Database : MEDLINE
Search on : Cowpox [Words]
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[PMID]: 29427674
[Au] Autor:Khlusevich Y; Matveev A; Baykov I; Bulychev L; Bormotov N; Ilyichev I; Shevelev G; Morozova V; Pyshnyi D; Tikunova N
[Ad] Address:Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, Novosibirsk, 630090, Russia.
[Ti] Title:Phage display antibodies against ectromelia virus that neutralize variola virus: Selection and implementation for p35 neutralizing epitope mapping.
[So] Source:Antiviral Res;152:18-25, 2018 Feb 07.
[Is] ISSN:1872-9096
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:In this study, five phage display antibodies (pdAbs) against ectromelia virus (ECTV) were selected from vaccinia virus (VACV)-immune phage-display library of human single chain variable fragments (scFv). ELISA demonstrated that selected pdAbs could recognize ECTV, VACV, and cowpox virus (CPXV). Atomic force microscopy visualized binding of the pdAbs to VACV. Three of the selected pdAbs neutralized variola virus (VARV) in the plaque reduction neutralization test. Western blot analysis of ECTV, VARV, VACV, and CPXV proteins indicated that neutralizing pdAbs bound orthopoxvirus 35 kDa proteins, which are encoded by the open reading frames orthologous to the ORF H3L in VACV. The fully human antibody fh1A was constructed on the base of the VH and VL domains of pdAb, which demonstrated a dose-dependent inhibition of plaque formation after infection with VARV, VACV, and CPXV. To determine the p35 region responsible for binding to neutralizing pdAbs, a panel of truncated p35 proteins was designed and expressed in Escherichia coli cells, and a minimal p35 fragment recognized by selected neutralizing pdAbs was identified. In addition, peptide phage-display combinatorial libraries were applied to localize the epitope. The obtained data indicated that the epitope responsible for recognition by the neutralizing pdAbs is discontinuous and amino acid residues located within two p35 regions, 15-19 aa and 232-237 aa, are involved in binding with neutralizing anti-p35 antibodies.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180304
[Lr] Last revision date:180304
[St] Status:Publisher

  2 / 1062 MEDLINE  
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[PMID]: 29491158
[Au] Autor:Georgana I; Sumner RP; Towers GJ; Maluquer de Motes C
[Ad] Address:Department of Microbial Sciences, University of Surrey, Guildford, United Kingdom.
[Ti] Title:Virulent poxviruses inhibit DNA sensing by preventing STING activation.
[So] Source:J Virol;, 2018 Feb 28.
[Is] ISSN:1098-5514
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Cytosolic recognition of DNA has emerged as a critical cellular mechanism of host immune activation upon pathogen invasion. The central cytosolic DNA sensor cGAS activates STING, which is phosphorylated, dimerises and translocates from the ER to a perinuclear region to mediate IRF-3 activation. Poxviruses are dsDNA viruses replicating in the cytosol and hence likely to trigger cytosolic DNA sensing. Here we investigated the activation of innate immune signalling by 4 different strains of the prototypic poxvirus vaccinia virus (VACV) in a cell line proficient in DNA sensing. Infection with the attenuated VACV strain MVA activated IRF-3 via cGAS and STING, and accordingly STING dimerised and was phosphorylated during MVA infection. Conversely, VACV strains Copenhagen and Western Reserve inhibited STING dimerisation and phosphorylation during infection and in response to transfected DNA and cGAMP, thus efficiently suppressing DNA sensing and IRF-3 activation. A VACV deletion mutant lacking protein C16, thought to be the only viral DNA sensing inhibitor acting upstream of STING, retained the ability to block STING activation. Similar inhibition of DNA-induced STING activation was also observed for cowpox and ectromelia viruses. Our data demonstrate that virulent poxviruses possess mechanisms for targeting DNA sensing at the level of the cGAS-STING axis and that these mechanisms do not operate in replication-defective strains such as MVA. These findings shed light on the role of cellular DNA sensing in poxvirus-host interactions and will open new avenues to determine its impact on VACV immunogenicity and virulence. Poxviruses are dsDNA viruses infecting a wide range of vertebrates and include the causative agent of smallpox (variola virus) and its vaccine vaccinia virus (VACV). Despite smallpox eradication VACV remains of interest as a therapeutic. Attenuated strains are popular vaccine candidates, whereas replication-competent strains are emerging as efficient oncolytics in virotherapy. The successful therapeutic use of VACV depends on a detailed understanding of its ability to modulate host innate immune responses. DNA sensing is a critical cellular mechanism for pathogen detection and activation of innate immunity that is centrally coordinated by the ER-resident protein STING. Here STING is shown to mediate immune activation in response to MVA, but not to virulent VACV strains or other virulent poxviruses, which prevent STING activation and DNA sensing during infection and after DNA transfection. These results provide new insights into poxvirus immune evasion and have implications in the rational design of VACV-based therapeutics.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180301
[Lr] Last revision date:180301
[St] Status:Publisher

