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  1 / 2780 MEDLINE  
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[PMID]:29190287
[Au] Autor:Hu B; Zeng LP; Yang XL; Ge XY; Zhang W; Li B; Xie JZ; Shen XR; Zhang YZ; Wang N; Luo DS; Zheng XS; Wang MN; Daszak P; Wang LF; Cui J; Shi ZL
[Ad] Endereço:CAS Key Laboratory of Special Pathogens and Biosafety, Center for Emerging Infectious Diseases of Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, China.
[Ti] Título:Discovery of a rich gene pool of bat SARS-related coronaviruses provides new insights into the origin of SARS coronavirus.
[So] Source:PLoS Pathog;13(11):e1006698, 2017 Nov.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A large number of SARS-related coronaviruses (SARSr-CoV) have been detected in horseshoe bats since 2005 in different areas of China. However, these bat SARSr-CoVs show sequence differences from SARS coronavirus (SARS-CoV) in different genes (S, ORF8, ORF3, etc) and are considered unlikely to represent the direct progenitor of SARS-CoV. Herein, we report the findings of our 5-year surveillance of SARSr-CoVs in a cave inhabited by multiple species of horseshoe bats in Yunnan Province, China. The full-length genomes of 11 newly discovered SARSr-CoV strains, together with our previous findings, reveals that the SARSr-CoVs circulating in this single location are highly diverse in the S gene, ORF3 and ORF8. Importantly, strains with high genetic similarity to SARS-CoV in the hypervariable N-terminal domain (NTD) and receptor-binding domain (RBD) of the S1 gene, the ORF3 and ORF8 region, respectively, were all discovered in this cave. In addition, we report the first discovery of bat SARSr-CoVs highly similar to human SARS-CoV in ORF3b and in the split ORF8a and 8b. Moreover, SARSr-CoV strains from this cave were more closely related to SARS-CoV in the non-structural protein genes ORF1a and 1b compared with those detected elsewhere. Recombination analysis shows evidence of frequent recombination events within the S gene and around the ORF8 between these SARSr-CoVs. We hypothesize that the direct progenitor of SARS-CoV may have originated after sequential recombination events between the precursors of these SARSr-CoVs. Cell entry studies demonstrated that three newly identified SARSr-CoVs with different S protein sequences are all able to use human ACE2 as the receptor, further exhibiting the close relationship between strains in this cave and SARS-CoV. This work provides new insights into the origin and evolution of SARS-CoV and highlights the necessity of preparedness for future emergence of SARS-like diseases.
[Mh] Termos MeSH primário: Quirópteros/virologia
Pool Gênico
Genoma Viral/genética
Vírus da SARS/genética
Síndrome Respiratória Aguda Grave/virologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos/genética
Animais
Infecções por Coronavirus/virologia
Evolução Molecular
Seres Humanos
Recombinação Genética/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006698


  2 / 2780 MEDLINE  
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[PMID]:28750053
[Au] Autor:Vazquez L; E Lima LMTDR; Almeida MDS
[Ad] Endereço:Instituto de Bioquímica Médica Leopoldo de Meis, Centro Nacional de Biologia Estrutural e Bioimagem (CENABIO), Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil.
[Ti] Título:Comprehensive structural analysis of designed incomplete polypeptide chains of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus.
[So] Source:PLoS One;12(7):e0182132, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cotranslational folding is recognized as a very cooperative process that occurs after the nearly completion of the polypeptide sequence of a domain. Here we investigated the challenges faced by polypeptide segments of a non-vectorial ß-barrel fold. Besides the biological interest behind the SARS coronavirus non-structural protein 1 (nsp1, 117 amino acids), this study model has two structural features that motivated its use in this work: 1- its recombinant production is dependent on the temperature, with greater solubility when expressed at low temperatures. This is an indication of the cotranslational guidance to the native protein conformation. 2- Conversely, nsp1 has a six-stranded, mixed parallel/antiparallel ß-barrel with intricate long-range interactions, indicating it will need the full-length protein to fold properly. We used non-denaturing purification conditions that allowed the characterization of polypeptide chains of different lengths, mimicking the landscape of the cotranslational fold of a ß-barrel, and avoiding the major technical hindrances of working with the nascent polypeptide bound to the ribosome. Our results showed partially folded states formed as soon as the amino acids of the second ß-strand were present (55 amino acids). These partially folded states are different based on the length of polypeptide chain. The native α-helix (amino acids 24-37) was identified as a transient structure (~20-30% propensity). We identified the presence of regular secondary structure after the fourth native ß-strand is present (89 amino acids), in parallel to the collapse to a non-native 3D structure. Interestingly the polypeptide sequences of the native strands ß2, ß3 and ß4 have characteristics of α-helices. Our comprehensive analyses support the idea that incomplete polypeptide chains, such as the ones of nascent proteins much earlier than the end of the translation, adopt an abundance of specific transient folds, instead of disordered conformations.
