Virusliterature

IV mutation literature information.

Multiple Border-Zone Infarcts Triggered by Influenza A Virus Infection in a Patient With Cerebral Autosomal Dominant Arteriopathy Presenting With Subcortical Infarcts and Leukoencephalopathy.

PMID: 32102741 2020 Journal of stroke and cerebrovascular diseases

Abstract: Gene analysis identified a heterozygous mutation c.160C>T in exon 2 of the NOTCH3 gene (p.Arg54Cys).

Comparison of antigenic mutation during egg and cell passage cultivation of H3N2 influenza virus.

PMID: 32095441 2020 Clinical and experimental vaccine research

Result: In case of viruses passaged in eggs, hemagglutinin sequence of the 1st to 2nd passage viruses was the same as that of the parent virus, but there were three mutations identified from the 3rd to 8th passage viruses, A515G, G604A, and C942T, and from the 9th passaged virus, additional hemagglutinin sequence mutation with C704T were detected (Table 2).

Result: The analysis revealed that the G186S mutation is relatively inward of the hemagglutinin, while the H156R and S219F mutations are located near the surface of receptor binding site and may cause structural changes.

Discussion: According to the structural analysis of the

Acetylation at K108 of the NS1 protein is important for the replication and virulence of influenza virus.

PMID: 32093780 2020 Veterinary research

Abstract: In vitro and mouse studies showed that the deacetylation-mimic mutation K108R in the NS1 protein attenuated the replication and virulence of WSN-NS1-108R, while the constant acetylation-mimic mutant virus WSN-NS1-108Q showed similar replication and pathogenicity as the wild-type WSN virus (WSN-wt).

Abstract: To further explore the function of the K108 acetylation modification of the NS1 protein, a deacetylation-mimic mutation (K108R) and a constant acetylation-mimic mutation (K108Q) were introduced into the NS1 protein in the background of A/WSN/1933 H1N1 (WSN), resulting in two mutant viruses (WSN-NS1-108R and WSN-NS1-108Q).

Optimization of 4-Aminopiperidines as Inhibitors of Influenza A Viral Entry That Are Synergistic with Oseltamivir.

PMID: 32069052 2020 Journal of medicinal chemistry

Abstract: Compound 16 displayed a significant decrease of viral titer when evaluated in the infectious assays with influenza virus H1N1 (A/Puerto Rico/8/1934) or H5N1 (A/Vietnam/1203/2004) strains and the oseltamivir-resistant strain with the most common H274Y mutation.

Rapid detection of an I38T amino acid substitution in influenza polymerase acidic subunit associated with reduced susceptibility to baloxavir marboxil.

PMID: 32064779 2020 Influenza and other respiratory viruses

Abstract: In vitro studies have revealed that an I38T substitution in the polymerase acidic subunit (PA) is associated with reduced susceptibility of influenza viruses to baloxavir.

Abstract: METHODS: Three assays were developed based on RNase H2-dependent PCR (rhPCR) and named A/H1pdm PA_I38T rhPCR, A/H3 PA_I38T rhPCR, and B PA_I38T rhPCR.

Abstract: OBJECTIVES: Development of a rapid and simple method for monitoring influenza A(H1N1)pdm09, A(H3N2), and B viruses possessing the I38T substitution in PA.

Method: The resulting PCR product of A/H3 was cloned using a TOPO TA Cloning Kit for Sequenci

Antigenic variants of influenza B viruses isolated in Japan during the 2017-2018 and 2018-2019 influenza seasons.

PMID: 31955521 2020 Influenza and other respiratory viruses

Abstract: One B/Yamagata-lineage isolate carrying a G407S mutation in its NA showed a marked reduction in susceptibility to zanamivir, peramivir, and laninamivir.

Result: B/Colorado/06/2017 contains a two-amino-acid deletion at positions 162 and 163 in its HA.

Result: B/Victoria-lineage viruses with the three-amino-acid deletion fell into two distinct subgroups (Figure 1B): one subgroup shared an amino acid substitution at position K136E, and the other subgroup had two common amino acid substitutions at I180T and K209N.

Result: Sequence analysis revealed no mutations known to confer resistance to NA inhibitors in the influenza B isolates, except for one B/Yamagata-lineage isolate (B/Tokyo/UT

H7N9 Influenza Virus Containing a Polybasic HA Cleavage Site Requires Minimal Host Adaptation to Obtain a Highly Pathogenic Disease Phenotype in Mice.

PMID: 31948040 2020 Viruses

Abstract: In addition to the PBC site, we identified three other mutations that are important for host-adaptation and virulence in mice: HA (A452T), PA (D347G), and PB2 (M483K).

Method: Amino acid mutations in HA (A452T, H7 HA numbering with the signal peptide included), PA (D347G), and PB2 (M483K) were also inserted into each respective pPol vector by PCR using PrimeSTAR Max and in-fusion cloning.

Result: Although introduction of D347G (PA) or

PMID: 31951605 2020 PloS one

Discussion: Last, C19Y mutation in M2, with tyrosine in place of cysteine, could limit disulfide linkage to the neighbor cysteine 17 and prevent the formation of M2 dimerization.

Discussion: Second, E627K in PB2 of the human H7N4 virus may have been a determinant of host range.

Discussion: The K683T mutant conferred enhanced polymerase activity at low temperatures and promoted efficient replication in the upper respiratory tract.

Discussion: The new K683T mutation in PB2 may also be crucial for increased polymerase activity in mammalian cells.

Epidemic of influenza A(H1N1)pdm09 analyzed by full genome sequences and the first case of oseltamivir-resistant strain in Myanmar 2017.

PMID: 32130243 2020 PloS one

Abstract: One case with no prior history of oseltamivir treatment possessed H275Y mutated virus in neuraminidase (NA), which confers resistance to oseltamivir and peramivir with elevated IC50 values.

Abstract: Phylogenetic analysis of the hemagglutinin sequence showed that the Myanmar strains belonged to the genetic subclade 6B.1, possessing mutations of S162N and S164T at potential antigenic sites.

Method: This assay utilizes single nucleotide polymorphisms (SNP) for detecting oseltamivir-sensitive (H275) and oseltamivir-resistant (H275Y) viruses based on the reaction curves of FAM (H275) or ROX (H275Y).

Discussion: Another known important amino acid change, D

Global update on the susceptibilities of human influenza viruses to neuraminidase inhibitors and the cap-dependent endonuclease inhibitor baloxavir, 2017-2018.

PMID: 32004620 2020 Antiviral research

Abstract: PA gene sequence data, available from public databases (n = 13523), were screened for amino acid substitutions associated with reduced susceptibility to baloxavir (PA E23G/K/R, PA A36V, PA A37T, PA I38F/M/T/L, PA E119D, PA E199G): 11 (0.08%) viruses possessed such substitutions.

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