LIVIVO - Search results -

Search results

Result 1 - 10 of total 25

Search options

Article ; Online: Functional Characterization of Adaptive Mutations during the West African Ebola Virus Outbreak.

Dietzel, Erik / Schudt, Gordian / Krähling, Verena / Matrosovich, Mikhail / Becker, Stephan

2017 Volume 91, Issue 2

Abstract: The Ebola virus (EBOV) outbreak in West Africa started in December 2013, claimed more than 11,000 lives, threatened to destabilize a whole region, and showed how easily health crises can turn into humanitarian disasters. EBOV genomic sequences of the ... ...

Abstract	The Ebola virus (EBOV) outbreak in West Africa started in December 2013, claimed more than 11,000 lives, threatened to destabilize a whole region, and showed how easily health crises can turn into humanitarian disasters. EBOV genomic sequences of the West African outbreak revealed nonsynonymous mutations, which induced considerable public attention, but their role in virus spread and disease remains obscure. In this study, we investigated the functional significance of three nonsynonymous mutations that emerged early during the West African EBOV outbreak. Almost 90% of more than 1,000 EBOV genomes sequenced during the outbreak carried the signature of three mutations: a D759G substitution in the active center of the L polymerase, an A82V substitution in the receptor binding domain of surface glycoprotein GP, and an R111C substitution in the self-assembly domain of RNA-encapsidating nucleoprotein NP. Using a newly developed virus-like particle system and reverse genetics, we found that the mutations have an impact on the functions of the respective viral proteins and on the growth of recombinant EBOVs. The mutation in L increased viral transcription and replication, whereas the mutation in NP decreased viral transcription and replication. The mutation in the receptor binding domain of the glycoprotein GP improved the efficiency of GP-mediated viral entry into target cells. Recombinant EBOVs with combinations of the three mutations showed a growth advantage over the prototype isolate Makona C7 lacking the mutations. This study showed that virus variants with improved fitness emerged early during the West African EBOV outbreak. Importance: The dimension of the Ebola virus outbreak in West Africa was unprecedented. Amino acid substitutions in the viral L polymerase, surface glycoprotein GP, and nucleocapsid protein NP emerged, were fixed early in the outbreak, and were found in almost 90% of the sequences. Here we showed that these mutations affected the functional activity of viral proteins and improved viral growth in cell culture. Our results demonstrate emergence of adaptive changes in the Ebola virus genome during virus circulation in humans and prompt further studies on the potential role of these changes in virus transmissibility and pathogenicity.
MeSH term(s)	Adaptation, Biological/genetics ; Africa, Western/epidemiology ; Amino Acid Substitution ; Cell Line ; DNA Replication ; Disease Outbreaks ; Ebolavirus/classification ; Ebolavirus/genetics ; Genome, Viral ; Hemorrhagic Fever, Ebola/epidemiology ; Hemorrhagic Fever, Ebola/virology ; Humans ; Models, Molecular ; Mutation ; Phylogeny ; Protein Conformation ; Transcription, Genetic ; Viral Envelope Proteins/chemistry ; Viral Envelope Proteins/genetics ; Viral Envelope Proteins/metabolism ; Viral Proteins/chemistry ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virus Replication
Chemical Substances	Viral Envelope Proteins ; Viral Proteins
Language	English
Publishing date	2017-01-03
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.01913-16
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 609: 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)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article: Protective CD8+ T Cell Response Induced by Modified Vaccinia Virus Ankara Delivering Ebola Virus Nucleoprotein.

Kupke, Alexandra / Volz, Asisa / Dietzel, Erik / Freudenstein, Astrid / Schmidt, Jörg / Shams-Eldin, Hosam / Jany, Sylvia / Sauerhering, Lucie / Krähling, Verena / Gellhorn Serra, Michelle / Herden, Christiane / Eickmann, Markus / Becker, Stephan / Sutter, Gerd

Vaccines

2022 Volume 10, Issue 4

Abstract: The urgent need for vaccines against Ebola virus (EBOV) was underscored by the large outbreak in West Africa (2014-2016). Since then, several promising vaccine candidates have been tested in pre-clinical and clinical studies. As a result, two vaccines ... ...

