Relevant bibliographies by topics / Influenza A Virus, NMR

Academic literature on the topic 'Influenza A Virus, NMR'

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Published: 9 March 2023
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Journal articles on the topic "Influenza A Virus, NMR"

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Sabesan, Subramaniam, Jens O. Duus, Susana Neira, Peter Domaille, Soerge Kelm, James C. Paulson, and Klaus Bock. "Cluster sialoside inhibitors for influenza virus: synthesis, NMR, and biological studies." Journal of the American Chemical Society 114, no. 22 (October 1992): 8363–75. http://dx.doi.org/10.1021/ja00048a004.

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Jadhav, P., M. Borkar, K. Malbari, M. Joshi, and M. Kanyalkar. "DESIGN, SYNTHESIS AND MOLECULAR MECHANISM OF FEW NEURAMINIDASE INHIBITORS IN TREATMENT OF H1N1 BY NMR TECHNIQUES." INDIAN DRUGS 56, no. 02 (February 26, 2019): 7–15. http://dx.doi.org/10.53879/id.56.02.11584.

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Considering the issue of resistance to anti-influenza drugs, there is a need for discovery of new antiviral drugs. In view of this, flavones and their synthetic precursors i.e. chalcones were designed as inhibitors of influenza virus - H1N1 neuraminidase enzyme using structure-based drug design. Based on the best docking scores, some chalcone and flavone derivatives were synthesized and characterized by IR and proton NMR. Few of them were selected for 31P NMR studies, in order to probe the molecular mechanism of their antiviral action. Reasonably good correlation between docking scores and 31P NMR results were observed. As antiviral drugs are known to show membrane stabilizing effect on host cell, 31P NMR data for methoxy chalcone showed stabilization effect on model membrane pointing towards good antiviral activity which remained unaffected even after its cyclization to flavone. These derivatives can be explored further to provide a future therapeutic option for the treatment and prophylaxis of H1N1 viral infections.
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Cheong, H. "Structure of influenza virus panhandle RNA studied by NMR spectroscopy and molecular modeling." Nucleic Acids Research 27, no. 5 (March 1, 1999): 1392–97. http://dx.doi.org/10.1093/nar/27.5.1392.

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SABESAN, S., J. OE DUUS, S. NEIRA, P. DOMAILLE, S. KELM, J. C. PAULSON, and K. BOCK. "ChemInform Abstract: Cluster Sialoside Inhibitors for Influenza Virus: Synthesis, NMR, and Biological Studies." ChemInform 24, no. 7 (August 20, 2010): no. http://dx.doi.org/10.1002/chin.199307273.

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Chang, S., J. Zhang, X. Liao, X. Zhu, D. Wang, J. Zhu, T. Feng, et al. "Influenza Virus Database (IVDB): an integrated information resource and analysis platform for influenza virus research." Nucleic Acids Research 35, Database (January 3, 2007): D376—D380. http://dx.doi.org/10.1093/nar/gkl779.

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Toraya, S., A. Naito, S. Tuzi, and H. Saito. "pH-dependent Fusogenic Mechanism of Influenza Virus Hemagglutinin2(1-27)Using Solid-state NMR." Seibutsu Butsuri 41, supplement (2001): S132. http://dx.doi.org/10.2142/biophys.41.s132_3.

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Cheong, H. "Secondary structure of the panhandle RNA of influenza virus A studied by NMR spectroscopy." Nucleic Acids Research 24, no. 21 (November 1, 1996): 4197–201. http://dx.doi.org/10.1093/nar/24.21.4197.

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Elkins, Matthew R., Jonathan K. Williams, Martin D. Gelenter, Peng Dai, Byungsu Kwon, Ivan V. Sergeyev, Bradley L. Pentelute, and Mei Hong. "Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR." Proceedings of the National Academy of Sciences 114, no. 49 (November 20, 2017): 12946–51. http://dx.doi.org/10.1073/pnas.1715127114.

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The influenza M2 protein not only forms a proton channel but also mediates membrane scission in a cholesterol-dependent manner to cause virus budding and release. The atomic interaction of cholesterol with M2, as with most eukaryotic membrane proteins, has long been elusive. We have now determined the cholesterol-binding site of the M2 protein in phospholipid bilayers using solid-state NMR spectroscopy. Chain-fluorinated cholesterol was used to measure cholesterol proximity to M2 while sterol-deuterated cholesterol was used to measure bound-cholesterol orientation in lipid bilayers. Carbon–fluorine distance measurements show that at a cholesterol concentration of 17 mol%, two cholesterol molecules bind each M2 tetramer. Cholesterol binds the C-terminal transmembrane (TM) residues, near an amphipathic helix, without requiring a cholesterol recognition sequence motif. Deuterium NMR spectra indicate that bound cholesterol is approximately parallel to the bilayer normal, with the rough face of the sterol rings apposed to methyl-rich TM residues. The distance- and orientation-restrained cholesterol-binding site structure shows that cholesterol is stabilized by hydrophobic interactions with the TM helix and polar and aromatic interactions with neighboring amphipathic helices. At the 1:2 binding stoichiometry, lipid 31P spectra show an isotropic peak indicative of high membrane curvature. This M2–cholesterol complex structure, together with previously observed M2 localization at phase boundaries, suggests that cholesterol mediates M2 clustering to the neck of the budding virus to cause the necessary curvature for membrane scission. The solid-state NMR approach developed here is generally applicable for elucidating the structural basis of cholesterol’s effects on membrane protein function.
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Zhang, Yun, Brian D. Aevermann, Tavis K. Anderson, David F. Burke, Gwenaelle Dauphin, Zhiping Gu, Sherry He, et al. "Influenza Research Database: An integrated bioinformatics resource for influenza virus research." Nucleic Acids Research 45, no. D1 (September 26, 2016): D466—D474. http://dx.doi.org/10.1093/nar/gkw857.

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Liao, Yu-Chieh, Chin-Yu Ko, Ming-Hsin Tsai, Min-Shi Lee, and Chao A. Hsiung. "ATIVS: analytical tool for influenza virus surveillance." Nucleic Acids Research 37, suppl_2 (May 8, 2009): W643—W646. http://dx.doi.org/10.1093/nar/gkp321.

