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  1. Artikel ; Online: New structural insights into the multifunctional influenza A matrix protein 1.

    Peukes, Julia / Xiong, Xiaoli / Briggs, John A G

    FEBS letters

    2021  Band 595, Heft 20, Seite(n) 2535–2543

    Abstract: Influenza A virus matrix protein 1 (M1) is the most abundant protein within virions and functions at multiple steps of the virus life cycle, including nuclear RNA export, virus particle assembly, and virus disassembly. Two recent publications have ... ...

    Abstract Influenza A virus matrix protein 1 (M1) is the most abundant protein within virions and functions at multiple steps of the virus life cycle, including nuclear RNA export, virus particle assembly, and virus disassembly. Two recent publications have presented the first structures of full-length M1 and show that it assembles filaments in vitro via an interface between the N- and C-terminal domains of adjacent monomers. These filaments were found to be similar to those that form the endoskeleton of assembled virions. The structures provide a molecular basis to understand the functions of M1 during the virus life cycle. Here, we compare and discuss the two structures, and explore their implications for the mechanisms by which the multifunctional M1 protein can mediate virus assembly, interact with viral ribonucleoproteins and act during infection of a new cell.
    Mesh-Begriff(e) Humans ; Influenza A virus/chemistry ; Protein Conformation ; Viral Matrix Proteins/chemistry
    Chemische Substanzen M1 protein, Influenza A virus ; Viral Matrix Proteins
    Sprache Englisch
    Erscheinungsdatum 2021-10-02
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.14194
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel: New structural insights into the multifunctional influenza A matrix protein 1

    Peukes, Julia / Xiong, Xiaoli / Briggs, John A. G.

    FEBS letters. 2021 Oct., v. 595, no. 20

    2021  

    Abstract: Influenza A virus matrix protein 1 (M1) is the most abundant protein within virions and functions at multiple steps of the virus life cycle, including nuclear RNA export, virus particle assembly, and virus disassembly. Two recent publications have ... ...

    Abstract Influenza A virus matrix protein 1 (M1) is the most abundant protein within virions and functions at multiple steps of the virus life cycle, including nuclear RNA export, virus particle assembly, and virus disassembly. Two recent publications have presented the first structures of full‐length M1 and show that it assembles filaments in vitro via an interface between the N‐ and C‐terminal domains of adjacent monomers. These filaments were found to be similar to those that form the endoskeleton of assembled virions. The structures provide a molecular basis to understand the functions of M1 during the virus life cycle. Here, we compare and discuss the two structures, and explore their implications for the mechanisms by which the multifunctional M1 protein can mediate virus assembly, interact with viral ribonucleoproteins and act during infection of a new cell.
    Schlagwörter Influenza A virus ; RNA transport ; influenza ; ribonucleoproteins ; virion ; virus assembly ; viruses
    Sprache Englisch
    Erscheinungsverlauf 2021-10
    Umfang p. 2535-2543.
    Erscheinungsort John Wiley & Sons, Ltd
    Dokumenttyp Artikel
    Anmerkung REVIEW
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.14194
    Datenquelle NAL Katalog (AGRICOLA)

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  3. Buch ; Online ; Dissertation / Habilitation: Structural studies of influenza A virus by cryo-electron tomography

    Peukes, Julia [Verfasser] / Briggs, John [Akademischer Betreuer]

    2020  

    Verfasserangabe Julia Peukes ; Betreuer: John Briggs
    Schlagwörter Naturwissenschaften ; Science
    Thema/Rubrik (Code) sg500
    Sprache Englisch
    Verlag Universitätsbibliothek Heidelberg
    Erscheinungsort Heidelberg
    Dokumenttyp Buch ; Online ; Dissertation / Habilitation
    Datenquelle Digitale Dissertationen im Internet

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  4. Artikel ; Online: Direct measurement of the cortical tension during the growth of membrane blebs.

    Peukes, Julia / Betz, Timo

    Biophysical journal

    2014  Band 107, Heft 8, Seite(n) 1810–1820

    Abstract: Mechanics is at the heart of many cellular processes and its importance has received considerable attention during the last two decades. In particular, the tension of cell membranes, and more specifically of the cell cortex, is a key parameter that ... ...

    Abstract Mechanics is at the heart of many cellular processes and its importance has received considerable attention during the last two decades. In particular, the tension of cell membranes, and more specifically of the cell cortex, is a key parameter that determines the mechanical behavior of the cell periphery. However, the measurement of tension remains challenging due to its dynamic nature. Here we show that a noninvasive interferometric technique can reveal time-resolved effective tension measurements by a high-accuracy determination of edge fluctuations in expanding cell blebs of filamin-deficient melanoma cells. The introduced technique shows that the bleb tension is ~10-100 pN/μm and increases during bleb growth. Our results directly confirm that the subsequent stop of bleb growth is induced by an increase of measured tension, possibly mediated by the repolymerized actin cytoskeleton.
    Mesh-Begriff(e) Actin Cytoskeleton/chemistry ; Actin Cytoskeleton/metabolism ; Cell Line, Tumor ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Humans ; Microscopy, Interference/methods ; Surface Tension
    Sprache Englisch
    Erscheinungsdatum 2014-10-21
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2014.07.076
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: The native structure of the assembled matrix protein 1 of influenza A virus.