Abstract	The urgent need for vaccines against Ebola virus (EBOV) was underscored by the large outbreak in West Africa (2014-2016). Since then, several promising vaccine candidates have been tested in pre-clinical and clinical studies. As a result, two vaccines were approved for human use in 2019/2020, of which one includes a heterologous adenovirus/Modified Vaccinia virus Ankara (MVA) prime-boost regimen. Here, we tested new vaccine candidates based on the recombinant MVA vector, encoding the EBOV nucleoprotein (MVA-EBOV-NP) or glycoprotein (MVA-EBOV-GP) for their efficacy after homologous prime-boost immunization in mice. Our aim was to investigate the role of each antigen in terms of efficacy and correlates of protection. Sera of mice vaccinated with MVA-EBOV-GP were virus-neutralizing and MVA-EBOV-NP immunization readily elicited interferon-γ-producing NP-specific CD8+ T cells. While mock-vaccinated mice succumbed to EBOV infection, all vaccinated mice survived and showed drastically decreased viral loads in sera and organs. In addition, MVA-EBOV-NP vaccinated mice became susceptible to lethal EBOV infection after depletion of CD8+ T cells prior to challenge. This study highlights the potential of MVA-based vaccines to elicit humoral immune responses as well as a strong and protective CD8+ T cell response and contributes to understanding the possible underlying mechanisms.
Language	English
Publishing date	2022-03-29
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2703319-3
ISSN	2076-393X
ISSN	2076-393X
DOI	10.3390/vaccines10040533
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Self-amplifying RNA vaccine protects mice against lethal Ebola virus infection.

Krähling, Verena / Erbar, Stephanie / Kupke, Alexandra / Nogueira, Sara S / Walzer, Kerstin C / Berger, Hendrik / Dietzel, Erik / Halwe, Sandro / Rohde, Cornelius / Sauerhering, Lucie / Aragão-Santiago, Letícia / Moreno Herrero, Jorge / Witzel, Sonja / Haas, Heinrich / Becker, Stephan / Sahin, Ugur

Molecular therapy : the journal of the American Society of Gene Therapy

2022 Volume 31, Issue 2, Page(s) 374–386

Abstract: Emerging and re-emerging viruses, such as Zaire Ebola virus (EBOV), pose a global threat and require immediate countermeasures, including the rapid development of effective vaccines that are easy to manufacture. Synthetic self-amplifying RNAs (saRNAs) ... ...

Abstract	Emerging and re-emerging viruses, such as Zaire Ebola virus (EBOV), pose a global threat and require immediate countermeasures, including the rapid development of effective vaccines that are easy to manufacture. Synthetic self-amplifying RNAs (saRNAs) attend to these needs, being safe and strong immune stimulators that can be inexpensively produced in large quantities, using cell-free systems and good manufacturing practice. Here, the first goal was to develop and optimize an anti-EBOV saRNA-based vaccine in terms of its antigen composition and route of administration. Vaccinating mice with saRNAs expressing the EBOV glycoprotein (GP) alone or in combination with the nucleoprotein (NP) elicited antigen-specific immune responses. GP-specific antibodies showed neutralizing activity against EBOV. Strong CD4
MeSH term(s)	Animals ; Mice ; Hemorrhagic Fever, Ebola/prevention & control ; Antibodies, Viral ; Antibodies, Neutralizing ; Ebolavirus/genetics ; Glycoproteins/genetics ; Ebola Vaccines/genetics
Chemical Substances	Antibodies, Viral ; Antibodies, Neutralizing ; Glycoproteins ; Ebola Vaccines
Language	English
Publishing date	2022-10-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2010592-7
ISSN	1525-0024 ; 1525-0016
ISSN (online)	1525-0024
ISSN	1525-0016
DOI	10.1016/j.ymthe.2022.10.011
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 5640: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Anti-Niemann Pick C1 Single-Stranded Oligonucleotides with Locked Nucleic Acids Potently Reduce Ebola Virus Infection In Vitro.

Sadewasser, Anne / Dietzel, Erik / Michel, Sven / Klüver, Michael / Helfer, Markus / Thelemann, Tamara / Klar, Richard / Eickmann, Markus / Becker, Stephan / Jaschinski, Frank

Molecular therapy. Nucleic acids

2019 Volume 16, Page(s) 686–697

Abstract: Ebola virus is the causative agent of Ebola virus disease, a severe, often fatal illness in humans. So far, there are no US Food and Drug Administration (FDA)-approved therapeutics directed against Ebola virus. Here, we selected the host factor Niemann- ... ...