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Dissertations / Theses on the topic "Influenza A Virus, NMR"

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Lai, Chun-cheong, and 黎振昌. "STD-NMR as a novel method to study influenza virus-receptor interactions." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2011. http://hub.hku.hk/bib/B47849745.

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Influenza infections continue to be a global health concern that causing both seasonal epidemics and unpredictable pandemics. Hemagglutinin (HA) and Neuraminidase (NA) are the two major surface glycoproteins of influenza viruses, which are important for their host cell sialic acid (Sia) receptor binding and cleaving activities. Although numerous methods have been developed to study the HA and NA interactions with sialic acid, x-ray crystallography remained the only method to provide detailed information at atomic resolution. The aim of this study is to develop and evaluate a novel strategy for the investigation of influenza virus-receptor interactions, which is able to provide information about an interaction down to atomic resolution. Influenza virus-like particles (VLPs) containing HA and NA separately were developed and it was reported here for the first time that sole expression of NA in mammalian cell led to VLP formation. Characterization of these VLPs demonstrated that they are non-infectious, but morphologically and biochemically mimic the native viruses. Therefore the VLPs can be regarded as an ideal research model to study the HA-Sia interaction without the interference of NA, or vice versa. Saturation transfer difference (STD) NMR spectroscopy is a state-of-the-art technology to determine how a binding-ligand interacts with its target protein. Modification of STD-NMR methodology was performed to adapt the technique to influenza VLP system. HA-Sia interaction was investigated in great detail and group epitope mapping of the interacting ligands was performed by analyzing the STD-NMR spectra. The data obtained are in a good agreement with the well established crystallography technique, reflecting the reliability of the STD-NMR technology. Regarding the NA-Sia interaction, my data demonstrated that substrate-hydrolysis specificity of NA is dependent on the binding of NA to those ligands. In addition, using competition experiments with NA inhibitor, a secondary sialic acid binding site was detected. It is the first direct experimental evidence that confirms avian, seasonal human and human pandemic swine-origin influenza virus N1 neuraminidases exhibit a distinct secondary binding site. In conclusion, here I presented a novel interdisciplinary strategy using VLP and NMR technology to study the interaction of influenza virus with its receptor. This method is unique in its ability to provide detailed information on the HA and NA interactions with sialic acid leading to group epitope mapping of the binding ligands, which will help us not only to understand the virus tropism but also to define new therapeutic targets.
published_or_final_version
Microbiology
Doctoral
Doctor of Philosophy
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MACCHI, ELEONORA. "NMR as a tool for structural characterization of carbohydrates and glycan-protein interactions." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2015. http://hdl.handle.net/10281/69274.

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Il virus dell’influenza A è un virus a RNA formato da 8 geni, tre dei quali - emagglutinina (HA), neuramminidasi (NA) e polimerasi (PB) –, risultano particolarmente critici nell’infezione e nella trasmissione uomo-uomo. L’infezione inizia con il legame dell’HA del virus ai recettori glicanici presenti sulle cellule dell’ospite; questa interazione è altamente specifica, ed è governata dal tipo di legame tra l’acido sialico e il galattosio all’interno del recettore. I recettori umani glicanici, siti di riconoscimento per i virus human-adapted, sono espressi principalmente nel tratto superiore dell’epitelio respiratorio umano e presentano un legame α2→6 tra l’acido sialico e il galattosio nell’estremità non riducente. I virus aviari invece, riconoscono recettori glicanici che presentano un legame α2→3 tra acido neuraminico e il galattosio. Studi precedenti dell’interazione tra HA e trisaccaridi hanno dimostrato che sia la conformazione dei glicani, che il diverso tipo di legame tra acido sialico e galattosio sono fattori chiave per la regolazione dell’interazione. Partendo dalle sopracitate considerazioni questo lavoro di ricerca si è occupato di studiare la dinamica e la conformazione in soluzione di due pentasaccaridi, usati come modelli per il recettore aviario (LSTa, Neu5Ac-α(2→3)-Gal-β(1→3)-GlcNAc-β(1→3)-Gal-β(1→4)-Glc) e umano (LSTc, Neu5Ac-α(2→6)-Gal-β(1→4)-GlcNAc-β(1→3)-Gal-β(1→4)-Glc), utilizzando tecniche NMR (Nuclear Magnetic Resonance) e simulazioni di dinamica molecolare (MD). I nostri studi dimostrano che in soluzione i due recettori presentano diverse conformazioni, dinamiche e topologie. Queste peculiarità uniche comportano caratteristiche molecolari diverse per il riconoscimento di HA, dimostrando quindi la specificità dell’interazione tra recettore e emagglutinina. La relazione tra la specificità dell’HA verso i recettori e la trasmissibilità del virus è stata precedentemente dimostrata usando il prototipo del virus SC18 (H1N1) A/South Carolina/1/1918. Combinando tecniche di Risonanza Magnetica Nucleare e di dinamica molecolare, abbiamo dimostrato come, durante l’interazione, il sito di binding dell’emagglutinina imponga differenti vincoli conformazionali al recettore. Il virus pandemico SC18, che presenta un’efficacia di trasmissione negli uomini molto alta, a confronto con il singolo (NY18, Asp225 → Gly) e doppio (AV18, Asp190 → Glu e Asp225 → Gly) mutante, impone maggiori vincoli alla conformazione del recettore umano, proprietà correlata all’affinità dell’interazione recettore-HA, misurata tramite saggi biochimici. Questa relazione tra affinità e vincoli conformazionali imposti al recettore è stata osservata anche per il virus aviario-adattato AV18, il quale impone vincoli conformazionali maggiori al recettore aviario in confronto a quelli imposti a quest’ultimo da NY18. In particolare, è interessante osservare come emagglutinine differenti impongano vincoli conformazionali diversi a seconda che leghino recettori umani o aviari. In ultimo, abbiamo esteso il nostro studio a un virus meno pandemico, H7N9, e due suoi mutanti, i quali sono in grado di legare sia il recettore umano che aviario, allo scopo di capire come avviene l’interazione tramite l’utilizzo di tecniche NMR e di dinamica molecolare. In questo studio descriviamo le basi strutturali dell’interazione tra l’emagglutinina di nuovi virus e i recettori umani e aviari, combinando l’approccio sperimentale a tecniche computazionali. Questa metodologia potrà essere usata come strumento utile per la sorveglianza di nuovi virus pandemici.
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Liao, Shu-Yu Ph D. Massachusetts Institute of Technology. "Structure and dynamics of full-length M2 protein of influenza A virus from solid-state NMR." Thesis, Massachusetts Institute of Technology, 2017. http://hdl.handle.net/1721.1/113974.

