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Article ; Online: Fusion-active glycoprotein G mediates the cytotoxicity of vesicular stomatitis virus M mutants lacking host shut-off activity.

Hoffmann, Markus / Wu, Yuan-Ju / Gerber, Markus / Berger-Rentsch, Marianne / Heimrich, Bernd / Schwemmle, Martin / Zimmer, Gert

The Journal of general virology

2010 Volume 91, Issue Pt 11, Page(s) 2782–2793

Abstract: ... shut-off activity of the viral matrix (M) protein, which inhibits both nuclear transcription and ... nucleocytoplasmic RNA transport, thereby effectively suppressing the synthesis of type I interferon (IFN). The M ... with S226R were the host shut-off activity of the M protein abolished and IFN induced, independently of M51R ...

Abstract	The cytopathogenicity of vesicular stomatitis virus (VSV) has been attributed mainly to the host shut-off activity of the viral matrix (M) protein, which inhibits both nuclear transcription and nucleocytoplasmic RNA transport, thereby effectively suppressing the synthesis of type I interferon (IFN). The M protein from persistently VSV-infected cells was shown to harbour characteristic amino acid substitutions (M51R, V221F and S226R) implicated in IFN induction. This study demonstrates that infection of human fibroblasts with recombinant VSV containing the M51R substitution resulted in IFN induction, whereas neither the V221F nor the S226R substitution effected an IFN-inducing phenotype. Only when V221F was combined with S226R were the host shut-off activity of the M protein abolished and IFN induced, independently of M51R. The M33A substitution, previously implicated in VSV cytotoxicity, did not affect host shut-off activity. M-mutant VSV containing all four amino acid substitutions retained cytotoxic properties in both Vero cells and IFN-competent primary fibroblasts. Infected-cell death was associated with the formation of giant polynucleated cells, suggesting that the fusion activity of the VSV G protein was involved. Accordingly, M-mutant VSV expressing a fusion-defective G protein or with a deletion of the G gene showed significantly reduced cytotoxic properties and caused long-lasting infections in Vero cells and mouse hippocampal slice cultures. In contrast, a G-deleted VSV expressing wild-type M protein remained cytotoxic. These findings indicate that the host shut-off activity of the M protein dominates VSV cytotoxicty, whilst the fusion-active G protein is mainly responsible for the cytotoxicity remaining with M-mutant VSV.
MeSH term(s)	Amino Acid Sequence ; Amino Acid Substitution/genetics ; Animals ; Cells, Cultured ; Cricetinae ; Cytopathogenic Effect, Viral ; Fibroblasts/virology ; Giant Cells/virology ; Hippocampus/virology ; Humans ; Interferons/biosynthesis ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; Mice ; Molecular Sequence Data ; Mutant Proteins/genetics ; Mutant Proteins/immunology ; Mutant Proteins/toxicity ; Organ Culture Techniques ; Vesiculovirus/immunology ; Vesiculovirus/pathogenicity ; Viral Envelope Proteins/genetics ; Viral Envelope Proteins/metabolism ; Viral Matrix Proteins/genetics ; Viral Matrix Proteins/immunology ; Viral Matrix Proteins/toxicity
Chemical Substances	G protein, vesicular stomatitis virus ; M protein, Vesicular stomatitis virus ; Membrane Glycoproteins ; Mutant Proteins ; Viral Envelope Proteins ; Viral Matrix Proteins ; Interferons (9008-11-1)
Language	English
Publishing date	2010-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	219316-4
ISSN	1465-2099 ; 0022-1317
ISSN (online)	1465-2099
ISSN	0022-1317
DOI	10.1099/vir.0.023978-0
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Advocating a watch-and-prepare approach with avian influenza.

Ciminski, Kevin / Chase, Geoffrey / Schwemmle, Martin / Beer, Martin

Nature microbiology

2023 Volume 8, Issue 9, Page(s) 1603–1605

MeSH term(s)	Animals ; Influenza in Birds/prevention & control
Language	English
Publishing date	2023-08-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2058-5276
ISSN (online)	2058-5276
DOI	10.1038/s41564-023-01457-0
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Article ; Online: Anti-influenza A virus restriction factors that shape the human species barrier and virus evolution.

Petric, Philipp Peter / Schwemmle, Martin / Graf, Laura

PLoS pathogens

2023 Volume 19, Issue 7, Page(s) e1011450

MeSH term(s)	Humans ; Influenza, Human ; Host-Pathogen Interactions ; Evolution, Molecular
Language	English
Publishing date	2023-07-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1011450
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Article ; Online: Bat-Borne Influenza A Viruses: An Awakening.