Abstract	Ebola virus is the causative agent of Ebola virus disease, a severe, often fatal illness in humans. So far, there are no US Food and Drug Administration (FDA)-approved therapeutics directed against Ebola virus. Here, we selected the host factor Niemann-Pick C1 (NPC1), which has been shown to be essential for Ebola virus entry into host cytoplasm, as a therapeutic target for suppression by locked nucleic acid-modified antisense oligonucleotides. Screening of antisense oligonucleotides in human and murine cell lines led to identification of candidates with up to 94% knockdown efficiency and 50% inhibitory concentration (IC
Language	English
Publishing date	2019-04-25
Publishing country	United States
Document type	Journal Article
ZDB-ID	2662631-7
ISSN	2162-2531
ISSN	2162-2531
DOI	10.1016/j.omtn.2019.04.018
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Nipah virus induces two inclusion body populations: Identification of novel inclusions at the plasma membrane.

Ringel, Marc / Heiner, Anja / Behner, Laura / Halwe, Sandro / Sauerhering, Lucie / Becker, Nico / Dietzel, Erik / Sawatsky, Bevan / Kolesnikova, Larissa / Maisner, Andrea

PLoS pathogens

2019 Volume 15, Issue 4, Page(s) e1007733

Abstract: Formation of cytoplasmic inclusion bodies (IBs) is a hallmark of infections with non-segmented negative-strand RNA viruses (order Mononegavirales). We show here that Nipah virus (NiV), a bat-derived highly pathogenic member of the Paramyxoviridae family, ...

Abstract	Formation of cytoplasmic inclusion bodies (IBs) is a hallmark of infections with non-segmented negative-strand RNA viruses (order Mononegavirales). We show here that Nipah virus (NiV), a bat-derived highly pathogenic member of the Paramyxoviridae family, differs from mononegaviruses of the Rhabdo-, Filo- and Pneumoviridae families by forming two types of IBs with distinct localizations, formation kinetics, and protein compositions. IBs in the perinuclear region form rapidly upon expression of the nucleocapsid proteins. These IBperi are highly mobile and associate with the aggresome marker y-tubulin. IBperi can recruit unrelated overexpressed cytosolic proteins but do not contain the viral matrix (M) protein. Additionally, NiV forms an as yet undescribed IB population at the plasma membrane (IBPM) that is y-tubulin-negative but contains the M protein. Infection studies with recombinant NiV revealed that IBPM require the M protein for their formation, and most likely represent sites of NiV assembly and budding. The identification of this novel type of plasma membrane-associated IBs not only provides new insights into NiV biology and may open new avenues to develop novel antiviral approaches to treat these highly pathogenic viruses, it also provides a basis for a more detailed characterization of IBs and their role in virus assembly and replication in infections with other Mononegavirales.
MeSH term(s)	Animals ; Cell Membrane/virology ; Chlorocebus aethiops ; Glycoproteins/metabolism ; Henipavirus Infections/metabolism ; Henipavirus Infections/pathology ; Henipavirus Infections/virology ; Humans ; Inclusion Bodies, Viral/metabolism ; Inclusion Bodies, Viral/pathology ; Inclusion Bodies, Viral/virology ; Nipah Virus/pathogenicity ; Vero Cells ; Viral Matrix Proteins/metabolism ; Virus Assembly ; Virus Internalization
Chemical Substances	Glycoproteins ; Viral Matrix Proteins
Language	English
Publishing date	2019-04-29
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.1007733
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Actin filaments disruption and stabilization affect measles virus maturation by different mechanisms.

Dietzel, Erik / Kolesnikova, Larissa / Maisner, Andrea

Virology journal

2013 Volume 10, Page(s) 249

Abstract: Background: Cytoskeletal proteins are often involved in the virus life cycle, either at early steps during virus entry or at later steps during formation of new virus particles. Though actin filaments have been shown to play a role in the production of ... ...