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Thesis: Ph. D., Massachusetts Institute of Technology, Department of Chemistry, 2017.
Cataloged from PDF version of thesis.
Includes bibliographical references.
Solid-state nuclear magnetic resonance (SSNMR) has been frequently used to elucidate the structure and dynamics of membrane proteins and fibrils that are difficult to characterize by Xray crystallography or solution NMR. This thesis focuses on the structure determination and the proton conduction mechanism of the full-length matrix protein 2 (M2) of influenza A virus. The M2 membrane protein can be separated into three domains: an N-terminal ectodomain (1-2 1), an cc-helical transmembrane domain (TM) (22-46) connected to an amphipathic helix (AH) and a Cterminal cytoplasmic tail (63-97). The TM domain of M2 is responsible for proton conduction ant the ectodomain has been the target for vaccine development. The cytoplasmic tail has been implicated in M2 interaction with other viral proteins from mutagenesis studies. Given the importance of both N- and C-termini, it is essential to determine the structure and the dynamics of M2FL. Furthermore, we are interested in how the cytoplasmic tail affects proton conduction and the interaction of the anti-viral drug amantadine with M2 in the presence of the C-terminus. Using uniformly ¹³C, ¹⁵N-labeled M2FL, our water-selected 2D ¹³C-¹³C correlation experiment indicated that N- and C- termini are on the surface of the lipid bilayer moreover combining with chemical shift prediction, we determined that these two domains are mostly disordered. Deleting the ectodomain of M2FL (M2(21-97)) proved that a small [beta]-strand is located at the N-terminus only in the DMPC-bound state. The M2 conformation is found to be cholesterol-dependent since [beta]-strand is not found in cholesterol-rich membranes. M2(21-97) shows cationic histidine at higher pH, in contrast to M2TM, indicating that the cytoplasmic tail shifts the His37 pKa equilibria. Quantification of the ¹⁵N intensities revealed two pKa's as opposed to of four in M2TM suggesting cooperative proton binding. A possible explanation is that the large number of positively charged residues in the cytoplasmic tail facilitates proton conduction. The cytoplasmic tail was also found to restore drug-binding as amantadine no longer binds to M2(21-61) a in virus-mimetic membrane. These results have extended our understanding of the influence of the cytoplasmic domain on the structure and proton conduction of M2.
by Shu-Yu Liao.
Ph. D.
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Hornick, Emma E. L. "Contributions of NLRS to pathogenic and protective immune responses during influenza virus infection." Diss., University of Iowa, 2018. https://ir.uiowa.edu/etd/6139.

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Pattern recognition receptors, including members of the NBD and LLR-containing (NLR) family, are key sensors of infection and injury. Early sensing of pathogen invasion and subsequent activation of pro-inflammatory signaling cascades is essential for controlling infection. However, signaling pathways activated upon pathogen recognition can also contribute to inflammation-mediated tissue damage. The studies detailed in Chapters 3 and 4 are primarily concerned with the roles of two NLR family members, Nlrp12 and Nlrc4, during influenza A virus (IAV) infection. While IAV itself is cytopathic, the immune response is responsible for a great deal of the tissue damage during infection in some contexts. NLR family members are involved in both pathogen sensing and modulation of pro-inflammatory signaling, thus they are perfectly situated to shift the balance between pathogen clearance and immunopathology. Nlrp12 has been implicated in regulation of pro-inflammatory signaling through NFκB family members. In Chapter 3 we report that during IAV infection, we find no differences in those pathways, and instead we describe a novel role for Nlrp12 in regulating transcript stability. Previous work has shown that one of the key differences between lethal and sublethal IAV infections is the early and exaggerated recruitment of neutrophils. Previous studies in our laboratory had established a role for Nlrp12 in CXCL1-mediated neutrophil recruitment during respiratory bacterial infections. We therefore hypothesized that Nlrp12-/- mice would be protected from pathogenic neutrophil recruitment during lethal IAV infection due to decreased CXCL1 production. In Chapter 3 we show that indeed, Nlrp12-/- mice have improved survival, decreased pulmonary microvascular permeability, and decreased necrosis and hemorrhage in their airways compared to WT mice. Nlrp12-/- mice also have fewer neutrophils in their lungs, due to decreased production of CXCL1 by neutrophils, DCs and macrophages. Our data showing decreased Cxcl1 transcript stability in R848-treated Nlrp12-/- BMDCs strongly suggest that the reduction in CXCL1 production by DCs in the Nlrp12-/- lungs is a result of decreased Cxcl1 transcript stability. Nlrc4 is a best known as a member of the Nlrc4 inflammasome, which is activated upon sensing of Gram-negative bacterial pathogens. However, a recent study from our laboratory showed an inflammasome-independent role for Nlrc4 in supporting critical anti-tumor T cell responses. Given that T cells are also critical for successful resolution of IAV infection, we hypothesized that during IAV infection, Nlrc4-/- mice would have compromised IAV-specific T cell responses and therefore poorer survival. Indeed, our studies in Chapter 4 show that in IAV-infected Nlrc4-/- mice, the pulmonary IAV-specific CD4 T cell response is significantly diminished and mortality is significantly increased compared to WT mice. During IAV infection, the blunted CD4 T cell response is a result of increased death of the CD4 T cells, perhaps due to increased expression of FasL on CD11c+ cells in the Nlrc4-/- lung environment.
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Williams, Jonathan K., Alexander A. Shcherbakov, Jun Wang, and Mei Hong. "Protonation equilibria and pore-opening structure of the dual-histidine influenza B virus M2 transmembrane proton channel from solid-state NMR." AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2017. http://hdl.handle.net/10150/626055.