  3 / 1062 MEDLINE  
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[PMID]: 29444189
[Au] Autor:Lauron EJ; Yang L; Elliott JI; Gainey MD; Fremont DH; Yokoyama WM
[Ad] Address:Department of Medicine, Washington University School of Medicine, St. Louis, Missouri, United States of America.
[Ti] Title:Cross-priming induces immunodomination in the presence of viral MHC class I inhibition.
[So] Source:PLoS Pathog;14(2):e1006883, 2018 Feb.
[Is] ISSN:1553-7374
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Viruses have evolved mechanisms of MHCI inhibition in order to evade recognition by cytotoxic CD8+ T cells (CTLs), which is well-illustrated by our prior studies on cowpox virus (CPXV) that encodes potent MHCI inhibitors. Deletion of CPXV viral MHCI inhibitors markedly attenuated in vivo infection due to effects on CTL effector function, not priming. However, the CTL response to CPXV in C57BL/6 mice is dominated by a single peptide antigen presented by H-2Kb. Here we evaluated the effect of viral MHCI inhibition on immunodominant (IDE) and subdominant epitopes (SDE) as this has not been thoroughly examined. We found that cross-priming, but not cross-dressing, is the main mechanism driving IDE and SDE CTL responses following CPXV infection. Secretion of the immunodominant antigen was not required for immunodominance. Instead, immunodominance was caused by CTL interference, known as immunodomination. Both immunodomination and cross-priming of SDEs were not affected by MHCI inhibition. SDE-specific CTLs were also capable of exerting immunodomination during primary and secondary responses, which was in part dependent on antigen abundance. Furthermore, CTL responses directed solely against SDEs protected against lethal CPXV infection, but only in the absence of the CPXV MHCI inhibitors. Thus, both SDE and IDE responses can contribute to protective immunity against poxviruses, implying that these principles apply to poxvirus-based vaccines.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180301
[Lr] Last revision date:180301
[St] Status:In-Data-Review
[do] DOI:10.1371/journal.ppat.1006883

  4 / 1062 MEDLINE  
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[PMID]: 29385360
[Au] Autor:Boylston AW
[Ad] Address:From the Nuffield Division of Clinical Laboratory Sciences-Radcliffe Department of Medicine, University of Oxford, Oxford, United Kingdom.
[Ti] Title:The Myth of the Milkmaid.
[So] Source:N Engl J Med;378(5):414-415, 2018 Feb 01.
[Is] ISSN:1533-4406
[Cp] Country of publication:United States
[La] Language:eng
[Mh] MeSH terms primary: Cowpox/history
Farmers/history
Immunization/history
Smallpox Vaccine/history
Smallpox/history
[Mh] MeSH terms secundary: Animals
Cattle
Cowpox/immunology
England
Female
History, 18th Century
History, 19th Century
Humans
Mythology
Orthopoxvirus/immunology
Smallpox/prevention & control
[Pt] Publication type:BIOGRAPHY; HISTORICAL ARTICLE; JOURNAL ARTICLE
[Ps] Personal name as subject:Fewster J; Jenner E
[Nm] Name of substance:0 (Smallpox Vaccine)
[Em] Entry month:1802
[Cu] Class update date: 180222
[Lr] Last revision date:180222
[Js] Journal subset:AIM; IM
[Da] Date of entry for processing:180201
[St] Status:MEDLINE
[do] DOI:10.1056/NEJMp1715349