Abstract	Background: Cytoskeletal proteins are often involved in the virus life cycle, either at early steps during virus entry or at later steps during formation of new virus particles. Though actin filaments have been shown to play a role in the production of measles virus (MV), the importance of actin dynamics for virus assembly and budding steps is not known yet. Aim of this work was thus to analyze the distinctive consequences of F-actin stabilization or disruption for MV protein trafficking, particle assembly and virus release. Results: MV infection studies in the presence of inhibitors differently affecting the actin cytoskeleton revealed that not only actin disruption but also stabilization of actin filaments interfered with MV particle release. While overall viral protein synthesis, surface expression levels of the MV glycoproteins, and cell-associated infectivity was not altered, cell-free virus titers were decreased. Interestingly, the underlying mechanisms of interference with late MV maturation steps differed principally after F-actin disruption by Cytochalasin D (CD) and F-actin stabilization by Jasplakinolide (Jaspla). While intact actin filaments were shown to be required for transport of nucleocapsids and matrix proteins (M-RNPs) from inclusions to the plasma membrane, actin dynamics at the cytocortex that are blocked by Jaspla are necessary for final steps in virus assembly, in particular for the formation of viral buds and the pinching-off at the plasma membrane. Supporting our finding that F-actin disruption blocks M-RNP transport to the plasma membrane, cell-to-cell spread of MV infection was enhanced upon CD treatment. Due to the lack of M-glycoprotein-interactions at the cell surface, M-mediated fusion downregulation was hindered and a more rapid syncytia formation was observed. Conclusion: While stable actin filaments are needed for intracellular trafficking of viral RNPs to the plasma membrane, and consequently for assembly at the cell surface and prevention of an overexerted fusion by the viral surface glycoproteins, actin dynamics are required for the final steps of budding at the plasma membrane.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Animals ; Cell Line ; Cell Membrane/virology ; Dogs ; Host-Pathogen Interactions ; Measles virus/physiology ; Virus Assembly ; Virus Release ; Virus Replication
Language	English
Publishing date	2013-08-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1743-422X
ISSN (online)	1743-422X
DOI	10.1186/1743-422X-10-249
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: A Polymorphism within the Internal Fusion Loop of the Ebola Virus Glycoprotein Modulates Host Cell Entry.

Hoffmann, Markus / Crone, Lisa / Dietzel, Erik / Paijo, Jennifer / González-Hernández, Mariana / Nehlmeier, Inga / Kalinke, Ulrich / Becker, Stephan / Pöhlmann, Stefan

Journal of virology

2017 Volume 91, Issue 9

Abstract: The large scale of the Ebola virus disease (EVD) outbreak in West Africa in 2013-2016 raised the question whether the host cell interactions of the responsible Ebola virus (EBOV) strain differed from those of other ebolaviruses. We previously reported ... ...

Abstract	The large scale of the Ebola virus disease (EVD) outbreak in West Africa in 2013-2016 raised the question whether the host cell interactions of the responsible Ebola virus (EBOV) strain differed from those of other ebolaviruses. We previously reported that the glycoprotein (GP) of the virus circulating in West Africa in 2014 (EBOV2014) exhibited reduced ability to mediate entry into two nonhuman primate (NHP)-derived cell lines relative to the GP of EBOV1976. Here, we investigated the molecular determinants underlying the differential entry efficiency. We found that EBOV2014-GP-driven entry into diverse NHP-derived cell lines, as well as human monocyte-derived macrophages and dendritic cells, was reduced compared to EBOV1976-GP, although entry into most human- and all bat-derived cell lines tested was comparable. Moreover, EBOV2014 replication in NHP but not human cells was diminished relative to EBOV1976, suggesting that reduced cell entry translated into reduced viral spread. Mutagenic analysis of EBOV2014-GP and EBOV1976-GP revealed that an amino acid polymorphism in the receptor-binding domain, A82V, modulated entry efficiency in a cell line-independent manner and did not account for the reduced EBOV2014-GP-driven entry into NHP cells. In contrast, polymorphism T544I, located in the internal fusion loop in the GP2 subunit, was found to be responsible for the entry phenotype. These results suggest that position 544 is an important determinant of EBOV infectivity for both NHP and certain human target cells.
MeSH term(s)	Amino Acid Substitution/genetics ; Animals ; COS Cells ; Cell Line ; Cercopithecus aethiops ; Ebolavirus/genetics ; Ebolavirus/pathogenicity ; HEK293 Cells ; Hemorrhagic Fever, Ebola/virology ; Humans ; Macaca mulatta ; Polymorphism, Single Nucleotide/genetics ; Protein Binding/genetics ; Protein Structure, Tertiary/genetics ; Vero Cells ; Viral Envelope Proteins/genetics ; Virus Attachment ; Virus Internalization ; Virus Replication/genetics
Chemical Substances	Viral Envelope Proteins ; envelope glycoprotein, Ebola virus
Keywords	covid19
Language	English
Publishing date	2017-04-13
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.00177-17
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 609: 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)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Nipah virus fusion protein: influence of cleavage site mutations on the cleavability by cathepsin L, trypsin and furin.