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The influenza A and B viruses are the primary cause of seasonal flu epidemics. Common to both viruses is the M2 protein, a homotetrameric transmembrane proton channel that acidifies the virion after endocytosis. Although influenza A M2 (AM2) and B M2 (BM2) are functional analogs, they have little sequence homology, except for a conserved HXXXW motif, which is responsible for proton selectivity and channel gating. Importantly, BM2contains a second titratable histidine, His-27, in the tetrameric transmembrane domain that forms a reverse WXXXH motif with the gating tryptophan. To understand how His-27 affects the proton conduction property of BM2, we have used solid-state NMR to characterize the pH-dependent structure and dynamics of His-27. In cholesterol-containing lipid membranes mimicking the virus envelope, N-15 NMR spectra show that the His-27 tetrad protonates with higher pKa values than His-19, indicating that the solvent-accessible His-27 facilitates proton conduction of the channel by increasing the proton dissociation rates of His-19. AM2is inhibited by the amantadine class of antiviral drugs, whereas BM2 has no known inhibitors. Wemeasured the N-terminal interhelical separation of the BM2 channel using fluorinated Phe-5. The interhelical F-19-F-19 distances show a bimodal distribution of a short distance of 7 angstrom and a long distance of 15-20 angstrom, indicating that the phenylene rings do not block small-molecule entry into the channel pore. These results give insights into the lack of amantadine inhibition of BM2 and reveal structural diversities in this family of viral proton channels.
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Harter, Cordula. "Zum Mechanismus der Interaktion der Ektodomäne von Influenza Virus Hämagglutinin mit Liposomen /." Zürich, 1988. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=8739.

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Delaforge, Elise. "Dynamique structurale et fonctionnelle du domaine C-terminal de la protéine PB2 du virus de la grippe A." Thesis, Université Grenoble Alpes (ComUE), 2015. http://www.theses.fr/2015GREAV037/document.

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La capacité du virus de la grippe aviaire à traverser la barrière des espèces et à devenir fortement pathogène chez les mammifères est un problème majeur de santé publique. Chez les oiseaux, la réplication a lieu dans l'intestin, à 4C, tandis que chez les humains elle a lieu dans l'appareil respiratoire, plus froid, à 33C. Il a été montré que l'adaptation à la température du virus de la grippe a lieu par de nombreuses mutations de la polymérase virale, notamment dans le domaine 627-NLS situé en C-terminal de la protéine PB2. Ce domaine est impliqué dans l'adaptation à l'hôte et interagit avec la protéine de l'hôte, importine alpha, étant donc indispensable pour l'entrée de la polymérase virale dans le noyau de la cellule [Tarendeau et al., 2008]. Les structures cristallographiques du 627-NLS et du complexe importine alpha/NLS existent. Cependant, lors de la superposition de ces structures via leur domaine NLS commun, un important choc stérique entre le domaine 627 et l'importine alpha devient évident. Ceci indique qu'une autre conformation du 627-NLS est requise pour l'interaction avec l'importine alpha [Boivin and Hart, 2011]. Dans cette étude, nous avons examiné les bases moléculaires de l'adaptation inter-espèces du virus à travers l'étude de la structure et de la dynamique du 627-NLS aviaire et humain. Nous avons identifié deux conformations du 627-NLS en échange lent (10-100 s-1), correspondant apparemment à une conformation ouverte et une conformation fermée des deux domaines. Nous proposons que la conformation ouverte du 627-NLS est la seule conformation compatible avec l'interaction avec l'importine alpha, et que l'équilibre entre conformation ouverte et fermée pourrait jouer le rôle de thermostat moléculaire, contrôlant l'efficacité de la réplication virale chez différents hôtes. La cinétique et la dynamique de ce comportement conformationnel important ainsi que de l'interaction entre le 627-NLS et l'importine alpha ont été caractérisées par résonance magnétique nucléaire (déplacements chimique, augmentation paramagnétique de la relaxation, relaxation de spin, transfert de saturation par l'échange chimique), combinée à la diffusion des rayons X et des neutrons aux petits angles ainsi qu'au transfert d'énergie par résonance de type Förster. Aussi, nous avons déterminé les affinités d'une série de mutants évolutifs du 627-NLS pour l'importine alpha et du 627-NLS aviaire ou humain pour différents isoformes de l'importine alpha, montrant que les affinités observées sont cohérentes avec les préférences d'interactions vues in vivo
The ability of avian influenza viruses to cross the species barrier and become dangerously pathogenic to mammalian hosts represents a major threat for human health. In birds the viral replication is carried out in the intestine at 40°C, while in humans it occurs in the cooler respiratory tract at 33°C. It has been shown that temperature adaption of the influenza virus occurs through numerous mutations in the viral polymerase, in particular in the C-terminal domain 627-NLS of the PB2 protein. This domain has already been shown to participate in host adaptation and is involved in importin alpha binding and therefore is required for entry of the viral polymerase into the nucleus [Tarendeau et al., 2008]. Crystallographic structures are available for 627-NLS and the complex importin alpha/NLS, however, a steric clash between importin alpha and the 627 domain becomes apparent when superimposing the NLS domain of the two structures, indicating that another conformation of 627-NLS is required for binding to importin alpha [Boivin and Hart, 2011]. Here we investigate the molecular basis of inter-species adaptation by studying the structure and dynamics of human and avian 627-NLS. We have identified two conformations of 627-NLS in slow exchange (10-100 s-1), corresponding to an apparently open and closed conformation of the two domains. We show that the equilibrium between closed and open conformations is strongly temperature dependent. We propose that the open conformation of 627-NLS is the only conformation compatible with binding to importin alpha and that the equilibrium between closed and open conformations may play a role as a molecular thermostat, controlling the efficiency of viral replication in the different species. The kinetics and domain dynamics of this important conformational behaviour and of the interaction between 627-NLS and importin alpha have been characterized using nuclear magnetic resonance chemical shifts, paramagnetic relaxation enhancement, spin relaxation and chemical exchange saturation transfer, in combination with X-ray and neutron small angle scattering and Förster resonance energy transfer. Also, we have determined the affinities of various evolutionnary mutants of 627-NLS to importin alpha and of avian and human 627-NLS to different isoforms of importin alpha, showing that the observed affinities are coherent with the preferred interactions seen in vivo
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Höfer, Chris Tina. "Influenza virus assembly." Doctoral thesis, Humboldt-Universität zu Berlin, Lebenswissenschaftliche Fakultät, 2015. http://dx.doi.org/10.18452/17251.

