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#Avian #Influenza #H7N9 in #China: Preventing the Next #SARS (@WHO, Apr. 2 ‘17)

  Title : #Avian #Influenza #H7N9 in #China: Preventing the Next #SARS. Subject : Avian Influenza, H7N9 subtype (Asian Lineage), poultry e...

8 May 2017

#Influenza Virus – #Journals #Archives, recent added articles (May 8 2017)

 

Title: #Influenza Virus – #Journals #Archives, recent added articles (May 8 2017).

Subject: Human and Animal Influenza Viruses research, deep web scanning for Journals’ Archives.

Source: WorldWideScience.org, full page: (LINK).

Code: [  R  ]

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See more at –> WorldWideScience.org - Alerts for 2017-05-08

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Recently added:

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      • Wang, Yang; Wu, Jialing; Xue, Chunyi; Wu, Zhihui; Lin, Ying; Wei, Ying; Wei, Xiaona; Qin, Jianru; Zhang, Yun; Wen, Zhifen; Chen, Li; Liu, George Dacai; Cao, Yongchang
      • 2017-04-10  PubMed
      • DOI: 10.1016/j.antiviral.2017.03.029  Volume: 143  Pages: 97-105
      • Keywords: Cross-protection, H7N9, Hemagglutinin, Influenza A virus, Transmembrane domain, Trimerization
        • Influenza A H7N9 virus is the latest emerging pandemic threat, and has rapidly diverged into three clades, demanding a H7N9 virus vaccine with broadened protection against unmatched strains. Hemagglutinin (HA)-based structural design approaches for stabilizing HA proteins have provided excitingly promising results. However, none of the HA-based structural design approaches has been applied to a recombinant replicative influenza virus. Here we report that our HA-based structural design approach is a first in the field to generate a recombinant replicative H7N9 virus (H7N9-53TM) showing broadened protection. The H7N9-53TM contains a replaced H3 HA transmembrane domain (TM) in its HA protein. In mice, the inactivated H7N9-53TM vaccine induced significantly higher HI titers, HA-specific IgG titers, and IFN-γ production than the corresponding H7N9-53WT inactivated virus vaccine containing wild-type HA. More excitingly, mice immunized with the H7N9-53TM showed full protection against homologous (H7N9-53) and interclade (H7N9-MCX) challenges with minimal weight loss, no detectable lung viral loads, and no apparent pulmonary lesions and inflammation, while mice immunized with the H7N9-53WT showed partial protection (only 60% against H7N9-MCX) with severe weight loss, detectable lung viral loads, and severe pulmonary lesions and inflammation. In summary, this study presents a better vaccine candidate (H7N9-53TM) against H7N9 pandemics. Furthermore, our HA-based structural design approach would be conceivably applicable to other subtype influenza viruses, especially the viruses from emerging pandemic and epidemic influenza viruses such as H5N1 and H1N1. Copyright © 2017. Published by Elsevier B.V.
      • Qi Tang; Meiying Shao; Lingzhong Xu
      • 2017-03-22  BioScience Trends
      • DOI: 10.5582/bst.2017.01041  ISSN: 1881-7815  Volume: 11  Issue: 1  Pages: 122-124
      • Full Text Available
      • Wada, Yamato; Nithichanon, Arnone; Nobusawa, Eri; Moise, Leonard; Martin, William D; Yamamoto, Norio; Terahara, Kazutaka; Hagiwara, Haruhisa; Odagiri, Takato; Tashiro, Masato; Lertmemongkolchai, Ganjana; Takeyama, Haruko; Groot, Anne S De; Ato, Manabu; Takahashi, Yoshimasa
      • 2017-04-28  PubMed
      • DOI: 10.1038/s41598-017-01372-5  Volume: 7  Issue: 1  Pages: 1283
        • Influenza vaccines of H7N9 subtype are consistently less immunogenic in humans than vaccines developed for other subtypes. Although prior immunoinformatic analysis identified T-cell epitopes in H7 hemagglutinin (HA) which potentially enhance regulatory T cell response due to conservation with the human genome, the links between the T-cell epitopes and low immunogenicity of H7 HA remains unknown due to the lack of animal models reproducing the response observed in humans. Here, we utilized a humanized mouse model to recapitulate the low immunogenicity of H7 HA. Our analysis demonstrated that modification of a single H7 epitope by changing 3 amino acids so that it is homologous with a known H3 immunogenic epitope sequence significantly improved the immunogenicity of the H7 HA in the humanized mouse model, leading to a greater than 4-fold increase in HA-binding IgG responses. Thus, we provide experimental evidence for the important contribution of this H7-specific T cell epitope in determining the immunogenicity of an influenza vaccine. Furthermore, this study delineates strategies that can be used for screening and selecting vaccine strains using immunoinformatics tools and a humanized mouse model.
      • Yinzhong Shen; Hongzhou Lu
      • 2017-03-22  BioScience Trends
      • DOI: 10.5582/bst.2017.01040  ISSN: 1881-7815  Volume: 11  Issue: 1  Pages: 120-121
