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

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

2021 Volume 595, Issue 20, Page(s) 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 term(s)	Humans ; Influenza A virus/chemistry ; Protein Conformation ; Viral Matrix Proteins/chemistry
Chemical Substances	M1 protein, Influenza A virus ; Viral Matrix Proteins
Language	English
Publishing date	2021-10-02
Publishing country	England
Document type	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
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Article: 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 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.
Keywords	Influenza A virus ; RNA transport ; influenza ; ribonucleoproteins ; virion ; virus assembly ; viruses
Language	English
Dates of publication	2021-10
Size	p. 2535-2543.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	REVIEW
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1002/1873-3468.14194
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Book ; Online ; Thesis: Structural studies of influenza A virus by cryo-electron tomography

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

2020

Author's details	Julia Peukes ; Betreuer: John Briggs
Keywords	Naturwissenschaften ; Science
Subject code	sg500
Language	English
Publisher	Universitätsbibliothek Heidelberg
Publishing place	Heidelberg
Document type	Book ; Online ; Thesis
Database	Digital theses on the web

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

Peukes, Julia / Betz, Timo

Biophysical journal

2014 Volume 107, Issue 8, Page(s) 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 term(s)	Actin Cytoskeleton/chemistry ; Actin Cytoskeleton/metabolism ; Cell Line, Tumor ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Humans ; Microscopy, Interference/methods ; Surface Tension
Language	English
Publishing date	2014-10-21
Publishing country	United States
Document type	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
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Article ; 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 Volume 587, Issue 7834, Page(s) 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 term(s)	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
Chemical Substances	Viral Matrix Proteins ; Histidine (4QD397987E)
Language	English
Publishing date	2020-09-09
Publishing country	England
Document type	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
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Article ; 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 Volume 94, Issue 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 term(s)	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
Chemical Substances	Antibodies, Viral ; Hemagglutinin Glycoproteins, Influenza Virus ; Hemagglutinins ; Influenza Vaccines ; RNA (63231-63-0) ; Neuraminidase (EC 3.2.1.18)
Language	English
Publishing date	2020-07-30
Publishing country	United States
Document type	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
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Article ; 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 Volume 588, Issue 7838, Page(s) 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 term(s)	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
Chemical Substances	Antibodies, Neutralizing ; COVID-19 Vaccines ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
Keywords	covid19
Language	English
Publishing date	2020-08-17
Publishing country	England
Document type	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
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Article ; 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

Keywords	Multidisciplinary ; covid19
Language	English
Publisher	Springer Science and Business Media LLC
Publishing country	us
Document type	Article ; Online
DOI	10.1038/s41586-020-2665-2
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; 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.
Keywords	covid19
Language	English
Publishing date	2020-06-27
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2020.06.27.174979
Database	COVID19

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Article: Structures and distributions of SARS-CoV-2 spike proteins on intact virions

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.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #720838
Database	COVID19

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