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Influenza A Viren besitzen ein segmentiertes, einzelsträngiges RNA-Genom, welches in Form viraler Ribonukleoprotein (vRNP)-Komplexe verpackt ist. Während das virale Genom im Zellkern repliziert wird, finden Assemblierung und Knospung reifer Viruspartikel an der apikalen Plasmamembran statt. Für die Virusbildung müssen die einzelnen viralen Komponenten hierher gebracht werden. Während intrinsische apikale Signale der viralen Transmembranproteine bekannt sind, sind der zielgerichtete Transport und der Einbau des viralen Genoms in neuentstehende Virionen noch wenig verstanden. In dieser Arbeit wurden potentielle Mechanismen des vRNP-Transportes untersucht, wie die Fähigkeit der vRNPs mit Lipidmembranen zu assoziieren und die intrinsische subzellulären Lokalisation des viralen Nukleoproteins (NP), eines Hauptbestandteils der vRNPs. Es konnte gezeigt werden, dass vRNPs nicht mit Lipidmembranen assoziieren, was mittels Flotation aufgereinigter vRNPs mit Liposomen unterschiedlicher Zusammensetzung untersucht wurde. Die Ergebnisse deuten jedoch darauf hin, dass das virale M1 in der Lage ist, Bindung von vRNPs an negativ-geladene Lipidmembranen zu vermitteln. Subzelluläre Lokalisation von NP wurde des Weiteren durch Expression fluoreszierender NP-Fusionsproteine und Fluoreszenzphotoaktivierung untersucht. Es konnte gezeigt werden, dass NP allein nicht mit zytoplasmatischen Strukturen assoziiert, stattdessen aber umfangreiche Interaktionen im Zellkern eingeht und mit hoher Affinität mit bestimmten Kerndomänen assoziiert, und zwar den Nukleoli sowie kleinen Kerndomänen, welche häufig in der Nähe von Cajal-Körperchen und PML-Körperchen zu finden waren. Schließlich wurde ein experimenteller Ansatz etabliert, welcher erlaubt, den Transport vRNP-ähnlicher Komplexe mittels Fluoreszenzdetektion aufzuzeichnen und Einzelpartikelverfolgungsanalysen durchzuführen. Unterschiedliche Phasen des vRNP-Transportes konnten beobachtet werden und ein 3-Phasen-Transportmodell wird skizziert.
Influenza A viruses have a segmented single-stranded RNA genome, which is packed in form of viral ribonucleoprotein (vRNP) complexes. While the viral genome is replicated and transcribed in the host cell nucleus, assembly and budding of mature virus particles take place at the apical plasma membrane. Efficient virus formation requires delivery of all viral components to this site. While intrinsic apical targeting signals of the viral transmembrane proteins have been identified, it still remains poorly understood how the viral genome is transported and targeted into progeny virus particles. In this study, potential targeting mechanisms were investigated like the ability of vRNPs to associate with lipid membranes and the intrinsic ability of the viral nucleoprotein (NP) – which is the major protein component of vRNPs – for subcellular targeting. It could be shown that vRNPs are not able to associate with model membranes in vitro, which was demonstrated by flotation of purified vRNPs with liposomes of different lipid compositions. Results indicated, however, that the matrix protein M1 can mediate binding of vRNPs to negatively charged lipid bilayers. Intrinsic subcellular targeting of NP was further investigated by expression of fluorescent NP fusion protein and fluorescence photoactivation, revealing that NP by itself does not target cytoplasmic structures. It was found to interact extensively with the nuclear compartment instead and to target specific nuclear domains with high affinity, in particular nucleoli and small interchromatin domains that frequently localized in close proximity to Cajal bodies and PML bodies. An experimental approach was finally established that allowed monitoring the transport of vRNP-like complexes in living infected cells by fluorescence detection. It was possible to perform single particle tracking and to describe different stages of vRNP transport between the nucleus and the plasma membrane. A model of three-stage transport is suggested.
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Green, P. C. "Serological and immunocytochemical studies on influenza virus and influenza virus infected cells." Thesis, University of Manchester, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.356114.

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Morgan, David John. "Defective interfering influenza virus reverses the immunopathological effects of standard influenza virus in mice." Thesis, University of Bristol, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.332491.

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Books on the topic "Influenza A Virus, NMR"

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Kawaoka, Yoshihiro, and Gabriele Neumann, eds. Influenza Virus. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-621-0.

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Yamauchi, Yohei, ed. Influenza Virus. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8678-1.

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Spackman, Erica, ed. Animal Influenza Virus. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0346-8.

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Spackman, Erica, ed. Avian Influenza Virus. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-279-3.

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Spackman, Erica, ed. Animal Influenza Virus. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0758-8.

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Animal influenza virus. New York: Humana Press, 2014.

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Erica, Spackman, ed. Avian influenza virus. Totowa, NJ: Humana Press, 2008.

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Influenza virus: Methods and protocols. New York: Humana, 2012.

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Morgan, David John. Dejective interfering influenza virus reverses the immunopathological effects of standard influenza virus in mice. [s.l.]: typescript, 1992.

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von Itzstein, Mark, ed. Influenza Virus Sialidase - A Drug Discovery Target. Basel: Springer Basel, 2012. http://dx.doi.org/10.1007/978-3-7643-8927-7.

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Book chapters on the topic "Influenza A Virus, NMR"

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Zinserling, Vsevolod A., and Vladimir A. Dedov. "Influenza Virus." In Infectious Disease and Parasites, 179–82. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-30009-2_1042.