  5 / 1062 MEDLINE  
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[PMID]: 29363167
[Au] Autor:Spel L; Luteijn RD; Drijfhout JW; Nierkens S; Boes M; Wiertz EJH
[Ad] Address:Laboratory of Translational Immunology, University Medical Center Utrecht, Heidelberglaan 100, Utrecht, 3584 EA, The Netherlands.
[Ti] Title:Endocytosed soluble cowpox virus protein CPXV012 inhibits antigen cross-presentation in human monocyte-derived dendritic cells.
[So] Source:Immunol Cell Biol;96(2):137-148, 2018 Feb.
[Is] ISSN:1440-1711
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Viruses may interfere with the MHC class I antigen presentation pathway in order to avoid CD8 T cell-mediated immunity. A key target within this pathway is the peptide transporter TAP. This transporter plays a central role in MHC class I-mediated peptide presentation of endogenous antigens. In addition, TAP plays a role in antigen cross-presentation of exogenously derived antigens by dendritic cells (DCs). In this study, a soluble form of the cowpox virus TAP inhibitor CPXV012 is synthesized for exogenous delivery into the antigen cross-presentation route of human monocyte-derived (mo)DCs. We show that soluble CPXV012 localizes to TAP compartments that carry internalized antigen and is a potent inhibitor of antigen cross-presentation. CPXV012 stimulates the prolonged deposition of antigen fragments in storage compartments of moDCs, as a result of reduced endosomal acidification and reduced antigen proteolysis when soluble CPXV012 is present. Thus, a dual function can be proposed for CPXV012: inhibition of TAP-mediated peptide transport and inhibition of endosomal antigen degradation. We propose this second function for soluble CPXV012 can serve to interfere with antigen cross-presentation in a peptide transport-independent manner.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180223
[Lr] Last revision date:180223
[St] Status:In-Data-Review
[do] DOI:10.1111/imcb.1024

  6 / 1062 MEDLINE  
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[PMID]: 29446492
[Au] Autor:Zehender G; Lai A; Veo C; Bergna A; Ciccozzi M; Galli M
[Ad] Address:Department of Biomedical and Clinical Sciences "Luigi Sacco", University of Milan, Milan, Italy.
[Ti] Title:BAYESIAN RECONSTRUCTION OF THE EVOLUTIONARY HISTORY AND CROSS-SPECIES TRANSITION OF VARIOLA VIRUS AND ORTHOPOXVIRUSES.
[So] Source:J Med Virol;, 2018 Feb 15.
[Is] ISSN:1096-9071
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Variola virus (VARV), the causative agent of smallpox, is an exclusively human virus belonging to the genus Orthopoxvirus, which includes many other viral species covering a wide range of mammal hosts, such as vaccinia, cowpox, camelpox, taterapox, ectromelia and monkeypox virus. The tempo and mode of evolution of Orthopoxviruses were reconstructed using a Bayesian phylodynamic framework by analysing 80 hemagglutinin sequences retrieved from public databases. Bayesian phylogeography was used to estimate their putative ancestral hosts. In order to estimate the substitution rate, the tree including all of the available Orthopoxviruses was calibrated using historical references dating the South American variola minor clade (alastrim) to between the XVI and XIX century. The mean substitution rate determined by the analysis was 6.5 × 10 substitutions/site/year. Based on this evolutionary estimate, the time of the most recent common ancestor of the genus Orthopoxvirus was placed at about 10,000 years before the present. Cowpox virus was the species closest to the root of the phylogenetic tree. The root of VARV circulating in the XX century was estimated to be about 700 years ago, corresponding to about 1300 AD. The divergence between West African and South American VARV went back about 500 years ago (falling approximately in the XVI century). A rodent species is the most probable ancestral host from which the ancestors of all the known Orthopoxviruses were transmitted to the other mammal host species, and each of these species represented a dead-end for each new poxvirus species, without any further inter-specific spread. This article is protected by copyright. All rights reserved.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180215
[Lr] Last revision date:180215
[St] Status:Publisher
[do] DOI:10.1002/jmv.25055

