging. We identify non-structural protein (nsp) 3 and 4 as minimal components required for the formation of a DMV-spanning pore, which is dependent on nsp3-4 proteolytic cleavage. In addition, we show that Mac2-Mac3-DPUP-Ubl2 domains are critical for nsp3 oligomerization and crown integrity which influences membrane curvature required for biogenesis of DMVs. Altogether, SARS-CoV-2 nsp3-4 have a dual role by driving the biogenesis of replication organelles and assembly of DMV-spanning pores which we propose here to term replicopores.
    MeSH term(s) Humans ; SARS-CoV-2/metabolism ; Virus Replication ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism ; COVID-19 ; Organelles/metabolism
    Chemical Substances Viral Nonstructural Proteins
    Language English
    Publishing date 2023-11-30
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-43666-5
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