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Kradin, Richard L., and Jay A. Fishman. "Influenza Virus." In Viruses and the Lung, 79–86. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-40605-8_9.

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Klenk, Hans Dieter. "Influenza-Virus." In Lexikon der Infektionskrankheiten des Menschen, 441–46. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-39026-8_512.

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Shahab, Shamsa Z., and W. Paul Glezen. "Influenza Virus." In Clinical Perspectives in Obstetrics and Gynecology, 215–23. New York, NY: Springer New York, 1994. http://dx.doi.org/10.1007/978-1-4612-2640-6_12.

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Hayden, Frederick G., and Peter Palese. "Influenza Virus." In Clinical Virology, 1009–58. Washington, DC, USA: ASM Press, 2016. http://dx.doi.org/10.1128/9781555819439.ch43.

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Matsubara, Teruhiko, and Toshinori Sato. "Influenza Virus." In Diamond Electrodes, 237–48. Singapore: Springer Singapore, 2022. http://dx.doi.org/10.1007/978-981-16-7834-9_15.

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Suarez, David L. "Influenza A virus." In Animal Influenza, 1–30. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2016. http://dx.doi.org/10.1002/9781118924341.ch1.

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Virmani, Nitin, S. Pavulraj, B. C. Bera, Taruna Anand, R. K. Singh, and B. N. Tripathi. "Equine Influenza Virus." In Emerging and Transboundary Animal Viruses, 215–38. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-0402-0_9.

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Luo, Ming. "Influenza Virus Entry." In Viral Molecular Machines, 201–21. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4614-0980-9_9.

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Nagarajan, S., Manoj Kumar, H. V. Murugkar, C. Tosh, and V. P. Singh. "Avian Influenza Virus." In Livestock Diseases and Management, 111–33. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-2651-0_5.

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Conference papers on the topic "Influenza A Virus, NMR"

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Ejima, Miho, Keiko Haraguchi, Tadashi Yamamoto, and Ayae Honda. "Effect of PB1c45 on Influenza Virus Replication." In 2006 IEEE International Symposium on MicroNanoMechanical and Human Science. IEEE, 2006. http://dx.doi.org/10.1109/mhs.2006.320241.

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Ueda, Ryuta, Akihiko Ichkawa, Mariko Kusunoki, Miho Ejima, Fumito Arai, Toshio Fukuda, and Ayae Honda. "Influenza virus selects cell phase for infection." In 2007 International Symposium on Micro-NanoMechatronics and Human Science. IEEE, 2007. http://dx.doi.org/10.1109/mhs.2007.4420821.

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Lee, Dongjin, Yogesh Chander, Sagar M. Goyal, and Tianhong Cui. "Carbon Nanotubes Swine Influenza (H1N1) Virus Sensors." In ASME 2010 International Mechanical Engineering Congress and Exposition. ASMEDC, 2010. http://dx.doi.org/10.1115/imece2010-40735.

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We present a label-free detection of swine influenza virus (SIV) H1N1 by means of the excellent electrical properties of single-walled carbon nanotubes (SWCNTs). The electrical resistance of SWCNT resistor tends to increase upon the surface adsorption of macromolecules such as poly-L-lysine, anti-SIV antibodies, and SIVs in the process of immunoassay. The SWCNT network resistor was successfully able to detect as low as 180 TCID50/ml of SIV using the resistance shifts upon immunobinding of SIVs. The sensor specificity was demonstrated against transmissible gastroenteritis virus (TGEV) and feline calicivirus (FCV). This facile CNT-based immnoassay has potential applications as a rapid point-of-care detection or a sensing platform for lab-on-a-chip systems.
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Mehrbod, Parvaneh, Aini Ideris, Abdul Rahman Omar, and Mohd Hair Bejo. "Statins as antiviral drugs against influenza virus." In 3rd Annual International Conference on Advances in Biotechnology (BioTech 2013). Global Science and Technology Forum, 2013. http://dx.doi.org/10.5176/2251-2489_biotech13.70.

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Marriott, HM, MK Whyte, and DH Dockrell. "Macrophage Apoptosis after Influenza A Virus Infection." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a5168.

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Pongsumpun, Puntani. "Local Stability of Influenza Virus with Vaccination." In ICISDM 2020: 2020 the 4th International Conference on Information System and Data Mining. New York, NY, USA: ACM, 2020. http://dx.doi.org/10.1145/3404663.3404684.

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Zavyalova, Elena G., Alexandra S.Gambaryan, Andrei Yu Olenin, Gleb A. Zhdanov, Vladimir I. Kukushkin, Georgii V. Lisichkin, Dmitry A. Gribanyov, and Oganes A. Ambartsumyan. "Optical nanostructured aptasensors for influenza virus detection." In 2021 International Conference on Information Technology and Nanotechnology (ITNT). IEEE, 2021. http://dx.doi.org/10.1109/itnt52450.2021.9649402.

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Ejima, Miho, Ryuta Ueda, Shinichiro Kume, Daisuke Okazaki, Takefumi Yamakawa, Hitoshi Shiku, and Ayae Honda. "Ebp1 expression is induced by influenza virus infection." In 2008 International Symposium on Micro-NanoMechatronics and Human Science (MHS). IEEE, 2008. http://dx.doi.org/10.1109/mhs.2008.4752452.

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Saleem, S., E. Shah, M. Corpuz, and M. Karwa. "Intractable Ventricular Fibrillation Following Influenza A Virus Infection." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a6583.

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Chronopoulos, J., E. Pernet, Y. Ishii, U. Fujii, M. Divangahi, and J. G. Martin. "Immunity to Influenza A Virus Infection During Pregnancy." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a2936.

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Reports on the topic "Influenza A Virus, NMR"

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Perk, Shimon, Maricarmen Garcia, Alexander Panshin, Caroline Banet-Noach, Irina Gissin, Mark W. Jackwood, and David Stallknecht. Avian Influenza Virus H9N2: Characterization and Control Strategies. United States Department of Agriculture, June 2007. http://dx.doi.org/10.32747/2007.7709882.bard.