[Mh] Termos MeSH primário: Peptídeos/química
Vírus da SARS/química
Proteínas não Estruturais Virais/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Dicroísmo Circular
Interações Hidrofóbicas e Hidrofílicas
Espectroscopia de Ressonância Magnética
Modelos Moleculares
Biossíntese de Proteínas
Dobramento de Proteína
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Proteínas Recombinantes de Fusão/química
Espalhamento a Baixo Ângulo
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); 0 (Recombinant Fusion Proteins); 0 (Viral Nonstructural Proteins); 0 (nonstructural protein, coronavirus)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182132


  3 / 2780 MEDLINE  
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[PMID]:28738245
[Au] Autor:Sakai Y; Kawachi K; Terada Y; Omori H; Matsuura Y; Kamitani W
[Ad] Endereço:Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan; Laboratory of Veterinary Pathology, Joint Faculty of Veterinary Medicine, Yamaguchi University, Yamaguchi, Japan.
[Ti] Título:Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication.
[So] Source:Virology;510:165-174, 2017 Oct.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Infection with coronavirus rearranges the host cell membrane to assemble a replication/transcription complex in which replication of the viral genome and transcription of viral mRNA occur. Although coexistence of nsp3 and nsp4 is known to cause membrane rearrangement, the mechanisms underlying the interaction of these two proteins remain unclear. We demonstrated that binding of nsp4 with nsp3 is essential for membrane rearrangement and identified amino acid residues in nsp4 responsible for the interaction with nsp3. In addition, we revealed that the nsp3-nsp4 interaction is not sufficient to induce membrane rearrangement, suggesting the participation of other factors such as host proteins. Finally, we showed that loss of the nsp3-nsp4 interaction eliminated viral replication by using an infectious cDNA clone and replicon system of SARS-CoV. These findings provide clues to the mechanism of the replication/transcription complex assembly of SARS-CoV and could reveal an antiviral target for the treatment of betacoronavirus infection.
[Mh] Termos MeSH primário: Substituição de Aminoácidos
Vírus da SARS/fisiologia
Proteínas não Estruturais Virais/genética
Replicação Viral
[Mh] Termos MeSH secundário: Análise Mutacional de DNA
Mapeamento de Interação de Proteínas
Vírus da SARS/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Viral Nonstructural Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE


  4 / 2780 MEDLINE  
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[PMID]:28727803
[Au] Autor:Xiao S; Li Y; Wong TW; Hui DSC
[Ad] Endereço:Department of Mechanical Engineering, The University of Hong Kong, Hong Kong SAR, China.
[Ti] Título:Role of fomites in SARS transmission during the largest hospital outbreak in Hong Kong.
[So] Source:PLoS One;12(7):e0181558, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The epidemic of severe acute respiratory syndrome (SARS) had a significant effect on global society in the early 2000s and the potential of its resurgence exists. Studies on the modes of transmission of SARS are limited though a number of outbreak studies have revealed the possible airborne route. To develop more specific and effective control strategies, we conducted a detailed mechanism-based investigation that explored the role of fomite transmission in the well-known Ward 8A outbreak. We considered three hypothetical transmission routes, i.e., the long-range airborne, fomite and combined routes, in 1,744 scenarios with combinations of some important parameters. A multi-agent model was used to predict the infection risk distributions of the three hypothetical routes. Model selection was carried out for different scenarios to compare the distributions of infection risk with that of the reported attack rates and select the hypotheses with the best fitness. Our results reveal that under the assumed conditions, the SARS coronavirus was most possible to have spread via the combined long-range airborne and fomite routes, and that the fomite route played a non-negligible role in the transmission.
