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.
Detection of H3N8 influenza A virus with multiple mammalian-adaptive mutations in a rescued Grey seal (Halichoerus grypus) pup.
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.
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
Influenza vaccine effectiveness by A(H3N2) phylogenetic sub-cluster and prior vaccination history: 2016-17 and 2017-18 epidemics in Canada.
PMID: 32215564
2020
The Journal of infectious diseases
Abstract: Circulating 3C.2a viruses showed considerable diversity in the hemagglutinin glycoprotein and the egg-adapted vaccine strain also bore mutations, notably T160K loss-of-glycosylation.
N-benzyl 4,4-disubstituted piperidines as a potent class of influenza H1N1 virus inhibitors showing a novel mechanism of hemagglutinin fusion peptide interaction.
PMID: 32220685
2020
European journal of medicinal chemistry
Abstract: Furthermore, the HA1-S326V mutation resulting in resistance to 2 is close to the proposed new binding pocket.
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
Abstract: Amino acid substitutions I155T, K156Q, K156E+V138A, N186K led to a decrease in thermal stability, replication activity of the mutant viruses in chicken embryos, and virulence for mice, although these effects differed between the variants.
Abstract: The A138V and N186K mutations seem to be adaptive in mammalian viruses.
Abstract: The analysis of the frequency of these mutations in natural isolates of H5N1 influenza viruses indicated that the K156E/Q and N186K mutations have little chance to gain a foothold during evolution, in contrast to the I155T mutation, which is the most responsible for antigenic drift.
Substitutions in the PB2 methionine 283 residue affect H5 subtype avian influenza virus virulence.
PMID: 32351035
2020
Transboundary and emerging diseases
Abstract: The substitution PB2-M283I had an opposite phenotype.
Abstract: The substitution PB2-M283L displayed high virulence, resulting in a greater virus load in different tissues, more severe histopathological lesions and proinflammatory cytokines burst in mice.
Abstract: The substitution PB2-M283L enhanced the growth capacity and polymerase activity in human and mammalian cells in comparison to the rWT virus.
Laninamivir-Interferon Lambda 1 Combination Treatment Promotes Resistance by Influenza A Virus More Rapidly than Laninamivir Alone.
PMID: 32393488
2020
Antimicrobial agents and chemotherapy
Abstract: Moreover, the E119G NA mutation emerged together with concomitant hemagglutinin (HA) mutations (T197A and D222G), which were selected more rapidly by combination treatment with laninamivir plus IFN-lambda1 (passages 2 and 3, respectively) than by laninamivir alone (passage 10).
Abstract: Surprisingly, laninamivir used in combination with IFN-lambda1 promoted the emergence of the E119G NA mutation five passages earlier than laninamivir alone (passage 2 versus passage 7, respectively).
Experimental Infection Using Mouse-Adapted Influenza B Virus in a Mouse Model.
Abstract: A Victoria lineage (clade 1A) IBV was serially passaged 17 times in BALB/c mice, and adaptive amino acid substitutions were found in hemagglutinin (HA) (T214I) and neuraminidase (NA) (D432N).
Result: Additionally, nucleotide substitution in the HA segment (C641T) led to amino acid substitution in the HA protein (T214I).
Result: B/2017-MA) showed the presence of synonymous (not leading to amino acid substitution) nucleotide substitution in the PB1 segment:A2175G.
Result: In addition, analysis of these strains of HA
mRNA display with library of even-distribution reveals cellular interactors of influenza virus NS1.
Abstract: We also use md-LED to identify a mutant of NS1, D92Y, results in a loss of interaction with CPSF1.
Introduction: In addition, we explore the use of md-LED to examine the differential cellular binders of wild-type NS1 and a point mutant, D92Y, which had been previously shown to weaken NS1's known function in disrupting the interferon response.
Introduction: We find that the D92Y mutant failed to engage CPSF1, likely resulting in an increased host response.
Meth
Method: HA-tagged WT or D92Y mutant NS1 protein was expressed in 293T cells, lysed at 2 days post transfection and bound with anti-HA overnight at 4 C.
IV mutation literature information.
PMID: 
2020
Research in veterinary science
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