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Control of Avian Influenza (AI) infection is a highly topical subject of major economicimportance for the worldwide poultry industry at the national level and for international trade.H9N2 viruses are endemic in poultry throughout Asia and the Middle East, causing major losses inproduction. Moreover, these viruses pose wider threats since they have been isolated from bothswine and humans. At the same time, study of the AI viruses affords an opportunity to explore anumber of problems of intriguing scientific interest. The overall goal of this project was to developa sound control strategy for avian influenza subtype H9N2 viruses (AI H9N2) in commercialpoultry in Israel. The one-year feasibility study focused on two main goals, namely: to study themolecular characteristics of AI H9N2 circulating during the last seven years in Israel and todevelop tools enabling differentiation between the immune response to vaccination and infectionwith H9N2.Genetic and phylogenetic characterization of 29 selected AI H9N2 isolates (2000-2006)was performed by complete sequencing of hemagglutinin (HA), neuraminidase (NA), and all sixinternal genes [nucleoprotein (NP), polymerase basic 1 (PB1), polymerase basic 2 (PB2),polymerase acid (PA), matrix (M), and nonstructural (NS) genes]; comparative phylogenetic andgenetic analyses of these sequences; and comparative genetic analyses of deduced amino acidsequences of the HA, NA, NS1, and NS2 proteins. The major conclusions of the molecularanalyses were: (1) Israeli isolates, together with other H9N2 viruses isolated in Middle Eastcountries, comprise a single regional sublineage related to the G1-lineage. In addition, Israeliisolates subdivided into three different subgroups. Genetic analysis of these viruses suggests thatthey underwent divergent evolution paths.
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Dimitrova, Adriana, Milka Mileva, Dimo Krastev, Ivan Kindekov, and Angel G. Galabov. Multiorgan Pathological Changes Caused by Experimental Influenza Virus Infection in Mice. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, October 2021. http://dx.doi.org/10.7546/crabs.2021.10.07.

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Perk, Simon, Egbert Mundt, Alexander Panshin, Irit Davidson, Irina Shkoda, Ameera AlTori, and Maricarmen Garcia. Characterization and Control Strategies of Low Pathogenic Avian Influenza Virus H9N2. United States Department of Agriculture, November 2012. http://dx.doi.org/10.32747/2012.7697117.bard.

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The avian influenza virus, subtype H9N2 subtype, defined as having a low pathogenicity, causes extensive economical losses in commercial flocks, probably due to management and synergism with other pathogens. AIV H9N2 was first identified in Israel in the year 2000, and since then it became endemic and widespread in Israel. Control by vaccination of commercial flocks with an inactivated vaccine has been introduced since 2007. In face of the continuous H9N2 outbreaks, and the application of the vaccination policy, we aimed in the present study to provide a method of differentiating naturally infected from vaccinated animals (DIVA). The aim of the assay would be detect only antibodies created by a de-novo infection, since the inactivated vaccine virus is not reproducing, and might provide a simple tool for mass detection of novel infections of commercial flocks. To fulfill the overall aim, the project was designed to include four operational objectives: 1. Evaluation of the genetic evolution of AIV in Israel; 2. Assessment of the diagnostic value of an NS1 ELISA; 3. NS1 ELISA as evaluation criteria for measuring the efficacy of vaccination against H9N2 AIV; 4. Development of an AIV H9 subtype specific ELISA systems. Major conclusion and implications drawn from the project were: 1. A continuous genetic change occurred in the collection of H9N2 isolates, and new introductions were identified. It was shown thatthe differences between the HA proteins of viruses used for vaccine productionand local fieldisolatesincreasedin parallelwith the durationand intensity ofvaccine use, therefore, developing a differential assay for the vaccine and the wild type viruses was the project main aim. 2. To assess the diagnostic value of an NS1 ELISA we first performed experimental infection trials using representative viruses of all introductions, and used the sera and recombinant NS1 antigens of the same viruses in homologous and heterologous NS1 ELISA combination. The NS1 ELISA was evidently reactive in all combinations, and did not discriminate significantly between different groups. 3. However, several major drawbacks of the NS1 ELISA were recognized: a) The evaluation of the vaccination effect in challenged birds, showed that the level of the NS1 antibodies dropped due to the vaccination-dependent virus level drop; b) the applicability of the NS1-ELISA was verified on sera of commercial flocks and found to be unusable due to physico-chemical composition of the sera and the recombinant antigen, c) commercial sera showed non-reactivity that might be caused by many factors, including vaccination, uncertainty regarding the infection time, and possibly low antigen avidity, d) NS1 elevated antibody levels for less than 2 months in SPF chicks. Due to the above mentioned reasons we do not recommend the application of the DIVA NS1 ELISA assay for monitoring and differentiation AIV H9N2 naturally-infected from vaccinated commercial birds.
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Chen, Qi, Ryan Vander Veen, Darin M. Madson, and D. L. Hank Harris. Immunization for Influenza A Virus by Intranasal Administration of Alphavirus Replicon Particles. Ames (Iowa): Iowa State University, January 2013. http://dx.doi.org/10.31274/ans_air-180814-29.

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Diaz, Leyla. Phase I Human Safety Studies of FGI-101-1A6 to Combat HINI Influenza Virus. Fort Belvoir, VA: Defense Technical Information Center, June 2013. http://dx.doi.org/10.21236/ada607997.

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Bosworth, Brad T., Matthew M. Erdman, Christa Irwin, Alan T. Loynachan, and D. L. Hank Harris. Evaluation of a Virus-like Replicon Particle Vaccine Expressing Proteins of Swine Influenza Virus in Pigs With and Without Maternally Derived Antibodies. Ames (Iowa): Iowa State University, January 2009. http://dx.doi.org/10.31274/ans_air-180814-644.

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Schat, Karel Antoni, Irit Davidson, and Dan Heller. Chicken infectious anemia virus: immunosuppression, transmission and impact on other diseases. United States Department of Agriculture, 2008. http://dx.doi.org/10.32747/2008.7695591.bard.