    Peukes, Julia / Xiong, Xiaoli / Erlendsson, Simon / Qu, Kun / Wan, William / Calder, Leslie J / Schraidt, Oliver / Kummer, Susann / Freund, Stefan M V / Kräusslich, Hans-Georg / Briggs, John A G

    Nature

    2020  Band 587, Heft 7834, Seite(n) 495–498

    Abstract: Influenza A virus causes millions of severe cases of disease during annual epidemics. The most abundant protein in influenza virions is matrix protein 1 (M1), which mediates virus assembly by forming an endoskeleton beneath the virus ... ...

    Abstract Influenza A virus causes millions of severe cases of disease during annual epidemics. The most abundant protein in influenza virions is matrix protein 1 (M1), which mediates virus assembly by forming an endoskeleton beneath the virus membrane
    Mesh-Begriff(e) Animals ; Cryoelectron Microscopy ; Dogs ; HEK293 Cells ; Histidine ; Humans ; Hydrogen-Ion Concentration ; Influenza A Virus, H3N2 Subtype/chemistry ; Influenza A Virus, H3N2 Subtype/metabolism ; Influenza A Virus, H3N2 Subtype/ultrastructure ; Madin Darby Canine Kidney Cells ; Models, Molecular ; Viral Matrix Proteins/chemistry ; Viral Matrix Proteins/metabolism ; Viral Matrix Proteins/ultrastructure ; Virion/chemistry ; Virion/metabolism ; Virion/ultrastructure
    Chemische Substanzen Viral Matrix Proteins ; Histidine (4QD397987E)
    Sprache Englisch
    Erscheinungsdatum 2020-09-09
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-020-2696-8
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: Enhancing Neuraminidase Immunogenicity of Influenza A Viruses by Rewiring RNA Packaging Signals.

    Zheng, Allen / Sun, Weina / Xiong, Xiaoli / Freyn, Alec W / Peukes, Julia / Strohmeier, Shirin / Nachbagauer, Raffael / Briggs, John A G / Krammer, Florian / Palese, Peter

    Journal of virology

    2020  Band 94, Heft 16

    Abstract: Humoral immune protection against influenza virus infection is mediated largely by antibodies against hemagglutinin (HA) and neuraminidase (NA), the two major glycoproteins on the virus surface. While influenza virus vaccination efforts have focused ... ...

    Abstract Humoral immune protection against influenza virus infection is mediated largely by antibodies against hemagglutinin (HA) and neuraminidase (NA), the two major glycoproteins on the virus surface. While influenza virus vaccination efforts have focused mainly on HA, NA-based immunity has been shown to reduce disease severity and provide heterologous protection. Current seasonal vaccines do not elicit strong anti-NA responses-in part due to the immunodominance of the HA protein. Here, we demonstrate that by swapping the 5' and 3' terminal packaging signals of the HA and NA genomic segments, which contain the RNA promoters, we are able to rescue influenza viruses that express more NA and less HA. Vaccination with formalin-inactivated "rewired" viruses significantly enhances the anti-NA antibody response compared to vaccination with unmodified viruses. Passive transfer of sera from mice immunized with rewired virus vaccines shows better protection against influenza virus challenge. Our results provide evidence that the immunodominance of HA stems in part from its abundance on the viral surface, and that rewiring viral packaging signals-thereby increasing the NA content on viral particles-is a viable strategy for improving the immunogenicity of NA in an influenza virus vaccine.
    Mesh-Begriff(e) Animals ; Antibodies, Viral/immunology ; Cross Protection ; Cross Reactions ; Female ; Gene Expression/genetics ; Gene Expression Regulation, Viral/genetics ; HEK293 Cells ; Hemagglutinin Glycoproteins, Influenza Virus/genetics ; Hemagglutinins/immunology ; Humans ; Influenza A Virus, H1N1 Subtype/genetics ; Influenza A Virus, H3N2 Subtype/genetics ; Influenza A Virus, H5N1 Subtype/genetics ; Influenza A virus/genetics ; Influenza Vaccines/immunology ; Influenza, Human/virology ; Mice ; Mice, Inbred BALB C ; Neuraminidase/genetics ; Neuraminidase/immunology ; Orthomyxoviridae Infections/virology ; RNA/genetics ; Vaccination/methods
    Chemische Substanzen Antibodies, Viral ; Hemagglutinin Glycoproteins, Influenza Virus ; Hemagglutinins ; Influenza Vaccines ; RNA (63231-63-0) ; Neuraminidase (EC 3.2.1.18)
    Sprache Englisch
    Erscheinungsdatum 2020-07-30
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; 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.00742-20
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  7. Artikel ; Online: Structures and distributions of SARS-CoV-2 spike proteins on intact virions.

