LEI 10882 DE 2004 PDF
Departamento de Física, Universidade de Aveiro, Aveiro, Portugal, CICECO, Universidade de Aveiro, Publication Date (Web): September 4, .. The Journal of Physical Chemistry C (29), .. Lei Zhang, Linlin Fu, Xingxing Yang, Zuoling Fu, Xiangdong Qi, Zhijian Wu. Chem., , (26), pp – Qian Zhou, Kendall Fitzgerald, Paul D. Boyle and Wesley A. Henderson Shu Li, Zhen Cao, Yuxing Peng, Lei Liu, Yonglong Wang, Shu Wang, Ji-Qiang Wang, Tianying Yan, Xue-Ping Gao, De- Ying Song and Pan-Wen .. Journal of Fluorine Chemistry , Nature Communications volume 7, Article number: () | Download Citation . (d) Data sets cover a range of detector types, including Area Welberry, T. Diffuse X-Ray Scattering and Models of Disorder OUP Oxford () . . Chinese Academy of Sciences, Shanghai , China. Ming Lei.
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The yellow histogram bar in each plot designates data for dimer-disrupting mutant RA at the protein-protein interface formed at high protein concentrations and observed in the X-ray crystal structure. The high-throughput protein sample production platform of the Northeast Structural Genomics Consortium. Residues are colored as follows: Structural basis for suppression of a host antiviral response by influenza A virus.
Associated Data Supplementary Materials.
Group publications – Inorganic Chemistry and Catalysis
Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: Leu structures of NS1 effector domain mutants. Author manuscript; available in PMC Sep 6. The molecular orientations in panels abcand d-left are the same. We demonstrate that single-site alanine replacements of basic residues in this site lead to reduced RNA-binding activity, and that recombinant influenza B viruses expressing these mutant NS1B proteins are 100882 attenuated in replication.
Assays for the activation phosphorylation of IRF3 were carried out as described previously Kuo et al. The replication of these mutant viruses was assayed in human A cells using a multiplicity of infection of 0.
Quantifying covalent interactions with resonant inelastic soft X-ray scattering Kunnus K. FP values were reported in millipolarization units mP. Several constructs, differing by varying the length of the N-terminal segment of the CTD, were produced and assessed by small-scale expression and NMR studies.
Alternatively, this mutation may be affecting other functions of NS1B in influenza B virus-infected cells. Influenza A virus strains that circulate in lel differ in the ability of their NS1 proteins to block the activation of IRF3 and interferon-beta transcription. B96DOI: However, they also interact with some different host factors. Dimer interface of the effector domain of non-structural protein 1 from influenza A virus: Find articles by Robert M. SUMO ldi technology for enhanced protein production in prokaryotic and eukaryotic expression systems.
J Phys Chem B. See other articles in PMC that cite the published article. The NS1 protein of influenza A virus NS1A protein has been extensively studied and shown to have multiple functions that counter host antiviral responses and regulate other cellular and viral functions Krug and Garcia-Sastre, The host binding partners of the NS1B protein of influenza B viruses are less well studied.
To determine the function of the NS1B CTD RNA-binding activity, it will be necessary to next identify the RNA species that bind to this domain in infected cells, followed 1082 a determination of the mechanism s by which this RNA inhibits specific steps in virus replication.
The monomeric form of the NS1B CTD is sufficient to bind RNA Dimeric interactions observed in crystal structures may or may not occur in solution, particularly under dilute protein conditions.
Unexpected RNA-binding site in the NS1B Protein from Influenza B Virus not present in NS1A
Virus stocks were grown in day-old fertilized eggs. Table 1 Data collection and refinement statistics. Electronic and bite angle effects in catalytic C—O bond cleavage of a lignin model compound using ruthenium Xantphos complexes Shaw L. Influenza viruses cause a highly contagious respiratory disease in humans. Contribution of NS1 effector domain dimerization to influenza A virus replication and virulence.
Xiao for helpful discussions and comments on this manuscript.
Group publications 2017
Evaluating protein structures determined by structural genomics consortia. Such conserved basic surfaces are typical of nucleic acid binding sites, a prediction that we verify below. We showed that this is not the case. Disruption of this RNA binding surface in the NS1B CTD by single site mutations of key basic residues substantially attenuates the replication of influenza B viruses in human cells, demonstrating that that this RNA-binding activity is required for optimal influenza B virus replication.
Investigating the interstellar dust through the Fe K-edge Rogantini D. Fluorescence polarization was measured on a Tecan GENios-Pro plate reader with excitation at nm and emission at nm. Open in a separate window. To determine whether the homodimerization interface of the CTD plays any role 108882 viral replication, we generated a recombinant virus expressing a NS1B protein with the RA mutation that inhibits CTD dimerization. SAD phasing using iodide ions in a high-throughput structural genomics environment.
In addition, some residues shown in white in Figure 1b within the apparent binding site did not provide ,ei CSP data, or are prolines which lack 15 N- 1 H resonances.