      • Full Text Available
      • Dai, Meiling; McBride, Ryan; Dortmans, Jos C F M; Peng, Wenjie; Bakkers, Mark J G; de Groot, Raoul J; van Kuppeveld, Frank J M; Paulson, James C; de Vries, Erik; de Haan, Cornelis A M
      • 2017-05-01  PubMed
      • DOI: 10.1128/JVI.00049-17  Volume: 91  Issue: 9
      • Keywords: H7N9, hemagglutinin, influenza A virus, neuraminidase, sialic acid
        • The emergence of the novel influenza A virus (IAV) H7N9 since 2013 has caused concerns about the ability of the virus to spread between humans. Analysis of the receptor-binding properties of the H7 protein of a human isolate revealed modestly increased binding to α2,6 sialosides and reduced, but still dominant, binding to α2,3-linked sialic acids (SIAs) compared to a closely related avian H7N9 virus from 2008. Here, we show that the corresponding N9 neuraminidases (NAs) display equal enzymatic activities on a soluble monovalent substrate and similar substrate specificities on a glycan array. In contrast, solid-phase activity and binding assays demonstrated reduced specific activity and decreased binding of the novel N9 protein. Mutational analysis showed that these differences resulted from substitution T401A in the 2nd SIA-binding site, indicating that substrate binding via this site enhances NA catalytic activity. Substitution T401A in the novel N9 protein appears to functionally mimic the substitutions that are found in the 2nd SIA-binding site of NA proteins of avian-derived IAVs that became human pandemic viruses. Our phylogenetic analyses show that substitution T401A occurred prior to substitutions in hemagglutinin (HA), causing the altered receptor-binding properties mentioned above. Hence, in contrast to the widespread assumption that such changes in NA are obtained only after acquisition of functional changes in HA, our data indicate that mutations in the 2nd SIA-binding site may have enabled and even driven the acquisition of altered HA receptor-binding properties and may have contributed to the spread of the novel H7N9 viruses.IMPORTANCE Novel H7N9 IAVs continue to cause human infections and pose an ongoing public health threat. Here, we show that their N9 proteins display reduced binding to and lower enzymatic activity against multivalent substrates, resulting from mutation of the 2nd sialic acid-binding site. This mutation preceded and may have driven the selection of substitutions in H7 that modify H7 receptor-binding properties. Of note, all animal IAVs that managed to cross the host species barrier and became human viruses carry mutated 2nd sialic acid-binding sites. Screening of animal IAVs to monitor their potential to cross the host species barrier should therefore focus not only on the HA protein, but also on the functional properties of NA. Copyright © 2017 American Society for Microbiology.
      • Xu, Yu-Lin; Tang, Hai-Lin; Peng, Hao-Ran; Zhao, Ping; Qi, Zhong-Tian; Wang, Wen
      • 2017-04-25  PubMed
      • DOI: 10.18632/oncotarget.16016  Volume: 8  Issue: 17  Pages: 27715-27724
      • Keywords: H7N9 virus, Immune response, Immunity, Immunology and Microbiology Section, RIP3, influenza A virus, necroptosis, proinflammatory cytokines
        • Influenza H7N9 virus infection causes an acute, highly contagious respiratory illness that triggers cell death of infected cells and airway epithelial destruction. RIP3 is a key regulator of cell death responses to a growing number of viral and microbial agents. This study aimed to investigate the role of RIP3 in inflammation of influenza H7N9 virus infection. Here, RIP3 knock out (RIP3-/-) mice and littermate wild type mice were infected intranasally with influenza H7N9 virus (A/Fujian/S03/2015) to determine the contribution of RIP3 to the inflammatory response of influenza H7N9 virus infection. It was found that RIP3-/- mice infected with H7N9 virus showed higher survival and less weight loss, compared with wild type littermate mice. In addition, RIP3-/- mice had fewer regions of edema, infiltration with inflammatory cells, and alvelolar collapses, and the secretions of IL-1β, IL-6, RANTES and MIP-1 in BALF were significantly decreased on days 3 and 7 p.i. when compared with WT mice. Moreover, caspase 1/IL1β signaling was found to be invovled in RIP3 associated imflammation of influenza H7N9 virus, but not RIP3/MLKL dependent necrosis. In the conclusion, our results indicated that RIP3 deficiency can protect mice from the infection of influenza H7N9 virus by downregulating caspase 1/IL1β signaling, which provided edivence of the RIP3 invovled necroptosis independent manner.
      • Bahl, Kapil; Senn, Joe J; Yuzhakov, Olga; Bulychev, Alex; Brito, Luis A; Hassett, Kimberly J; Laska, Michael E; Smith, Mike; Almarsson, Örn; Thompson, James; Ribeiro, Amilcar Mick; Watson, Mike; Zaks, Tal; Ciaramella, Giuseppe
      • 2017-04-11  PubMed
