Base de datos : MEDLINE
Búsqueda : B04.820.545.405.400.106 [Categoria DeCS]
Referencias encontradas : 31 [refinar]
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  1 / 31 MEDLINE  
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PMID:28402848
Autor:Tzarum N; de Vries RP; Peng W; Thompson AJ; Bouwman KM; McBride R; Yu W; Zhu X; Verheije MH; Paulson JC; Wilson IA
Dirección:Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Título:The 150-Loop Restricts the Host Specificity of Human H10N8 Influenza Virus.
Fuente:Cell Rep; 19(2):235-245, 2017 Apr 11.
ISSN:2211-1247
País de publicación:United States
Idioma:eng
Resumen:Adaptation of influenza A viruses to new hosts are rare events but are the basis for emergence of new influenza pandemics in the human population. Thus, understanding the processes involved in such events is critical for anticipating potential pandemic threats. In 2013, the first case of human infection by an avian H10N8 virus was reported, yet the H10 hemagglutinin (HA) maintains avian receptor specificity. However, the 150-loop of H10 HA, as well as related H7 and H15 subtypes, contains a two-residue insert that can potentially block human receptor binding. Mutation of the 150-loop on the background of Q226L and G228S mutations, which arose in the receptor-binding site of human pandemic H2 and H3 viruses, resulted in acquisition of human-type receptor specificity. Crystal structures of H10 HA mutants with human and avian receptor analogs, receptor-binding studies, and tissue staining experiments illustrate the important role of the 150-loop in H10 receptor specificity.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Hemagglutinins); 0 (Mutant Proteins)


  2 / 31 MEDLINE  
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PMID:27983474
Autor:Kuah LF; Tang LH; Sutton T; Lim JH; Sin WL; Lamirande E; Subbarao K; Lau YF
Dirección:1​Host-Pathogen Interactions Laboratory, DMERI, DSO National Laboratories, 27 Medical Drive, Singapore 117510, Singapore.
Título:Induction of protective immunity against influenza A/Jiangxi-Donghu/346/2013 (H10N8) in mice.
Fuente:J Gen Virol; 98(2):155-165, 2017 Feb.
ISSN:1465-2099
País de publicación:England
Idioma:eng
Resumen:Human infections with A/Jiangxi-Donghu/346/2013 (H10N8) virus have raised concerns about its pandemic potential. In order to develop a vaccine against this virus, the immunogenicity of its haemagglutinin protein was evaluated in mice. Using both whole-virion and recombinant subunit protein vaccines, we showed that two doses of either vaccine elicited neutralizing antibody responses. The protective efficacy of the vaccine-induced responses was assessed using a reverse-genetics-derived H10 reassortant virus on the A/Puerto Rico/8/34 (H1N1) backbone. The reassortant virus replicated efficiently in the respiratory tract of unvaccinated mice whereas vaccinated mice were completely protected from challenge, with no detectable viral load in the lower respiratory tract. Finally, the serum neutralizing antibody responses elicited by the H10 vaccines also exhibited cross-neutralizing activity against three heterologous wild-type H10 viruses. Collectively, these findings demonstrate that different vaccine platforms presenting the H10 haemagglutinin protein induce protective immunity.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Antibodies, Neutralizing); 0 (Antibodies, Viral); 0 (Hemagglutinin Glycoproteins, Influenza Virus); 0 (Influenza Vaccines); 0 (Vaccines, Synthetic)


  3 / 31 MEDLINE  
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PMID:26782141
Autor:Xiao C; Ma W; Sun N; Huang L; Li Y; Zeng Z; Wen Y; Zhang Z; Li H; Li Q; Yu Y; Zheng Y; Liu S; Hu P; Zhang X; Ning Z; Qi W; Liao M
Dirección:National and Local Joint Engineering Laboratory for Medicament of Zoonosis Prevention and Control, College of Veterinary Medicine, South China Agricultural University, Guangzhou, Guangdong Province 510642, People's Republic of China.
Título:PB2-588 V promotes the mammalian adaptation of H10N8, H7N9 and H9N2 avian influenza viruses.
Fuente:Sci Rep; 6:19474, 2016 Jan 19.
ISSN:2045-2322
País de publicación:England
Idioma:eng
Resumen:Human infections with avian influenza H7N9 or H10N8 viruses have been reported in China, raising concerns that they might cause human epidemics and pandemics. However, how these viruses adapt to mammalian hosts is unclear. Here we show that besides the commonly recognized viral polymerase subunit PB2 residue 627 K, other residues including 87E, 292 V, 340 K, 588 V, 648 V, and 676 M in PB2 also play critical roles in mammalian adaptation of the H10N8 virus. The avian-origin H10N8, H7N9, and H9N2 viruses harboring PB2-588 V exhibited higher polymerase activity, more efficient replication in mammalian and avian cells, and higher virulence in mice when compared to viruses with PB2-588 A. Analyses of available PB2 sequences showed that the proportion of avian H9N2 or human H7N9 influenza isolates bearing PB2-588 V has increased significantly since 2013. Taken together, our results suggest that the substitution PB2-A588V may be a new strategy for an avian influenza virus to adapt mammalian hosts.
Tipo de publicación:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nombre de substancia:0 (Viral Proteins); EC 2.7.7.48 (RNA Replicase)


