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 IV mutation literature information.


  V292I mutation in PB2 polymerase induces increased effects of E627K on influenza H7N9 virus replication in cells.
 PMID: 33075446       2021       Virus research
Abstract: Here, we studied two new potential adaptive mutations, V292I and D740A, in the PB2 protein that were identified by a multi-factor regression model.
Abstract: The study shows that the prevalence of the PB2-V292I mutation is increased in H7N9 influenza viruses isolated from both humans and birds over the past 6 years.


  Comprehensive assessment of amino acid substitutions in the trimeric RNA polymerase complex of influenza A virus detected in clinical trials of baloxavir marboxil.
 PMID: 33099886       2021       Influenza and other respiratory viruses
Abstract: RESULTS: PA/I38N in A(H1N1)pdm09 and PA/I38R in A(H3N2) were newly identified as treatment-emergent substitutions in the CAPSTONE-2 study.
Abstract: The I38N substitution conferred reduced susceptibility by 24-fold, whereas replicative capacity of the I38N-substituted virus was impaired compared with the wild-type.
Abstract: The I38R-substituted virus was not viable in cell culture.
Method: In the CAPSTONE-2 study, next-generation sequencing (NGS) was also employed with the samples meeting the following criteria: (a) subjects shedding A(H3N2) viruses with PA/I38T substitution, (b) virology data (viral titer and RNA) are available at days 1, 2, 3 or 4, and


  Mechanism and Kinetics of Copper Complexes Binding to the Influenza A M2 S31N and S31N/G34E Channels.
 PMID: 33248127       2021       Biophysical journal
Abstract: Electrophysiology and DFT studies also show that the complexes block the G34E amantadine-resistant mutant despite some crowding in the binding site by the glutamates.
Abstract: In voltage-clamp oocyte studies using the ubiquitous amantadine-insensitive M2 S31N variant, the current block showed fast and slow phases, in contrast to the single phase found for amantadine block of wild-type M2.


  Discovery of highly potent and selective influenza virus neuraminidase inhibitors targeting 150-cavity.
 PMID: 33385836       2021       European journal of medicinal chemistry
Abstract: Among them, compound 5c bearing 4-(3-methoxybenzyloxy)benzyl group exhibited the most potent activity, which was lower or modestly improved activities than oseltamivir carboxylate (OSC) against N1 (H1N1), N1 (H5N1) and N1 (H5N1-H274Y).
Abstract: However, 5c displayed 4.85-fold more potent activity than OSC against H5N1-H274Y NA.
Abstract: Molecular docking studies provided insights into the high potency of 5c against N1 and N1-H274Y mutant NAs.


  A bivalent live attenuated influenza virus vaccine protects against H1N2 and H3N2 viral infection in swine.
 PMID: 33418392       2021       Veterinary microbiology
Abstract: The hemagglutinin (HA) cleavage site from both SD191-WT and SD69-WT were engineered from a trypsin-sensitive to an elastase-sensitive motif, to generate SD191-R342V and SD69-K345V, respectively.
Abstract: The elastase dependent SD191-R342V virus possesses a mutation from arginine to valine at amino acid (aa) 342 on HA, whereas the elastase dependent SD69-K345V virus possesses a mutation from lysine to valine at aa 345 on HA.


  Next-Generation Sequencing Analysis of the Within-Host Genetic Diversity of Influenza A(H1N1)pdm09 Viruses in the Upper and Lower Respiratory Tracts of Patients with Severe Influenza.
 PMID: 33408229       2021       mSphere
Abstract: However, the D222G/N substitution in hemagglutinin (HA) protein was the only amino acid substitution common to multiple patients.
Abstract: Therefore, it is important to investigate influenza A(H1N1)pdm09 virus populations using multiple paired samples from the upper and lower respiratory tract to avoid overlooking potentially important substitutions, especially in patients with severe disease.IMPORTANCE The D222G/N substitution in the hemagglutinin (HA) protein of influenza A(H1N1)pdm09 virus has been reported to be associated with disease severity and mortality in numerous previous studies.
Discussion: Conversely, previous studies have identified that the HA-D222G/N and othe


  Phosphorylation of Influenza A Virus NS1 at Serine 205 Mediates Its Viral Polymerase-Enhancing Function.
 PMID: 33408177       2021       Journal of virology
Abstract: CK2 inhibition significantly reduced the replication of WT viruses and decreased NS1-DDX21 interaction, as observed for NS1 S205G.
Abstract: However, PR8 NS1 S205N showed remarkably higher attenuation than PR8 NS1 S205G in a human cell line, highlighting a potential host-independent advantage of phosphorylatable S205, while an asparagine at this position led to a potential host-specific attenuation.
Abstract: Interestingly, PR8 NS1 S205G did not show polymerase activity-enhancing functions, in contrast to the WT, which can be attributed to diminished interaction with cellular restriction factor DDX21.
Abstract: To identify


  Ser-Leu substitution at P2 position of the hemagglutinin cleavage site attenuates replication and pathogenicity of Eurasian avian-like H1N2 swine influenza viruses.
 PMID: 33360319       2021       Veterinary microbiology
Abstract: In this study, we found a serine-leucine (Ser-Leu) substitution at the P2 position of the HA cleavage site (S328 L) in naturally occurring EA H1N2 virus.
Abstract: In vivo analyses revealed that, while all mice inoculated with r/DG2-S328 L or r/YJ28 viruses survived, the survival rates of r/DG2- and r/YJ28-L328S-inoculated animals were 20 % and 40 %, respectively.


  Multiple polymerase acidic (PA) I38X substitutions in influenza A(H1N1)pdm09 virus permit polymerase activity and cause reduced baloxavir inhibition.
 PMID: 33351916       2021       The Journal of antimicrobial chemotherapy
Abstract: PA I38T/M/F substitutions reduce its antiviral efficacy.
Abstract: METHODS: Influenza A(H1N1)pdm09 viral polymerase complexes containing all 19 I38X AA substitutions were reconstituted in HEK293T cells in a mini-replicon assay.


  Generation and properties of one strain of H3N2 influenza virus with enhanced replication.
 PMID: 33421685       2021       Veterinary microbiology
Abstract: For this viral strain all segments exhibit a homology close to 100 % with its parental strain A/Canine/Jiangsu/06/2010 (JS/10), except for two site mutations K156E and R201 K which occur in the receptor-binding sites of hemagglutinin (HA) and antigen binding sites of neuraminidase (NA), respectively.



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