Diederich, Sandra / Dietzel, Erik / Maisner, Andrea

Virus research

2009 Volume 145, Issue 2, Page(s) 300–306

Abstract: Nipah virus (NiV), a highly pathogenic member of the Paramyxoviridae which originated from bats, encodes for a fusion (F) protein which is proteolytically processed within endosomes by cathepsin L. We show here that sequence requirements for NiV F ... ...

Abstract	Nipah virus (NiV), a highly pathogenic member of the Paramyxoviridae which originated from bats, encodes for a fusion (F) protein which is proteolytically processed within endosomes by cathepsin L. We show here that sequence requirements for NiV F activation differ markedly from other para- or orthomyxoviral fusion proteins. In contrast to other viral fusion proteins with monobasic cleavage sites, processing of NiV F proteins with one single basic amino acid in the cleavage peptide by exogenous trypsin is very inefficient, and introduction of a consensus sequence for furin does not result in cleavage by this ubiquitous protease. In contrast, a multibasic cleavage peptide in the NiV F protein completely impairs proteolytic processing and the generation of biological activity.
MeSH term(s)	Amino Acid Sequence ; Animals ; Cathepsin L/metabolism ; Chiroptera/virology ; Furin/metabolism ; Molecular Sequence Data ; Mutation, Missense ; Nipah Virus/genetics ; Nipah Virus/isolation & purification ; Nipah Virus/physiology ; Sequence Alignment ; Trypsin/metabolism ; Viral Envelope Proteins/genetics ; Viral Envelope Proteins/metabolism
Chemical Substances	F protein, Nipah virus ; Viral Envelope Proteins ; Trypsin (EC 3.4.21.4) ; Furin (EC 3.4.21.75) ; Cathepsin L (EC 3.4.22.15)
Keywords	covid19
Language	English
Publishing date	2009-08-07
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	605780-9
ISSN	1872-7492 ; 0168-1702
ISSN (online)	1872-7492
ISSN	0168-1702
DOI	10.1016/j.virusres.2009.07.020
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1965: 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)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Cyclophilin inhibitors restrict Middle East respiratory syndrome coronavirus

Sauerhering, Lucie / Kupke, Alexandra / Meier, Lars / Dietzel, Erik / Hoppe, Judith / Gruber, Achim D / Gattenloehner, Stefan / Witte, Biruta / Fink, Ludger / Hofmann, Nina / Zimmermann, Tobias / Goesmann, Alexander / Nist, Andrea / Stiewe, Thorsten / Becker, Stephan / Herold, Susanne / Peteranderl, Christin

The European respiratory journal

2020 Volume 56, Issue 5

Abstract: While severe coronavirus infections, including Middle East respiratory syndrome coronavirus (MERS-CoV), cause lung injury with high mortality rates, protective treatment strategies are not approved for clinical use.We elucidated the molecular mechanisms ... ...