  4 / 31 MEDLINE  
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PMID:26529299
Autor:Tretyakova I; Hidajat R; Hamilton G; Horn N; Nickols B; Prather RO; Tumpey TM; Pushko P
Dirección:Medigen, Inc., 8420 Gas House Pike, Suite S, Frederick, MD, USA.
Título:Preparation of quadri-subtype influenza virus-like particles using bovine immunodeficiency virus gag protein.
Fuente:Virology; 487:163-71, 2016 Jan.
ISSN:1096-0341
País de publicación:United States
Idioma:eng
Resumen:Influenza VLPs comprised of hemagglutinin (HA), neuraminidase (NA), and matrix (M1) proteins have been previously used for immunological and virological studies. Here we demonstrated that influenza VLPs can be made in Sf9 cells by using the bovine immunodeficiency virus gag (Bgag) protein in place of M1. We showed that Bgag can be used to prepare VLPs for several influenza subtypes including H1N1 and H10N8. Furthermore, by using Bgag, we prepared quadri-subtype VLPs, which co-expressed within the VLP the four HA subtypes derived from avian-origin H5N1, H7N9, H9N2 and H10N8 viruses. VLPs showed hemagglutination and neuraminidase activities and reacted with specific antisera. The content and co-localization of each HA subtype within the quadri-subtype VLP were evaluated. Electron microscopy showed that Bgag-based VLPs resembled influenza virions with the diameter of 150-200nm. This is the first report of quadri-subtype design for influenza VLP and the use of Bgag for influenza VLP preparation.
Tipo de publicación:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
Nombre de substancia:0 (Antibodies, Viral); 0 (Gene Products, gag); 0 (Hemagglutinin Glycoproteins, Influenza Virus); 0 (Vaccines, Virus-Like Particle); EC 3.2.1.18 (Neuraminidase)


  5 / 31 MEDLINE  
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PMID:26477933
Autor:Mei K; Liu G; Chen Z; Gao Z; Zhao L; Jin T; Yu X; Chen Q
Dirección:CAS Key Laboratory of Special Pathogens and Biosafety, Wuhan Institute of Virology, Chinese Academy of Sciences, Hubei 430071, China; Hubei Collaborative Innovation Center for Green Transformation of Bio-resources, Hubei Key Laboratory of Industrial Biotechnology, College of Life Sciences, Hubei Uni
Título:Deep sequencing reveals the viral adaptation process of environment-derived H10N8 in mice.
Fuente:Infect Genet Evol; 37:8-13, 2016 Jan.
ISSN:1567-7257
País de publicación:Netherlands
Idioma:eng
Resumen:The H10N8 virus was isolated from the water of Dongting Lake, China. Mice were infected while showing no obvious symptoms and replication was restricted to the lungs. When the wild-type virus was serially passaged in the lungs of mice, the resulting viruses became lethal and capable of replication in many other organs. This offered an applicable model for the exploration of viral genome gradual mutation during adaptation in mice. The different passage viruses from mice lung lavage were named P1, P3, P5, and P7, respectively. We sequenced the four viruses using next-generation sequencing (NGS) to analyze the dynamics of the H10N8 viral genome, polymorphism, and amino acid mutation of related proteins. We aimed to demonstrate how a mutant strain of low pathogenicity could become lethal to mice. Using Illumina high-throughput data, we detected the gradual mutations of F277S, C278Q, F611S and L653P in the polymerase acidic (PA) protein, and of L207V and E627K in the PB2 protein during adaptation. Interestingly, many amino acid sites mutated quickly; the others did so more slowly and remained in a heterozygous state for several generations. The PA amino acids S277 and Q278 have previously been found in clinical wild-type strains, including the human-H10N8 isolate in 2013. This demonstrates that the wild-type H10N8 virus had mutated to adapt to mammalian hosts. These data provide important reference information for influenza virus research.
Tipo de publicación:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nombre de substancia:0 (PA protein, influenza viruses); 0 (PB2 protein, Influenzavirus A); 0 (RNA, Viral); 0 (Viral Proteins); EC 2.7.7.48 (RNA Replicase)