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1. Original Objectives. The original broad objectives of the grant were to determine A) the impact of CAV on the generation of cytotoxic T lymphocytes (CTL) to reticuloendotheliosis virus (REV) (CU), B). the interactions between chicken anemia virus (CAV) and Marek’s disease virus (MDV) with an emphasis on horizontal spread of CAV through feathers (KVI), and C) the impact of CAV infection on Salmonella typhimurium (STM) (HUJI). During the third year and the one year no cost extension the CU group included some work on the development of an antigen-antibody complex vaccine for CAV, which was partially funded by the US Poultry and Egg Association. 2. Background to the topic. CAV is a major pathogen causing clinical disease if maternal antibody-free chickens are infected vertically or horizontally between 1 and 14 days of age. Infection after 3 weeks of age when maternal antibodies are not longer present can cause severe subclinical immunosuppression affecting CTL and cytokine expression. The subclinical immunosuppression can aggravate many diseases including Marek’s disease (MD) and several bacterial infections. 3. Major conclusions and achievements. The overall project contributed in the following ways to the knowledge about CAV infection in poultry. As expected CAV infections occur frequently in Israel causing problems to the industry. To control subclinical infections vaccination may be needed and our work indicates that the development of an antigen-antibody complex vaccine is feasible. It was previously known that CAV can spread vertically and horizontally, but the exact routes of the latter had not been confirmed. Our results clearly show that CAV can be shed into the environment through feathers. A potential interaction between CAV and MD virus (MDV) in the feathers was noted which may interfere with MDV replication. It was also learned that inoculation of 7-day-old embryos causes growth retardation and lesions. The potential of CAV to cause immunosuppression was further examined using CTL responses to REV. CTL were obtained from chickens between 36 and 44 days of age with REV and CAV given at different time points. In contrast to our earlier studies, in these experiments we were unable to detect a direct impact of CAV on REV-specific CTL, perhaps because the CTL were obtained from older birds. Inoculation of CAV at one day of age decreased the IgG antibody responses to inactivated STM administered at 10 days of age. 4. Scientific and Agricultural Implications The impact of the research was especially important for the poultry industry in Israel. The producers have been educated on the importance of the disease through the many presentations. It is now well known to the stakeholders that CAV can aggravate other diseases, decrease productivity and profitability. As a consequence they monitor the antibody status of the breeders so that the maternal antibody status of the broilers is known. Also vaccination of breeder flock that remain antibody negative may become feasible further reducing the negative impact of CAV infection. Vaccination may become more important because improved biosecurity of the breeder flocks to prevent avian influenza and Salmonella may delay the onset of seroconversion for CAV by natural exposure resulting in CAV susceptible broilers lacking maternal antibodies. Scientifically, the research added important information on the horizontal spread of CAV through feathers, the interactions with Salmonella typhimurium and the demonstration that antigen-antibody complex vaccines may provide protective immunity.
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Elbers, Armin R. W., Evelien A. Germeraad, José L. Gonzales, Thomas J. Hagenaars, and Clazien J. de Vos. Omgevingstransmissie van aviaire influenza virus door de lucht via wilde watervogels naar commercieel gehouden pluimvee : met een focus op transmissie vanuit HPAIV-gecontamineerde uitwerpselen van wilde watervogels via de lucht of vanuit een aerosol geproduceerd door uitademen of proesten van HPAIV-besmette wilde watervogels. Lelystad: Wageningen Bioveterinary Research, 2021. http://dx.doi.org/10.18174/556247.

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Lees, Shelley, and Mark Marchant. Key Considerations: Cross-Border Dynamics Between Uganda and Tanzania in the Context of the Outbreak of Ebola, 2022. Institute of Development Studies, December 2022. http://dx.doi.org/10.19088/sshap.2022.046.

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This brief summarises key considerations concerning cross-border dynamics between Tanzania and Uganda in the context of the outbreak of Ebola (Sudan Virus Disease, SVD) in Uganda. It is part of a series focusing on at-risk border areas between Uganda and four high priority neighbouring countries: Rwanda; Tanzania; Kenya and South Sudan. The current outbreak is of the Sudan strain of Ebola (SVD). SVD is used in this paper to refer to the current outbreak in East Africa, whereas outbreaks of Zaire Ebolavirus disease or general references to Ebola are referred to as EVD. The current outbreak began in Mubende, Uganda, on 19 September 2022, approximately 240km from the Uganda-Tanzania border. It has since spread to nine Ugandan districts, including two in the Kampala metropolitan area. Kampala is a transport hub, with a population over 3.6 million. While the global risk from SVD remains low according to the World Health Organization, its presence in the Ugandan capital has significantly heightened the risk to regional neighbours. At the time of writing, there had been no cases of Ebola imported from Uganda into Tanzania. This brief provides details about cross-border relations, the political and economic dynamics likely to influence these, and specific areas and actors most at risk. It is based on a rapid review of existing published and grey literature, previous ethnographic research in Tanzania, and informal discussions with colleagues from the Tanzania’s Ministry of Health, Community Development, Gender, Elderly and Children (MoHCDGEC), Tanzania National Institute for Medical Research (NIMR), Uganda Red Cross Society, Tanzania Red Cross Society (TRCS), International Organization for Migration (IOM), IFRC, US CDC and CDC Tanzania. The brief was developed by Shelley Lees and Mark Marchant (London School of Hygiene & Tropical Medicine) with support from Olivia Tulloch (Anthrologica) and Hugh Lamarque (University of Edinburgh). Additional review and inputs were provided by The Tanzania Red Cross and UNICEF. The brief is the responsibility of the Social Science in Humanitarian Action Platform (SSHAP).
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Health hazard evaluation report: HETA-2009-0206-3117, evaluation of 2009 pandemic influenza A (H1N1) virus exposure among internal medicine housestaff and fellows, University of Utah School of Medicine, Salt Lake City, Utah. U.S. Department of Health and Human Services, Public Health Service, Centers for Disease Control and Prevention, National Institute for Occupational Safety and Health, October 2010. http://dx.doi.org/10.26616/nioshheta200902063117.

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