[Mh] Termos MeSH primário: Infecção Hospitalar/epidemiologia
Infecção Hospitalar/transmissão
Surtos de Doenças
Fômites/virologia
Vírus da SARS
Síndrome Respiratória Aguda Grave/epidemiologia
Síndrome Respiratória Aguda Grave/transmissão
[Mh] Termos MeSH secundário: Adulto
Ar
Hong Kong/epidemiologia
Hospitais
Seres Humanos
Masculino
Modelos Biológicos
Membrana Mucosa/virologia
Enfermeiras e Enfermeiros
Médicos
Sistema Respiratório/virologia
Risco
Tato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170721
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181558


  5 / 2780 MEDLINE  
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[PMID]:28624700
[Au] Autor:Wang L; Bao BB; Song GQ; Chen C; Zhang XM; Lu W; Wang Z; Cai Y; Li S; Fu S; Song FH; Yang H; Wang JG
[Ad] Endereço:State-Key Laboratory and Research Institute of Elemento-Organic Chemistry, National Pesticide Engineering Research Center, College of Chemistry, Nankai University, Tianjin 300071, China.
[Ti] Título:Discovery of unsymmetrical aromatic disulfides as novel inhibitors of SARS-CoV main protease: Chemical synthesis, biological evaluation, molecular docking and 3D-QSAR study.
[So] Source:Eur J Med Chem;137:450-461, 2017 Sep 08.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:The worldwide outbreak of severe acute respiratory syndrome (SARS) in 2003 had caused a high rate of mortality. Main protease (M ) of SARS-associated coronavirus (SARS-CoV) is an important target to discover pharmaceutical compounds for the therapy of this life-threatening disease. During the course of screening new anti-SARS agents, we have identified that a series of unsymmetrical aromatic disulfides inhibited SARS-CoV M significantly for the first time. Herein, 40 novel unsymmetrical aromatic disulfides were synthesized chemically and their biological activities were evaluated in vitro against SARS-CoV M . These novel compounds displayed excellent IC data in the range of 0.516-5.954 µM. Preliminary studies indicated that these disulfides are reversible and mpetitive inhibitors. A possible binding mode was generated via molecular docking simulation and a comparative field analysis (CoMFA) model was constructed to understand the structure-activity relationships. The present research therefore has provided some meaningful guidance to design and identify anti-SARS drugs with totally new chemical structures.
[Mh] Termos MeSH primário: Antivirais/farmacologia
Dissulfetos/farmacologia
Descoberta de Drogas
Hidrocarbonetos Aromáticos/farmacologia
Simulação de Acoplamento Molecular
Inibidores de Proteases/farmacologia
Relação Quantitativa Estrutura-Atividade
Vírus da SARS/efeitos dos fármacos
Proteínas Virais/antagonistas & inibidores
[Mh] Termos MeSH secundário: Antivirais/síntese química
Antivirais/química
Cisteína Endopeptidases/metabolismo
Dissulfetos/síntese química
Dissulfetos/química
Relação Dose-Resposta a Droga
Hidrocarbonetos Aromáticos/síntese química
Hidrocarbonetos Aromáticos/química
Testes de Sensibilidade Microbiana
Estrutura Molecular
Inibidores de Proteases/síntese química
Inibidores de Proteases/química
Vírus da SARS/enzimologia
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Disulfides); 0 (Hydrocarbons, Aromatic); 0 (Protease Inhibitors); 0 (Viral Proteins); EC 3.4.22.- (3C-like protease, SARS coronavirus); EC 3.4.22.- (Cysteine Endopeptidases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170619
[St] Status:MEDLINE


  6 / 2780 MEDLINE  
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[PMID]:28580734
[Au] Autor:Hammond RG; Tan X; Johnson MA
[Ad] Endereço:Department of Chemistry, University of Alabama at Birmingham, Birmingham, Alabama, 35294.
[Ti] Título:SARS-unique fold in the Rousettus bat coronavirus HKU9.