  6 / 31 MEDLINE  
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PMID:26512088
Autor:Wohlbold TJ; Chromikova V; Tan GS; Meade P; Amanat F; Comella P; Hirsh A; Krammer F
Dirección:Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York, USA Graduate School of Biomedical Sciences, Icahn School of Medicine at Mount Sinai, New York, New York, USA.
Título:Hemagglutinin Stalk- and Neuraminidase-Specific Monoclonal Antibodies Protect against Lethal H10N8 Influenza Virus Infection in Mice.
Fuente:J Virol; 90(2):851-61, 2015 Oct 28.
ISSN:1098-5514
País de publicación:United States
Idioma:eng
Resumen:UNLABELLED: Between November 2013 and February 2014, China reported three human cases of H10N8 influenza virus infection in the Jiangxi province, two of which were fatal. Using hybridoma technology, we isolated a panel of H10- and N8-directed monoclonal antibodies (MAbs) and further characterized the binding reactivity of these antibodies (via enzyme-linked immunosorbent assay) to a range of purified virus and recombinant protein substrates. The H10-directed MAbs displayed functional hemagglutination inhibition (HI) and neutralization activity, and the N8-directed antibodies displayed functional neuraminidase inhibition (NI) activity against H10N8. Surprisingly, the HI-reactive H10 antibodies, as well as a previously generated, group 2 hemagglutinin (HA) stalk-reactive antibody, demonstrated NI activity against H10N8 and an H10N7 strain; this phenomenon was absent when virus was treated with detergent, suggesting the anti-HA antibodies inhibited neuraminidase enzymatic activity through steric hindrance. We tested the prophylactic efficacy of one representative H10-reactive, N8-reactive, and group 2 HA stalk-reactive antibody in vivo using a BALB/c challenge model. All three antibodies were protective at a high dose (5 mg/kg). At a low dose (0.5 mg/kg), only the anti-N8 antibody prevented weight loss. Together, these data suggest that antibody targets other than the globular head domain of the HA may be efficacious in preventing influenza virus-induced morbidity and mortality. IMPORTANCE: Avian H10N8 and H10N7 viruses have recently crossed the species barrier, causing morbidity and mortality in humans and other mammals. Although these reports are likely isolated incidents, it is possible that more cases may emerge in future winter seasons, similar to H7N9. Furthermore, regular transmission of avian influenza viruses to humans increases the risk of adaptive mutations and reassortment events, which may result in a novel virus with pandemic potential. Currently, no specific therapeutics or vaccines are available against the H10N8 influenza virus subtype. We generated a panel of H10- and N8-reactive MAbs. Although these antibodies may practically be developed into therapeutic agents, characterizing the protective potential of MAbs that have targets other than the HA globular head domain will provide insight into novel antibody-mediated mechanisms of protection and help to better understand correlates of protection for influenza A virus infection.
Tipo de publicación:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
Nombre de substancia:0 (Antibodies, Monoclonal); 0 (Antibodies, Neutralizing); 0 (Antibodies, Viral); 0 (Hemagglutinin Glycoproteins, Influenza Virus); 0 (Immunologic Factors); 0 (Viral Proteins); EC 3.2.1.18 (NA protein, influenza A virus); EC 3.2.1.18 (Neuraminidase)