      • DOI: 10.1016/j.ymthe.2017.03.035
      • Keywords: H10N8, H7N9, immunogenicity, influenza, mRNA, mRNA vaccines, pandemic, vaccines
        • Recently, the World Health Organization confirmed 120 new human cases of avian H7N9 influenza in China resulting in 37 deaths, highlighting the concern for a potential pandemic and the need for an effective, safe, and high-speed vaccine production platform. Production speed and scale of mRNA-based vaccines make them ideally suited to impede potential pandemic threats. Here we show that lipid nanoparticle (LNP)-formulated, modified mRNA vaccines, encoding hemagglutinin (HA) proteins of H10N8 (A/Jiangxi-Donghu/346/2013) or H7N9 (A/Anhui/1/2013), generated rapid and robust immune responses in mice, ferrets, and nonhuman primates, as measured by hemagglutination inhibition (HAI) and microneutralization (MN) assays. A single dose of H7N9 mRNA protected mice from a lethal challenge and reduced lung viral titers in ferrets. Interim results from a first-in-human, escalating-dose, phase 1 H10N8 study show very high seroconversion rates, demonstrating robust prophylactic immunity in humans. Adverse events (AEs) were mild or moderate with only a few severe and no serious events. These data show that LNP-formulated, modified mRNA vaccines can induce protective immunogenicity with acceptable tolerability profiles. Copyright © 2017 The Authors. Published by Elsevier Inc. All rights reserved.
      • Lin, Yong Ping; Yang, Zi Feng; Liang, Ying; Li, Zheng Tu; Bond, Helen S; Chua, Huiying; Luo, Ya Sha; Chen, Yuan; Chen, Ting Ting; Guan, Wen Da; Lai, Jimmy Chun Cheong; Siu, Yu Lam; Pan, Si Hua; Malik Peiris, J S; Cowling, Benjamin J; Mok, Chris Ka Pun
      • 2017-04-19  PubMed
      • DOI: 10.1186/s12879-017-2359-z  Volume: 17  Issue: 1  Pages: 286
      • 汪闻; 李永吉; 冯玉奇; 马建军
      • 2015-01-01  China health standard management
      • Issue: 16  Pages: 176-177
        • 目的:探讨人感染H7N9禽流感医院感染的预防和控制措施。方法在科学认识H7N9,及时调整各项方案,依照方案开展综合演练人感染H7N9禽流感医院感染的预防和控制措施同时,建立和完善落实正确的H7N9医院感染预防措施和制度。结果科学的医院感染预防措施,可有效地控制H7N9传染源、切断传播途径、保护高危人群。结论在H7N9流行期间正确制定和落实医院感染预防措施和制度,可防止和减少H7N9医院感染的发生。%Objective To investigate the prevention and control measures of human infection of H7N9 avian influenza hospital infection. Methods Scientific understanding H7N9 in a timely manner to adjust the plan, in accordance with the plan to carry out comprehensive training infection in the avian hospital infection prevention and control measures at the same time, to establish and improve the implementation of the correct H7N9 hospital infection prevention measures and systems. Results The hospital infection prevention measures can effectively control the H7N9 source of infection, cut off the route of transmission and protect the high risk population. Conclusion To develop and implement the prevention measures and system of hospital infection during H7N9 epidemic can prevent and reduce the occurrence of H7N9 hospital infection.
      • Xie, Jianfeng; Weng, Yuwei; Ou, Jianming; Zhao, Lin; Zhang, Yanhua; Wang, Jinzhang; Chen, Wei; Huang, Meng; Xiu, Wenqiong; Chen, Hongbin; Zhang, Yongjun; Wu, Binshan; He, Wenxiang; Zhu, Ying; You, Libin; Huang, Zhimiao; Zhang, Canming; Hong, Longtao; Wang, Wei; Zheng, Kuicheng
      • 2017-05-04  PubMed
      • DOI: 10.1038/s41598-017-01761-w  Volume: 7  Issue: 1  Pages: 1512
        • This study aimed to investigate the epidemiological, clinical, and virologic characteristics of avian influenza A (H7N9) confirmed cases from two family clusters in Southeast China. Epidemiological data of the H7N9 confirmed cases and their close contacts were obtained through interviews and reviews of medical records. Of the four patients in these two family clusters, two cases had mild symptoms, one had severe symptoms, and one died. Three of the four patients had a history of exposure to live poultry or contaminated environments. The complete genome sequences of the H7N9 viruses from the same family cluster were highly homologous, and the four isolated viruses from the two family clusters exhibited the virologic features of the H7N9 virus, in terms of transmissibility, pathogenicity, host adaptation, and antiviral drug resistance. In addition, our findings indicated that the A/Fujian/18/2015 viral strain contained an additional hemagglutinin G225D substitution, which preferentially binds α2,6-linked sialic acids. The results of this study demonstrate that one family cluster was infected through common exposure to live poultry or contaminated environments, and the other was more likely to be infected through the human-to-human route.

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Copyright © 2017 Deep Web Technologies, Inc. All Rights Reserved

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Keywords: Research; Abstracts; Avian Influenza; H7N9; WWS.

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