[So] Source:Protein Sci;26(9):1726-1737, 2017 Sep.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The coronavirus nonstructural protein 3 (nsp3) is a multifunctional protein that comprises multiple structural domains. This protein assists viral polyprotein cleavage, host immune interference, and may play other roles in genome replication or transcription. Here, we report the solution NMR structure of a protein from the "SARS-unique region" of the bat coronavirus HKU9. The protein contains a frataxin fold or double-wing motif, which is an α + ß fold that is associated with protein/protein interactions, DNA binding, and metal ion binding. High structural similarity to the human severe acute respiratory syndrome (SARS) coronavirus nsp3 is present. A possible functional site that is conserved among some betacoronaviruses has been identified using bioinformatics and biochemical analyses. This structure provides strong experimental support for the recent proposal advanced by us and others that the "SARS-unique" region is not unique to the human SARS virus, but is conserved among several different phylogenetic groups of coronaviruses and provides essential functions.
[Mh] Termos MeSH primário: Coronavirus/química
RNA Replicase/química
RNA Replicase/metabolismo
Vírus da SARS/química
Proteínas não Estruturais Virais/química
Proteínas não Estruturais Virais/metabolismo
[Mh] Termos MeSH secundário: Animais
Quirópteros
Modelos Moleculares
Ressonância Magnética Nuclear Biomolecular
Domínios Proteicos
Dobramento de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Viral Nonstructural Proteins); EC 2.7.7.48 (RNA Replicase); EC 2.7.7.48 (nonstructural protein 3, SARS coronovirus)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170606
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3208


  7 / 2780 MEDLINE  
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[PMID]:28438633
[Au] Autor:Daczkowski CM; Dzimianski JV; Clasman JR; Goodwin O; Mesecar AD; Pegan SD
[Ad] Endereço:Department of Pharmaceutical and Biomedical Sciences, University of Georgia, Athens, GA 30602, USA.
[Ti] Título:Structural Insights into the Interaction of Coronavirus Papain-Like Proteases and Interferon-Stimulated Gene Product 15 from Different Species.
[So] Source:J Mol Biol;429(11):1661-1683, 2017 Jun 02.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Severe acute respiratory syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus (MERS-CoV) encode multifunctional papain-like proteases (PLPs) that have the ability to process the viral polyprotein to facilitate RNA replication and antagonize the host innate immune response. The latter function involves reversing the post-translational modification of cellular proteins conjugated with either ubiquitin (Ub) or Ub-like interferon-stimulated gene product 15 (ISG15). Ub is known to be highly conserved among eukaryotes, but surprisingly, ISG15 is highly divergent among animals. The ramifications of this sequence divergence to the recognition of ISG15 by coronavirus PLPs at a structural and biochemical level are poorly understood. Therefore, the activity of PLPs from SARS-CoV, MERS-CoV, and mouse hepatitis virus was evaluated against seven ISG15s originating from an assortment of animal species susceptible, and not, to certain coronavirus infections. Excitingly, our kinetic, thermodynamic, and structural analysis revealed an array of different preferences among PLPs. Included in these studies is the first insight into a coronavirus PLP's interface with ISG15 via SARS-CoV PLpro in complex with the principle binding domain of human ISG15 (hISG15) and mouse ISG15s (mISG15s). The first X-ray structure of the full-length mISG15 protein is also reported and highlights a unique, twisted hinge region of ISG15 that is not conserved in hISG15, suggesting a potential role in differential recognition. Taken together, this new information provides a structural and biochemical understanding of the distinct specificities among coronavirus PLPs observed and addresses a critical gap of how PLPs can interact with ISG15s from a wide variety of species.
[Mh] Termos MeSH primário: Cisteína Endopeptidases/química
Cisteína Endopeptidases/metabolismo
Coronavírus da Síndrome Respiratória do Oriente Médio/enzimologia
Vírus da Hepatite Murina/enzimologia
Vírus da SARS/enzimologia
Ubiquitinas/química
Ubiquitinas/metabolismo
Proteínas Virais/química
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Animais
Cristalografia por Raios X
Seres Humanos
Cinética
Camundongos
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ubiquitins); 0 (Viral Proteins); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.28 (3C proteases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171011
[Lr] Data última revisão:
171011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170426
[St] Status:MEDLINE


  8 / 2780 MEDLINE  
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[PMID]:28404843
[Au] Autor:Venkataraman T; Coleman CM; Frieman MB
[Ad] Endereço:Department of Microbiology and Immunology, The University of Maryland at Baltimore, Baltimore, Maryland, USA.
[Ti] Título:Overactive Epidermal Growth Factor Receptor Signaling Leads to Increased Fibrosis after Severe Acute Respiratory Syndrome Coronavirus Infection.
[So] Source:J Virol;91(12), 2017 Jun 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Severe acute respiratory syndrome coronavirus (SARS-CoV) is a highly pathogenic respiratory virus that causes morbidity and mortality in humans. After infection with SARS-CoV, the acute lung injury caused by the virus must be repaired to regain lung function. A dysregulation in this wound healing process leads to fibrosis. Many survivors of SARS-CoV infection develop pulmonary fibrosis (PF), with higher prevalence in older patients. Using mouse models of SARS-CoV pathogenesis, we have identified that the wound repair pathway, controlled by the epidermal growth factor receptor (EGFR), is critical to recovery from SARS-CoV-induced tissue damage. In mice with constitutively active EGFR [EGFR(DSK5) mice], we find that SARS-CoV infection causes enhanced lung disease. Importantly, we show that during infection, the EGFR ligands amphiregulin and heparin-binding EGF-like growth factor (HB-EGF) are upregulated, and exogenous addition of these ligands during infection leads to enhanced lung disease and altered wound healing dynamics. Our data demonstrate a key role of EGFR in the host response to SARS-CoV and how it may be implicated in lung disease induced by other highly pathogenic respiratory viruses. PF has many causative triggers, including severe respiratory viruses such as SARS-CoV. Currently there are no treatments to prevent the onset or limit the progression of PF, and the molecular pathways underlying the development of PF are not well understood. In this study, we identified a role for the balanced control of EGFR signaling as a key factor in progression to PF. These data demonstrate that therapeutic treatment modulating EGFR activation could protect against PF development caused by severe respiratory virus infection.
[Mh] Termos MeSH primário: Pulmão/patologia
Fibrose Pulmonar/virologia
Receptor do Fator de Crescimento Epidérmico/metabolismo
Vírus da SARS/patogenicidade
Síndrome Respiratória Aguda Grave/metabolismo
Síndrome Respiratória Aguda Grave/patologia
[Mh] Termos MeSH secundário: Anfirregulina/administração & dosagem
Anfirregulina/metabolismo
Animais
Modelos Animais de Doenças
Seres Humanos
Pulmão/virologia
Camundongos
Fibrose Pulmonar/metabolismo
Fibrose Pulmonar/patologia
Vírus da SARS/fisiologia
Síndrome Respiratória Aguda Grave/virologia
Transdução de Sinais
Cicatrização/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amphiregulin); EC 2.7.10.1 (EGFR protein, mouse); EC 2.7.10.1 (Receptor, Epidermal Growth Factor)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE


  9 / 2780 MEDLINE  
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[PMID]:28373583
[Au] Autor:Channappanavar R; Fett C; Mack M; Ten Eyck PP; Meyerholz DK; Perlman S
[Ad] Endereço:Department of Microbiology, University of Iowa, Iowa City, IA 52242.
[Ti] Título:Sex-Based Differences in Susceptibility to Severe Acute Respiratory Syndrome Coronavirus Infection.
[So] Source:J Immunol;198(10):4046-4053, 2017 May 15.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pathogenic human coronaviruses (CoVs), such as the severe acute respiratory syndrome (SARS)-CoV and the Middle East respiratory syndrome-CoV, cause acute respiratory illness. Epidemiological data from the 2002-2003 SARS epidemic and recent Middle East respiratory syndrome outbreak indicate that there may be sex-dependent differences in disease outcomes. To investigate these differences, we infected male and female mice of different age groups with SARS-CoV and analyzed their susceptibility to the infection. Our results showed that male mice were more susceptible to SARS-CoV infection compared with age-matched females. The degree of sex bias to SARS-CoV infection increased with advancing age, such that middle-aged mice showed much more pronounced differences compared with young mice. Enhanced susceptibility of male mice to SARS-CoV was associated with elevated virus titers, enhanced vascular leakage, and alveolar edema. These changes were accompanied by increased accumulation of inflammatory monocyte macrophages and neutrophils in the lungs of male mice, and depletion of inflammatory monocyte macrophages partially protected these mice from lethal SARS. Moreover, the sex-specific differences were independent of T and B cell responses. Furthermore, ovariectomy or treating female mice with an estrogen receptor antagonist increased mortality, indicating a protective effect for estrogen receptor signaling in mice infected with SARS-CoV. Together, these data suggest that sex differences in the susceptibility to SARS-CoV in mice parallel those observed in patients and also identify estrogen receptor signaling as critical for protection in females.
[Mh] Termos MeSH primário: Suscetibilidade a Doenças
Síndrome Respiratória Aguda Grave/fisiopatologia
Caracteres Sexuais
[Mh] Termos MeSH secundário: Animais
Antagonistas do Receptor de Estrogênio/farmacologia
Feminino
Pulmão/imunologia
Pulmão/patologia
Pulmão/virologia
Masculino
Camundongos
Monócitos/imunologia
Ovariectomia
Receptores Estrogênicos/metabolismo
Vírus da SARS/isolamento & purificação
Vírus da SARS/patogenicidade
Síndrome Respiratória Aguda Grave/patologia
Síndrome Respiratória Aguda Grave/virologia
Carga Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Estrogen Receptor Antagonists); 0 (Receptors, Estrogen)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170405
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1601896


  10 / 2780 MEDLINE  
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[PMID]:28220326
[Au] Autor:Noh JY; Yoon SW; Kim DJ; Lee MS; Kim JH; Na W; Song D; Jeong DG; Kim HK
[Ad] Endereço:Infectious Disease Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea.
[Ti] Título:Simultaneous detection of severe acute respiratory syndrome, Middle East respiratory syndrome, and related bat coronaviruses by real-time reverse transcription PCR.
[So] Source:Arch Virol;162(6):1617-1623, 2017 Jun.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Since severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome (MERS) coronaviruses (CoVs) share similar characteristics with respect to clinical signs, etiology, and transmission, methods for a rapid and accurate differential diagnosis are important. Therefore, the aim of this study was to develop a duplex real-time reverse transcription (RT)-PCR method for the simultaneous detection of these viruses. Primers and probes that target the conserved spike S2 region of human SARS-CoV, MERS-CoV, and their related bat CoVs were designed. The results of real-time RT-PCR showed specific reactions for each virus with adequate detection limits of 50-100 copies/mL and 5-100 copies/mL using pUC57-SARS-pS2 (a template for SARS-CoV) and pGEM-MERS-S2 (a template for MERS-CoV), respectively. In addition, this real-time RT-PCR system was able to detect the target viruses SARS-like bat CoV and MERS-CoV in bat fecal samples and sputum of MERS patients, respectively. Therefore, this newly developed real-time RT-PCR method is expected to detect not only SARS-CoV and MERS-CoV in humans but also several bat CoVs that are closely related to these viruses in bats.
[Mh] Termos MeSH primário: Coronaviridae/isolamento & purificação
Coronavírus da Síndrome Respiratória do Oriente Médio/isolamento & purificação
Reação em Cadeia da Polimerase em Tempo Real/métodos
Reação em Cadeia da Polimerase Via Transcriptase Reversa/métodos
Vírus da SARS/isolamento & purificação
[Mh] Termos MeSH secundário: Animais
Quirópteros/virologia
Coronaviridae/genética
Infecções por Coronavirus/virologia
Diagnóstico Diferencial
Fezes/virologia
Seres Humanos
Limite de Detecção
Coronavírus da Síndrome Respiratória do Oriente Médio/genética
RNA Viral/genética
Vírus da SARS/genética
Alinhamento de Sequência
Síndrome Respiratória Aguda Grave/virologia
Escarro/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Viral)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170720
[Lr] Data última revisão:
170720
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170222
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3281-9



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