  7 / 31 MEDLINE  
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PMID:26378283
Autor:Bao H; Feng X; Ma Y; Shi J; Zhao Y; Gu L; Wang X; Chen H
Dirección:Animal Influenza Laboratory of the Ministry of Agriculture, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, People's Republic of China.
Título:Rapid Detection of Subtype H10N8 Influenza Virus by One-Step Reverse Transcription-Loop-Mediated Isothermal Amplification Methods.
Fuente:J Clin Microbiol; 53(12):3884-7, 2015 Dec.
ISSN:1098-660X
País de publicación:United States
Idioma:eng
Resumen:We developed hemagglutinin- and neuraminidase-specific one-step reverse transcription-loop-mediated isothermal amplification assays for detecting the H10N8 virus. The detection limit of the assays was 10 copies of H10N8 virus, and the assays did not amplify nonspecific RNA. The assays can detect H10N8 virus from chicken samples with high sensitivity and specificity, and they can serve as an effective tool for detecting and monitoring H10N8 virus in live poultry markets.
Tipo de publicación:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nombre de substancia:0 (Hemagglutinin Glycoproteins, Influenza Virus); 0 (Viral Proteins); EC 3.2.1.18 (NA protein, influenza A virus); EC 3.2.1.18 (Neuraminidase)


  8 / 31 MEDLINE  
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PMID:26350451
Autor:Chen H; Huang L; Li H; Zhou X; Li H; Sun N; Qi W; Xiao C; Ni X; Liu M; Liao M
Dirección:Department of Infectious Diseases, Nanchang Center for Disease Control and Prevention, Nanchang, China; College of Veterinary Medicine, South China Agricultural University, Guangzhou, China.
Título:High Pathogenicity of Influenza A (H10N8) Virus in Mice.
Fuente:Am J Trop Med Hyg; 93(6):1360-3, 2015 Dec.
ISSN:1476-1645
País de publicación:United States
Idioma:eng
Resumen:Three human cases of H10N8 virus infections were initially reported in China in late 2013 and early 2014, two of which were fatal. This was the first time the H10N8 subtype has been detected in humans, and the pathogenicity of this virus remains under characterized. We first assessed its pathogenicity by infecting BALB/c mice with two H10N8 isolates, A/Jiangxi-Donghu/346-1/2013 and A/Chicken/Jiangxi/102/2013. The human isolate (H346-1) demonstrated stronger capability of replication and induced higher cytokine response in vivo than the chicken isolate (C102). In addition, H346-1 was fatal to mice, while all mice (N = 14) in C102-infected group survived during the infection course without weight loss. We hypothesized that the 627K mutation in the PB2 gene (PB2-K627) in H346-1 was associated with high pathogenicity in mice. Taken together, this study based on mouse model provides some insight into understanding the pathogenicity of the emerging viruses in mammals.
Tipo de publicación:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nombre de substancia:0 (Cytokines)


  9 / 31 MEDLINE  
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PMID:26079843
Autor:Ramos I; Mansour M; Wohlbold TJ; Ermler ME; Hirsh A; Runstadler JA; Fernandez-Sesma A; Krammer F
Título:Hemagglutinin Receptor Binding of a Human Isolate of Influenza A(H10N8) Virus.
Fuente:Emerg Infect Dis; 21(7):1197-201, 2015 Jul.
ISSN:1080-6059
País de publicación:United States
Idioma:eng
Resumen:Three cases of influenza A(H10N8) virus infection in humans have been reported; 2 of these infected persons died. Characterization of the receptor binding pattern of H10 hemagglutinin from avian and human isolates showed that both interact weakly with human-like receptors and maintain strong affinity for avian-like receptors.
Tipo de publicación:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
Nombre de substancia:0 (Hemagglutinins); 0 (Receptors, Virus)


  10 / 31 MEDLINE  
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PMID:25993111
Autor:Chen S; Li Z; Hu M; Guo S; Wu J; Wang B; Hu W; Sun Y; Li H; Liu M; Moore JB; Chen H
Dirección:Nanchang Centre for Disease Control and Prevention, Nanchang, Jiangxi Province, The People's Republic of China.
Título:Knowledge, Attitudes, and Practices (KAP) Relating to Avian Influenza (H10N8) among Farmers' Markets Workers in Nanchang, China.
Fuente:PLoS One; 10(5):e0127120, 2015.
ISSN:1932-6203
País de publicación:United States
Idioma:eng
Resumen:Three cases of avian influenza virus H10N8 were reported in Nanchang, China, as of April 2014. To identify the knowledge, attitudes, and practices (KAP) related to H10N8 among farmers' market workers, a cross-sectional survey was conducted in 63 farmers' markets in Nanchang. Using the resulting data, characteristics of poultry and non-poultry workers' knowledge, attitudes, and practice were described. Results suggest that interventions targeting high-risk workers should be developed and implemented by public health agencies to prevent the spread of H10N8. Additionally policies that encourage farmers' market workers to receive influenza vaccine should be developed, adopted, and enforced.
Tipo de publicación:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T



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