Abstract	While severe coronavirus infections, including Middle East respiratory syndrome coronavirus (MERS-CoV), cause lung injury with high mortality rates, protective treatment strategies are not approved for clinical use.We elucidated the molecular mechanisms by which the cyclophilin inhibitors cyclosporin A (CsA) and alisporivir (ALV) restrict MERS-CoV to validate their suitability as readily available therapy in MERS-CoV infection.Calu-3 cells and primary human alveolar epithelial cells (hAECs) were infected with MERS-CoV and treated with CsA or ALV or inhibitors targeting cyclophilin inhibitor-regulated molecules including calcineurin, nuclear factor of activated T-cells (NFATs) or mitogen-activated protein kinases. Novel CsA-induced pathways were identified by RNA sequencing and manipulated by gene knockdown or neutralising antibodies. Viral replication was quantified by quantitative real-time PCR and 50% tissue culture infective dose. Data were validated in a murine MERS-CoV infection model.Both CsA and ALV reduced MERS-CoV titres and viral RNA replication in Calu-3 cells and hAECs, improving epithelial integrity. While neither calcineurin nor NFAT inhibition reduced MERS-CoV propagation, blockade of c-Jun N-terminal kinase diminished infectious viral particle release but not RNA accumulation. Importantly, CsA induced interferon regulatory factor 1 (IRF1), a pronounced type III interferon (IFNλ) response and expression of antiviral genes. Downregulation of IRF1 or IFNλ increased MERS-CoV propagation in the presence of CsA. Importantly, oral application of CsA reduced MERS-CoV replication
MeSH term(s)	Alveolar Epithelial Cells/drug effects ; Alveolar Epithelial Cells/metabolism ; Alveolar Epithelial Cells/virology ; Animals ; Calcineurin Inhibitors/pharmacology ; Cell Culture Techniques ; Coronavirus Infections/metabolism ; Coronavirus Infections/prevention & control ; Cyclophilins/antagonists & inhibitors ; Cyclosporine/pharmacology ; Disease Models, Animal ; Humans ; Interferon Regulatory Factor-1/drug effects ; Interferon Regulatory Factor-1/metabolism ; Interferons/drug effects ; Interferons/metabolism ; Mice ; Middle East Respiratory Syndrome Coronavirus/drug effects ; Middle East Respiratory Syndrome Coronavirus/physiology ; Virus Replication/drug effects
Chemical Substances	Calcineurin Inhibitors ; IRF1 protein, human ; Interferon Regulatory Factor-1 ; interferon type III ; Cyclosporine (83HN0GTJ6D) ; Interferons (9008-11-1) ; Cyclophilins (EC 5.2.1.-) ; alisporivir (VBP9099AA6)
Keywords	covid19
Language	English
Publishing date	2020-11-26
Publishing country	England
Document type	Journal Article
ZDB-ID	639359-7
ISSN	1399-3003 ; 0903-1936
ISSN (online)	1399-3003
ISSN	0903-1936
DOI	10.1183/13993003.01826-2019
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 2322: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 292: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Nipah virus entry and egress from polarized epithelial cells.

Lamp, Boris / Dietzel, Erik / Kolesnikova, Larissa / Sauerhering, Lucie / Erbar, Stephanie / Weingartl, Hana / Maisner, Andrea

Journal of virology

2013 Volume 87, Issue 6, Page(s) 3143–3154

Abstract: Highly pathogenic Nipah virus (NiV) infections are transmitted via airway secretions and urine, commonly via the respiratory route. Epithelial surfaces represent important replication sites in both primary and systemic infection phases. NiV entry and ... ...

Abstract	Highly pathogenic Nipah virus (NiV) infections are transmitted via airway secretions and urine, commonly via the respiratory route. Epithelial surfaces represent important replication sites in both primary and systemic infection phases. NiV entry and spread from polarized epithelial cells therefore determine virus entry and dissemination within a new host and influence virus shedding via mucosal surfaces in the respiratory and urinary tract. To date, there is no knowledge regarding the entry and exit sites of NiV in polarized epithelial cells. In this report, we show for the first time that NiV can infect polarized kidney epithelial cells (MDCK) from both cell surfaces, while virus release is primarily restricted to the apical plasma membrane. Substantial amounts of basolateral infectivity were detected only after infection with high virus doses, at time points when the integrity of the cell monolayer was largely disrupted as a result of cell-to-cell fusion. Confocal immunofluorescence analyses of envelope protein distribution at early and late infection stages suggested that apical virus budding is determined by the polarized sorting of the NiV matrix protein, M. Studies with stably M-expressing and with monensin-treated cells furthermore demonstrated that M protein transport is independent from the glycoproteins, implying that the M protein possesses an intrinsic apical targeting signal.
MeSH term(s)	Cell Line ; Epithelial Cells/virology ; Humans ; Microscopy, Confocal ; Microscopy, Fluorescence ; Nipah Virus/physiology ; Protein Transport ; Viral Matrix Proteins/metabolism ; Virus Internalization ; Virus Release
Chemical Substances	Viral Matrix Proteins
Language	English
Publishing date	2013-01-02
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.02696-12
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 609: 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)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito