Abstract: Here, we identify Pasteurella multocida alpha2-3-sialyltransferase M144D mutant, Photobacterium damsela alpha2-6-sialyltransferase, and Helicobacter mustelae alpha1-2-fucosyltransferase, as efficient tools for live-cell glycan modification.
Introduction: Moreover, Pm2,3ST-M144D and Pd2,6ST are tolerant to large substituents introduced to the C-5 position of the cytidine-5'-monophosphate-N-acetylneuraminic acid (CMP-NeuAc) donor.
Introduction: We report that Pasteurella multocida alpha2-3-ST M144D mutant (Pm2,3ST-M144D), Photobacterium damsela alpha2-6-ST (Pd2,6ST), and H.
Method: CHO, CHO-Lec2, and CHO-Lec 8 cells were labeled by Pm2,3ST-M144D, Pd2,6ST, or Hp1,3FT with CMP-SiaNAz-biotin or GDP-FucAz-biotin for 30 mins at 37 C, washed twice with PBS, and lysed on ice in
Hydrogen-Deuterium Exchange Supports Independent Membrane-Interfacial Fusion Peptide and Transmembrane Domains in Subunit 2 of Influenza Virus Hemagglutinin Protein, a Structured and Aqueous-Protected Connection between the Fusion Peptide and Soluble Ectodomain, and the Importance of Membrane Apposition by the Trimer-of-Hairpins Structure.
Result: 8 (center) displays a structural model for I173E-HA2 that is supported by our HDX-MS data.
Result: 8 (right) displays a model for G1E-HA2 with a I173E-like SE structure with dissociated C-terminal strand bound to unfolded FP.
Result: 8 model supports that highly-impaired fusion for I173E is due to greater inter-membrane distance that results from a more flexible SE hairpin.
Result: Distinct G1E SE states similar to either WT or I173E structures are also evidenced by the bimodal behavior for 39-52, with one distribution of peaks in a m/z range similar to WT and the other in a m/z range similar to I173E.
Result: For tHDX = 120 min, there are approxi
Alternative interaction sites in the influenza A virus nucleoprotein mediate viral escape from the importin-alpha7 mediated nuclear import pathway.
Abstract: We show that three mutations in particular occur with high frequency in the viral nucleoprotein (NP) protein (G102R, M105K and D375N) in a specific structural area upon in vivo adaptation.
PB2 and hemagglutinin mutations confer a virulent phenotype on an H1N2 avian influenza virus in mice.
Abstract: By evaluating the virulence of mouse-adapted H1N2 variants at different generations, we found that the PB2-D701N and HA-G228S mutations both contribute to the virulence of this virus in mammals.
Abstract: Furthermore, we found that the PB2-D701N and HA-G228S mutations both enhance the ability of the virus to replicate in vivo and in vitro and that the PB2-D701N substitution results in an expansion of viral tissue tropism.
Abstract: These results suggest that the PB2-D701N mutation and the HA-
Pathogenicity of the H1N1 influenza virus enhanced by functional synergy between the NPV100I and NAD248N pair.
Abstract: To investigate the effect of these co-occurring substitution pairs, the V100I substitution in NP and the D248N substitution in NA were introduced into laboratory-adapted WSN IAVs.
Introduction: For example, the HA2 E47K substitution in Method: 293T cells were transfected with the pCAGGS WSN PB2, pCAGGS WSN PB1, pCAGGS WSN PA, pCAGGS WSN NP 0/14 (WT or V100I), pCAGGS and WSN NA (WT or D248N) expression vectors along with the pHH21 WSN NS-GFP reporter plasmid.
Preventing an Antigenically Disruptive Mutation in Egg-Based H3N2 Seasonal Influenza Vaccines by Mutational Incompatibility.
Result: A/Uruguay/716/2007 (NYMC X-175C) carried an egg-adaptive mutation, L194P, which has been extensively characterized, both structurally and antigenically, in our previous study using Bris07 HA.
Result: Among them, G186V and L194P, which are located on opposite sides of the 190-helix, had particularly high-occurrence frequencies (Figure 1A).
Result: An ELISA experiment was then performed to assess binding of these sera to Bris07 WT, G186V, and L194P recombinant HA proteins (Figures 6A and S4A).
Result: As expected, when the G186V mutant was passaged in eggs, the L194P mutation did not emerge.
Result: Besides IVR-165 H
Segment 2 from influenza A(H1N1) 2009 pandemic viruses confers temperature-sensitive haemagglutinin yield on candidate vaccine virus growth in eggs that can be epistatically complemented by PB2 701D.
PMID: 31169484
2019
The Journal of general virology
Abstract: Of these, PB2 N701D affected the temperature dependence of viral transcription and, furthermore, improved and drastically reduced the temperature sensitivity of the HA yield from the 5 : 3 CVV mimic.
Two mutations in viral protein enhance the adaptation of waterfowl-origin H3N2 virus in murine model.
Abstract: Furthermore, we found that PB2-D701N could enhance viral replication in vitro and in vivo and expanded viral tissue tropism.
Abstract: Our data suggest that PB2-D701N and M1-M192V are the virulence markers of H3N2 avian influenza virus, and these markers can be used in the trans-species transmission surveillance for the H3N2 avian influenza virus.
Abstract: We found that both PB2-D701N mutation and M1-M192V mutation were implicated in the viral pathogenic phenotypic variation of H3N2 avian influenza virus in mice.
The L46P mutant confers a novel allosteric mechanism of resistance toward the influenza A virus M2 S31N proton channel blockers.
Abstract: In this study, serial viral passages were applied to select resistance against a newly developed isoxazole-conjugated adamantane inhibitor that targets the AM2 S31N channel.
Abstract: Intriguingly, when the L46P mutant was introduced to AM2 WT, the channel remained sensitive toward amantadine inhibition.
Abstract: It was found that the L46P mutation caused a conformational change in the N terminus of transmembrane residues 22-31 that ultimately broadened the drug-binding site of AM2 S31N inhibitor 4, which spans residues 26-34, but not of AM2 WT inhibitor amantadine, which spans residues 31-34.
Abstract: Molecular dynamics simulations showed that L46P causes a dilation of drug-binding site between residues 22 and 31, which affects the binding of AM2 S31N channel
"Design, synthesis and biological evaluation of ""Multi-Site""-binding influenza virus neuraminidase inhibitors."
PMID: 31176096
2019
European journal of medicinal chemistry
Abstract: Among the synthesized compounds, compound 15e, the most potent N1-selective inhibitor targeting 150-cavity, showed 1.5 and 1.8 times greater activity than oseltamivir carboxylate (OSC) against N1 (H5N1) and N1 (H5N1-H274Y).
Abstract: Molecular docking studies provided insights into the high potency of 15e against N1 and N1-H274Y mutant NA.
IV mutation literature information.
PMID: 
2019
Nature communications
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