Ciminski, Kevin / Schwemmle, Martin

Cold Spring Harbor perspectives in medicine

2021 Volume 11, Issue 2

Abstract: Influenza A viruses (IAVs) originating from aquatic waterfowl recurrently cross interspecies barriers, which is greatly facilitated by utilizing cell surface-exposed monosaccharide sialic acids located on vertebrate cells as a universal host cell ... ...

Abstract	Influenza A viruses (IAVs) originating from aquatic waterfowl recurrently cross interspecies barriers, which is greatly facilitated by utilizing cell surface-exposed monosaccharide sialic acids located on vertebrate cells as a universal host cell receptor. These glycan structures are first bound by the viral hemagglutinin (HA) for cell entry and then cleaved by the viral neuraminidase (NA) for particle release. In contrast, viruses of the recently identified bat-borne IAV subtypes H17N10 and H18N11 encode HA and NA homologs unable to interact with sialic acid residues despite a high degree of structural homology with their conventional counterparts. However, the most recent findings show that bat IAV HAs make use of the major histocompatibility complex class II proteins of different vertebrate species to gain entry into host cells, potentially permitting a broader host tropism. This review recapitulates current progress in the field of bat IAV research including the first assessment of the spillover potential of these bat viruses into other mammals.
MeSH term(s)	Animals ; Chiroptera/virology ; Humans ; Influenza A virus/metabolism ; Viral Tropism ; Viral Zoonoses ; Virus Replication
Language	English
Publishing date	2021-02-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	2157-1422
ISSN (online)	2157-1422
DOI	10.1101/cshperspect.a038612
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Reverse Genetics of Bat Influenza A Viruses.

Kessler, Susanne / García-Sastre, Adolfo / Schwemmle, Martin / Ciminski, Kevin

Methods in molecular biology (Clifton, N.J.)

2023 Volume 2733, Page(s) 75–86

Abstract: New World fruit bats were recently found to harbor two distinct and previously unknown influenza A viruses (IAVs) of the subtypes H17N10 and H18N11. Although viral genome sequences were detected in the liver, intestine, lung, and kidney of infected bats ... ...

Abstract	New World fruit bats were recently found to harbor two distinct and previously unknown influenza A viruses (IAVs) of the subtypes H17N10 and H18N11. Although viral genome sequences were detected in the liver, intestine, lung, and kidney of infected bats and the complete genome sequences have been isolated from their rectal swab samples, all attempts to isolate an infectious virus from bats in nature have failed. The lack of an infectious bat IAV isolate was overcome by reverse genetic approaches that led to the generation of an infectious virus in vitro. Using such synthetic bat IAVs enabled the identification of their unconventional cell entry via major histocompatibility complex II (MCH-II) molecules and their ability to replicate in mice, ferrets, and bats. Importantly, we also showed that these synthetic recombinant bat IAVs are not able to reassort with conventional IAVs, preventing the acquisition of enhanced transmission properties in non-bat species by reassortment with conventional IAVs. As authentic viruses are key for understanding the molecular biology of bat IAVs, in this chapter, we describe our recently established reverse genetics protocol for generating H17N10 and H18N11 in vitro. This step-by-step protocol starts with cloning of cDNA copies of the viral RNA segments into reverse genetics plasmids, followed by the generation of a highly concentrated stock and finally a method to determine viral titers.
MeSH term(s)	Animals ; Mice ; Influenza A virus/genetics ; Chiroptera ; Orthomyxoviridae Infections ; Reverse Genetics ; Ferrets/genetics
Language	English
Publishing date	2023-12-08
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-3533-9_5
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Article ; Online: Different but Not Unique: Deciphering the Immunity of the Jamaican Fruit Bat by Studying Its Viriome.

David, Quinnlan / Schountz, Tony / Schwemmle, Martin / Ciminski, Kevin

Viruses

2022 Volume 14, Issue 2

Abstract: A specialized and fine-tuned immune response of bats upon infection with viruses is believed to provide the basis for a "friendly" coexistence with these pathogens, which are often lethal for humans and other mammals. First insights into the immunity of ... ...

