IV mutation literature information.


  In silico analysis and molecular characterization of Influenza A (H1N1) pdm09 virus circulating and causing major outbreaks in central India, 2009-2019.
 PMID: 33604005       2020       Iranian journal of microbiology
Result: Analysis of amino acid sequence alignment revealed changes at two positions (T151A, D239G) at RBS of HA between genogroup 2 and 3, three positions (A151T, S200P, S202T) between genogroup 3 and 4, two positions (N114D, E279G) between 4 and 6A, four positions (N101S, Q180K, G279E, E300K) between 6A and 6B, three positions (S101N, K180Q, I251V) between 6B and 6C genogroup, four positions (G101S, T214A


  Detection of H3N8 influenza A virus with multiple mammalian-adaptive mutations in a rescued Grey seal (Halichoerus grypus) pup.
 PMID: 32211197       2020       Virus evolution
Abstract: From examining the protein alignments, we found several residue changes in the seal virus that did not occur in the bird viruses, including D701N in the PB2 segment, a rare mutation, and a hallmark of mammalian adaptation of bird viruses.
Result: Changes at positions 226 and 228 in HA (reference H3 numbering) which can change receptor-binding preferences between avian and mammalian hosts, were not found in either of the H3N8 seal viruses, but the H10 equivalent of H3-Q226L was identified in viruses from the 2014-15 H10N7 outbreak in European seals.
Result: Many of these changes occur in the polymerase complex genes:
Result: and S678N found in the seal PB1 gene has been associated with increased polymerase activity and virulence in mice.


  Amino acid substitutions involved in the adaptation of a novel H7N7 avian influenza virus in mice.
 PMID: 32200160       2020       Research in veterinary science
Abstract: Genomic analysis of the mouse-adapted virus revealed amino acid changes in the PB2 (E525G, M645I, and D701N), NP (I475V), HA(D103N), and NA(K142E) proteins.


  Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
 PMID: 32161172       2020       Journal of virology
Abstract: PA-X R195K was present in all human H7N9 and H1N1/2009 viruses and predominated in human H5N6 viruses.
Abstract: Reverse genetics analyses of PA-X substitutions conserved in human influenza viruses indicated that R195K, K206R, and P210L substitutions conferred significantly increased replication and pathogenicity on H9N2 virus in mice and ferrets.


  Antigenic drift of hemagglutinin and neuraminidase in seasonal H1N1 influenza viruses from Saudi Arabia in 2014 to 2015.
 PMID: 32159230       2020       Journal of medical virology
Abstract: Amino acid changes at key antigenic sites, such as position S101N, S179N (antigenic site-Sa), I233T (antigenic site-Sb) in the head domain might have resulted in antigenic drift and emergence of variant viruses.
Abstract: For NA protein, 36% isolates showed the presence of amino acid changes such as V13I (n = 29), I314M (n = 29) and 12% had I34V (n = 10).
Abstract: However, H257Y mutation responsible for resistance to neuraminidase inhibitors was missing.
Introduction: Furthermore, a high number of the strains possessed the amino acid changes D97N (aspartic acid to asparagine), S185T


  Antigenic changes among the predominantly circulating C/Sao Paulo lineage strains of influenza C virus in Yamagata, Japan, between 2015 and 2018.
 PMID: 32135195       2020       Infection, genetics and evolution
Abstract: Aichi99 sublineage strains exhibiting decreased reactivity with the monoclonal antibody YA3 became predominant after 2016, and these strains possessed the K190N mutation.
Abstract: The Aichi99 sublineage strains possessing the K190N mutation were detected after 2012 in Europe, Australia, the USA, and Asia as well as Japan.
Abstract: These observations suggest that antigenic variants with K190N mutations have circulated extensively around the world and caused outbreaks in Japan between 2016 and 2018.


  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


  Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
 PMID: 31894969       2020       Biochemistry
1Abstract: Compared to the M2 ""wild type"" (WT) with valine at position 27, we observe that the channel pore is wider at its N-terminus as a result of the V27A mutation and that this removes V27 side chain hydrophobic interactions that are important for binding of amantad
Abstract: A 300 ns molecular dynamics simulation of the M2(22-46) V27A-spiro-adamantyl amine complex predicts with accuracy the position of the ligands and waters inside the pore in the X-ray crystal structure of the M2(22-46) V27A complex.
Abstract: Additionally, in the structure of the M2(21-61) V27A construct, the C-terminus of the channel is tightly packed relative to that of the M2(22-46) construct.


  Sporadic occurrence of H9N2 avian influenza infections in human in Anhui province, eastern China: A notable problem.
 PMID: 31863839       2020       Microbial pathogenesis
Abstract: None of the human-isolated H9N2 AIVs had the I368V mutation in PB1 protein, but all the poultry-isolated H9N2 viruses in 2017 carried this mutation.


  Neuraminidase from Influenza A and B Viruses is Susceptible to the Compound 4-(4-Phenyl-1H-1,2,3-Triazol-1-yl)-2,2,6,6-Tetramethylpiperidine-1- Oxyl.
 PMID: 31880262       2020       Current topics in medicinal chemistry
Abstract: When we passaged the influenza A virus in the presence of Tritempo, a mutant virus with the G248P change in the NA was detected.



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