  7 / 1062 MEDLINE  
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[PMID]: 29224735
[Au] Autor:Koban R; Neumann M; Daugs A; Bloch O; Nitsche A; Langhammer S; Ellerbrok H
[Ad] Address:Robert Koch Institute, Seestr. 10, 13353 Berlin, Germany.
[Ti] Title:A novel three-dimensional cell culture method enhances antiviral drug screening in primary human cells.
[So] Source:Antiviral Res;150:20-29, 2018 02.
[Is] ISSN:1872-9096
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Gefitinib is a specific inhibitor of the epidermal growth factor receptor (EGFR) and FDA approved for treatment of non-small cell lung cancer. In a previous study we could show the in vitro efficacy of gefitinib for treatment of poxvirus infections in monolayer (2D) cultivated cell lines. Permanent cell lines and 2D cultures, however, are known to be rather unphysiological; therefore it is difficult to predict whether determined effective concentrations or the drug efficacy per se are transferable to the in vivo situation. 3D cell cultures, which meanwhile are widely distributed across all fields of research, are a promising tool for more predictive in vitro investigations of antiviral compounds. In this study the spreading of cowpox virus and the antiviral efficacy of gefitinib were analyzed in primary human keratinocytes (NHEK) grown in a novel 3D extracellular matrix-based cell culture model and compared to the respective monolayer culture. 3D-cultivated NHEK grew in a polarized and thus a more physiological manner with altered morphology and close cell-cell contact. Infected cultures showed a strongly elevated sensitivity towards gefitinib. EGFR phosphorylation, cell proliferation, and virus replication were significantly reduced in 3D cultures at gefitinib concentrations which were at least 100-fold lower than those in monolayer cultures and well below the level of cytotoxicity. Our newly established 3D cell culture model with primary human cells is an easy-to-handle alternative to conventional monolayer cell cultures and previously described more complex 3D cell culture systems. It can easily be adapted to other cell types and a broad spectrum of viruses for antiviral drug screening and many other aspects of virus research under more in vivo-like conditions. In consequence, it may contribute to a more targeted realization of necessary in vivo experiments.
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Entry month:1712
[Cu] Class update date: 180213
[Lr] Last revision date:180213
[St] Status:In-Process

  8 / 1062 MEDLINE  
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[PMID]: 29422319
[Au] Autor:Jungwirth N; Puff C; Köster K; Mischke R; Meyer H; Stark A; Thoma B; Zöller G; Seehusen F; Hewicker-Trautwein M; Beineke A; Baumgärtner W; Wohlsein P
[Ad] Address:Department of Pathology, University of Veterinary Medicine Hannover, Hannover, Germany; Centre for Systems Neuroscience, Hannover, Germany.
[Ti] Title:Atypical Cowpox Virus Infection in a Series of Cats.
[So] Source:J Comp Pathol;158:71-76, 2018 Jan.
[Is] ISSN:1532-3129
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Within 4 weeks, five cats with skin lesions affecting the hindlimbs and mainly consisting of oedema, hyperaemia and plaque-like alterations were presented to the same veterinary clinic. The cats were suffering from lameness, trauma, renal insufficiency or complicated tail amputation. Although the lesions seemed unusual for a poxvirus infection, microscopical examination of biopsy samples or specimens taken during necropsy examination revealed ballooning degeneration of keratinocytes with eosinophilic, cytoplasmic inclusion bodies indicative of an orthopoxvirus infection. Cowpox virus infection was verified using immunohistochemistry and virus isolation. Molecular analysis revealed identical haemagglutinin gene sequences in four cases and spatiotemporal circumstances in some cases pointed to hospital-acquired transmission. Unusual manifestations of feline cowpox may have an unexpected risk for human infection.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180209
[Lr] Last revision date:180209
[St] Status:In-Process