Abstract	A specialized and fine-tuned immune response of bats upon infection with viruses is believed to provide the basis for a "friendly" coexistence with these pathogens, which are often lethal for humans and other mammals. First insights into the immunity of bats suggest that bats have evolved to possess their own strategies to cope with viral infections. Yet, the molecular details for this innocuous coexistence remain poorly described and bat infection models are the key to unveiling these secrets. In Jamaican fruit bats
MeSH term(s)	Adaptive Immunity ; Animals ; Arenaviridae Infections/immunology ; Arenaviridae Infections/veterinary ; Arenaviridae Infections/virology ; Arenaviruses, New World/isolation & purification ; Chiroptera/immunology ; Chiroptera/virology ; Immunity, Innate ; Influenza A virus/isolation & purification ; Orthomyxoviridae Infections/immunology ; Orthomyxoviridae Infections/veterinary ; Rabies/immunology ; Rabies/veterinary ; Rabies/virology ; Rabies virus/isolation & purification ; Virome ; Virus Diseases/immunology ; Virus Diseases/veterinary
Language	English
Publishing date	2022-01-25
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v14020238
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Advocating a watch-and-prepare approach with avian influenza

Ciminski, Kevin / Chase, Geoffrey / Schwemmle, Martin / Beer, Martin

2023

Abstract: The global outbreak of H5N1 highly pathogenic avian influenza virus and its high toll on animal populations raise concerns about spillover into humans, but human host barriers need to be considered when estimating transmission potential. ...

Abstract	The global outbreak of H5N1 highly pathogenic avian influenza virus and its high toll on animal populations raise concerns about spillover into humans, but human host barriers need to be considered when estimating transmission potential.
Keywords	Text ; ddc:630
Language	English
Publishing date	2023-08-28
Publishing country	de
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Functionality of IAV packaging signals depends on site-specific charges within the viral nucleoprotein.

Ciminski, Kevin / Flore, Viktoria / Jakob, Celia / Mues, Helen / Smedegaard Frederiksen, Anne / Schwemmle, Martin / Bolte, Hardin / Giese, Sebastian

Journal of virology

2024 Volume 98, Issue 4, Page(s) e0197223

Abstract: The coordinated packaging of the segmented genome of the influenza A virus (IAV) into virions is an essential step of the viral life cycle. This process is controlled by the interaction of packaging signals present in all eight viral RNA (vRNA) segments ... ...

Abstract	The coordinated packaging of the segmented genome of the influenza A virus (IAV) into virions is an essential step of the viral life cycle. This process is controlled by the interaction of packaging signals present in all eight viral RNA (vRNA) segments and the viral nucleoprotein (NP), which binds vRNA via a positively charged binding groove. However, mechanistic models of how the packaging signals and NP work together to coordinate genome packaging are missing. Here, we studied genome packaging in influenza A/SC35M virus mutants that carry mutated packaging signals as well as specific amino acid substitutions at the highly conserved lysine (K) residues 184 and 229 in the RNA-binding groove of NP. Because these lysines are acetylated and thus neutrally charged in infected host cells, we replaced them with glutamine to mimic the acetylated, neutrally charged state or arginine to mimic the non-acetylated, positively charged state. Our analysis shows that the coordinated packaging of eight vRNAs is influenced by (i) the charge state of the replacing amino acid and (ii) its location within the RNA-binding groove. Accordingly, we propose that lysine acetylation induces different charge states within the RNA-binding groove of NP, thereby supporting the activity of specific packaging signals during coordinated genome packaging. Importance: Influenza A viruses (IAVs) have a segmented viral RNA (vRNA) genome encapsidated by multiple copies of the viral nucleoprotein (NP) and organized into eight distinct viral ribonucleoprotein complexes. Although genome segmentation contributes significantly to viral evolution and adaptation, it requires a highly sophisticated genome-packaging mechanism. How eight distinct genome complexes are incorporated into the virion is poorly understood, but previous research suggests an essential role for both vRNA packaging signals and highly conserved NP amino acids. By demonstrating that the packaging process is controlled by charge-dependent interactions of highly conserved lysine residues in NP and vRNA packaging signals, our study provides new insights into the sophisticated packaging mechanism of IAVs.
MeSH term(s)	Influenza A virus/genetics ; Influenza A virus/metabolism ; Nucleoproteins/genetics ; Nucleoproteins/metabolism ; Lysine/genetics ; Virus Assembly/genetics ; Genome, Viral ; Amino Acids/genetics ; Nucleocapsid Proteins/genetics ; RNA, Viral/metabolism
Chemical Substances	Nucleoproteins ; Lysine (K3Z4F929H6) ; Amino Acids ; Nucleocapsid Proteins ; RNA, Viral
Language	English
Publishing date	2024-03-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.01972-23
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Article ; Online: The M2 proteins of bat influenza A viruses reveal atypical features compared to conventional M2 proteins.