    Ke, Zunlong / Oton, Joaquin / Qu, Kun / Cortese, Mirko / Zila, Vojtech / McKeane, Lesley / Nakane, Takanori / Zivanov, Jasenko / Neufeldt, Christopher J / Cerikan, Berati / Lu, John M / Peukes, Julia / Xiong, Xiaoli / Kräusslich, Hans-Georg / Scheres, Sjors H W / Bartenschlager, Ralf / Briggs, John A G

    Nature

    2020  Band 588, Heft 7838, Seite(n) 498–502

    Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers ... ...

    Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude
    Mesh-Begriff(e) Antibodies, Neutralizing/immunology ; COVID-19/immunology ; COVID-19 Vaccines/immunology ; Cell Line, Tumor ; Cryoelectron Microscopy ; Humans ; Models, Molecular ; Pliability ; Protein Conformation ; Protein Multimerization ; SARS-CoV-2/chemistry ; SARS-CoV-2/isolation & purification ; SARS-CoV-2/metabolism ; SARS-CoV-2/ultrastructure ; Spike Glycoprotein, Coronavirus/analysis ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/isolation & purification ; Spike Glycoprotein, Coronavirus/ultrastructure ; Virion/chemistry ; Virion/isolation & purification ; Virion/metabolism ; Virion/ultrastructure
    Chemische Substanzen Antibodies, Neutralizing ; COVID-19 Vaccines ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-08-17
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-020-2665-2
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  8. Artikel ; Online: Structures and distributions of SARS-CoV-2 spike proteins on intact virions

    Ke, Zunlong / Oton, Joaquin / Qu, Kun / Cortese, Mirko / Zila, Vojtech / McKeane, Lesley / Nakane, Takanori / Zivanov, Jasenko / Neufeldt, Christopher J. / Cerikan, Berati / Lu, John M. / Peukes, Julia / Xiong, Xiaoli / Kräusslich, Hans-Georg / Scheres, Sjors H. W. / Bartenschlager, Ralf / Briggs, John A. G.

    Nature ; ISSN 0028-0836 1476-4687

    2020  

    Schlagwörter Multidisciplinary ; covid19
    Sprache Englisch
    Verlag Springer Science and Business Media LLC
    Erscheinungsland us
    Dokumenttyp Artikel ; Online
    DOI 10.1038/s41586-020-2665-2
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  9. Artikel ; Online: Structures, conformations and distributions of SARS-CoV-2 spike protein trimers on intact virions

    Ke, Zunlong / Oton, Joaquin / Qu, Kun / Cortese, Mirko / Zila, Vojtech / McKeane, Lesley / Nakane, Takanori / Zivanov, Jasenko / Neufeldt, Christopher J / Lu, John M / Peukes, Julia / Xiong, Xiaoli / Krausslich, Hans-Georg / Scheres, Sjors H.W. / Bartenschlager, Ralf / Briggs, John A.G.

    bioRxiv

    Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude. Heavily glycosylated S trimers bind the ACE2 receptor and mediate entry of virions into target cells. S ... ...

    Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude. Heavily glycosylated S trimers bind the ACE2 receptor and mediate entry of virions into target cells. S exhibits extensive conformational flexibility: it modulates the exposure of its receptor binding site and later undergoes complete structural rearrangement to drive fusion of viral and cellular membranes. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy. The structure and distribution of S on the virion surface, however, has not been characterised. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions, determining the high-resolution structure, conformational flexibility and distributions of S trimers in situ on the virion surface. These results provide a basis for understanding the conformations of S present on the virion, and for studying their interactions with neutralizing antibodies.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-06-27
    Verlag Cold Spring Harbor Laboratory
    Dokumenttyp Artikel ; Online
    DOI 10.1101/2020.06.27.174979
    Datenquelle COVID19

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  10. Artikel: Structures and distributions of SARS-CoV-2 spike proteins on intact virions

    Ke, Zunlong / Oton, Joaquin / Qu, Kun / Cortese, Mirko / Zila, Vojtech / McKeane, Lesley / Nakane, Takanori / Zivanov, Jasenko / Neufeldt, Christopher J / Cerikan, Berati / Lu, John M / Peukes, Julia / Xiong, Xiaoli / Kräusslich, Hans-Georg / Scheres, Sjors H W / Bartenschlager, Ralf / Briggs, John A G

    Nature (Lond.)

    Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude1. Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry ... ...

    Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude1. Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells2-6. S exhibits extensive conformational flexibility: it modulates exposure of its receptor-binding site and subsequently undergoes complete structural rearrangement to drive fusion of viral and cellular membranes2,7,8. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy2,7,9-12, but the structure and distribution of S on the virion surface remain unknown. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions and determine the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination.
    Schlagwörter covid19
    Verlag WHO
    Dokumenttyp Artikel
    Anmerkung WHO #Covidence: #720838
    Datenquelle COVID19

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