  9 / 1062 MEDLINE  
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[PMID]: 29379051
[Au] Autor:Grossegesse M; Doellinger J; Fritsch A; Laue M; Piesker J; Schaade L; Nitsche A
[Ad] Address:Robert Koch Institute, Centre for Biological Threats and Special Pathogens: Highly Pathogenic Viruses (ZBS 1), Berlin, 13353, Germany.
[Ti] Title:Global ubiquitination analysis reveals extensive modification and proteasomal degradation of cowpox virus proteins, but preservation of viral cores.
[So] Source:Sci Rep;8(1):1807, 2018 Jan 29.
[Is] ISSN:2045-2322
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:The emergence of Variola virus-like viruses by natural evolution of zoonotic Orthopoxviruses, like Cowpox virus (CPXV), is a global health threat. The proteasome is essential for poxvirus replication, making the viral components interacting with the ubiquitin-proteasome system attractive antiviral targets. We show that proteasome inhibition impairs CPXV replication by prevention of uncoating, suggesting that uncoating is mediated by proteasomal degradation of viral core proteins. Although Orthopoxvirus particles contain considerable amounts of ubiquitin, distinct modification sites are largely unknown. Therefore, for the first time, we analyzed globally ubiquitination sites in CPXV mature virion proteins using LC-MS/MS. Identification of 137 conserved sites in 54 viral proteins among five CPXV strains revealed extensive ubiquitination of structural core proteins. Moreover, since virions contained primarily K48-linked polyubiquitin, we hypothesized that core proteins are modified accordingly. However, quantitative analysis of ubiquitinated CPXV proteins early in infection showed no proteasomal degradation of core proteins. Instead, our data indicate that the recently suggested proteasomal regulation of the uncoating factor E5 is a prerequisite for uncoating. Expanding our understanding of poxvirus uncoating and elucidating a multitude of novel ubiquitination sites in poxvirus proteins, the present study verifies the major biological significance of ubiquitin in poxvirus infection.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180209
[Lr] Last revision date:180209
[St] Status:In-Data-Review
[do] DOI:10.1038/s41598-018-20130-9

  10 / 1062 MEDLINE  
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[PMID]: 29323851
[Au] Autor:Borisevich SV; Marennikova SS; Stovba LF; Petrov AA; Krotvov VT; Makhlai AA
[Ti] Title:Buffalopox.
[So] Source:Vopr Virusol;61(5):200-4, 2016.
[Is] ISSN:0507-4088
[Cp] Country of publication:Russia (Federation)
[La] Language:eng
[Ab] Abstract:Buffalopox is a contagious viral disease affecting milch buffaloes (Bubalus Bubalis) and, rarely, cows. The disease has zoonotic implications, as outbreaks are frequently associated with human infections, particularly in the milkers. Buffalopox is associated with high morbidity (80%). The clinical symptoms of the disease are characterized by wartline lesions on the udder, teats, inguinal region, base of the ears, and over the parotid. In the severe form, generalized rash is observed. Although the disease does not lead to high mortality, it has an adverse effect on the productivity and working capacity of the animals resulting in large economic losses. The outbreaks of buffalopox occurred frequently in India, Pakistan, Bangladesh, Nepal, Iran, Egypt, and Indonesia, where buffaloes are reared as milch animals. The buffalopox is closely related with other Orthopoxviruses. In particular, it is close to the vaccinia virus. There is a view that the buffalopox virus might be derived from the vaccinia virus. It is possible that it became pathogenic to humans and animals through adaptive evolution of the genome by obtaining the virulence genes. PCR is performed for the C18L gene for the purpose of specific detection and differentiation of the buffalopox virus from other orthopoxviruses. The C18L gene encodes the ankyrin repeat protein, which determines the virus host range. The open reading frame of this gene is only 150-nucleotide long as against 453 nucleotide in the vaccinia virus, 756 - in the camelpox virus, and 759 - in the cowpox virus. It can be concluded that a systematic study based on the epidemiology of the virus, existence of reservoirs, biological transmission, and the molecular organization of the buffalopox virus from buffalo, cow, and humans may pave the way to a better understanding of the circulating virus and contribute to the control of the disease using the suitable diagnostic and prophylactic measures.
[Mh] MeSH terms primary: Cowpox virus/genetics
Cowpox/epidemiology
Disease Outbreaks
Vaccinia virus/genetics
Vaccinia/veterinary
Zoonoses/epidemiology
[Mh] MeSH terms secundary: Animals
Ankyrin Repeat
Asia, Western/epidemiology
Buffaloes/virology
Cattle
Cowpox/transmission
Cowpox/virology
Cowpox virus/classification
Cowpox virus/isolation & purification
DNA, Viral/genetics
Middle East/epidemiology
Phylogeny
Vaccinia/epidemiology
Vaccinia/transmission
Vaccinia/virology
Vaccinia virus/classification
Vaccinia virus/isolation & purification
Viral Proteins/genetics
Zoonoses/transmission
Zoonoses/virology
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (DNA, Viral); 0 (Viral Proteins)
[Em] Entry month:1802
[Cu] Class update date: 180208
[Lr] Last revision date:180208
[Js] Journal subset:IM
[Da] Date of entry for processing:180112
[St] Status:MEDLINE


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