Thompson, Danielle / Cismaru, Christiana Victoria / Rougier, Jean-Sebastien / Schwemmle, Martin / Zimmer, Gert

Journal of virology

2023 Volume 97, Issue 8, Page(s) e0038823

Abstract: The influenza A virus (IAV) M2 protein has proton channel activity, which plays a role in virus uncoating and may help to preserve the metastable conformation of the IAV hemagglutinin (HA). In contrast to the highly conserved M2 proteins of conventional ... ...

Abstract	The influenza A virus (IAV) M2 protein has proton channel activity, which plays a role in virus uncoating and may help to preserve the metastable conformation of the IAV hemagglutinin (HA). In contrast to the highly conserved M2 proteins of conventional IAV, the primary sequences of bat IAV H17N10 and H18N11 M2 proteins show remarkable divergence, suggesting that these proteins may differ in their biological function. We, therefore, assessed the proton channel activity of bat IAV M2 proteins and investigated its role in virus replication. Here, we show that the M2 proteins of bat IAV did not fully protect acid-sensitive HA of classical IAV from low pH-induced conformational change, indicating low proton channel activity. Interestingly, the N31S substitution not only rendered bat IAV M2 proteins sensitive to inhibition by amantadine but also preserved the metastable conformation of acid-sensitive HA to a greater extent. In contrast, the acid-stable HA of H18N11 did not rely on such support by M2 protein. When mutant M2(N31S) protein was expressed in the context of chimeric H18N11/H5N1(6:2) encoding HA and NA of avian IAV H5N1, amantadine significantly inhibited virus entry, suggesting that ion channel activity supported virus uncoating. Finally, the cytoplasmic domain of the H18N11 M2 protein mediated rapid internalization of the protein from the plasma membrane leading to low-level expression at the cell surface. However, cell surface levels of H18N11 M2 protein were significantly enhanced in cells infected with the chimeric H18N11/H5N1(6:2) virus. The potential role of the N1 sialidase in arresting M2 internalization is discussed. IMPORTANCE Bat IAV M2 proteins not only differ from the homologous proteins of classical IAV by their divergent primary sequence but are also unable to preserve the metastable conformation of acid-sensitive HA, indicating low proton channel activity. This unusual feature may help to avoid M2-mediated cytotoxic effects and inflammation in bats infected with H17N10 or H18N11. Unlike classical M2 proteins, bat IAV M2 proteins with the N31S substitution mediated increased protection of HA from acid-induced conformational change. This remarkable gain of function may help to understand how single point mutations can modulate proton channel activity. In addition, the cytoplasmic domain was found to be responsible for the low cell surface expression level of bat IAV M2 proteins. Given that the M2 cytoplasmic domain of conventional IAV is well known to participate in virus assembly at the plasma membrane, this atypical feature might have consequences for bat IAV budding and egress.
MeSH term(s)	Animals ; Amantadine/pharmacology ; Cell Line ; Chiroptera ; Hemagglutinin Glycoproteins, Influenza Virus/genetics ; Influenza A virus/physiology ; Influenza A Virus, H5N1 Subtype/metabolism ; Protons
Chemical Substances	Amantadine (BF4C9Z1J53) ; Hemagglutinin Glycoproteins, Influenza Virus ; Protons ; M2 protein, Influenza A virus
Language	English
Publishing date	2023-08-04
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.00388-23
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Article ; Online: Bats reveal the true power of influenza A virus adaptability.

Ciminski, Kevin / Pfaff, Florian / Beer, Martin / Schwemmle, Martin

PLoS pathogens

2020 Volume 16, Issue 4, Page(s) e1008384

MeSH term(s)	Adaptation, Biological ; Animals ; Chiroptera/virology ; Disease Reservoirs/virology ; Evolution, Molecular ; Humans ; Influenza A virus/pathogenicity ; Influenza, Human/epidemiology ; Influenza, Human/virology ; Orthomyxoviridae Infections/epidemiology ; Orthomyxoviridae Infections/veterinary ; Orthomyxoviridae Infections/virology ; Selection, Genetic ; Viral Proteins/metabolism
Chemical Substances	Viral Proteins
Keywords	covid19
Language	English
Publishing date	2020-04-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1008384
Database	MEDical Literature Analysis and Retrieval System OnLINE

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