Abstract: Influenza A virus expressing C terminus-truncated NS1 with a T49A mutation dramatically increases IFN-beta mRNA in infected cells and causes slower replication than that of virus without the T-to-A mutation.
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
Abstract: A third attempted mutation (K391E) in PB1 was not always stable.
Abstract: In previous work, incorporation of two mutations (E580G, S660A) along with the addition of an HA epitope tag in the PB1 segment of B/Brisbane/60/2008 (B/Bris) resulted in an attenuated strain that was safe and effective as a live attenuated vaccine.
Abstract: Interestingly, viruses that maintained the K391E mutation were associated with the mutation E48K.
Abstract: These results confirm the compensatory effect of mutation E48K to stabilize the K391E mutation, resulting in a safer, yet still protective, IBV LAIV vaccine.
Abstract: To
A novel mechanism of enhanced transcription activity and fidelity for influenza A viral RNA-dependent RNA polymerase.
Abstract: In particular, we employed a single-turnover NTP incorporation assay for the first time on IAV RdRp to show that K235R mutant RdRp possessed a 1.9-fold increase in the transcription activity of the cognate NTP and a 4.6-fold increase in fidelity compared to wild-type.
Abstract: Our all-atom molecular dynamics simulations further elucidated that the higher activity is attributed to the shorter distance between K235R and the triphosphate moiety of NTP compared with wild-type.
Introduction: A recent study also reported an IAV RdRp with R229K point mutation in PB1, which exhibited elevated fidelity and resistance to favipiravir.
Introduction: For example, we previously discovered the high fidelity V43I mutation in PB1 subunits of IAV RdRp with a slower rate f
Cold and distant: structural features of the nucleoprotein complex of a cold-adapted influenza A virus strain.
PMID: 32490728
2021
Journal of biomolecular structure & dynamics
Abstract: In the filament interface peptide model, it was shown that the peptide corresponding in primary structure to the wild-type NP (SGYDFEREGYS) is prone to temperature-dependent self-association, unlike the peptide corresponding to E292G substitution (SGYDFGREGYS).
Abstract: Presence of the E292G substitution was shown by DSF to affect nucleoprotein complex melting temperature.
Abstract: The E292G mutation has been previously shown to pro
Abstract: The data suggest that the mechanism behind cold adaptation with E292G is associated with a weakening of the interaction between strands of the ribonucleoprotein complex and, as a result, the appearance of inter-chain interface flexibility necessary for complex function at low temperature.Communicated by Ramaswamy H.
Ancestral sequence reconstruction pinpoints adaptations that enable avian influenza virus transmission in pigs.
Result: Among 20 amino acids that differentiate the internal proteins of RG-EA2 and -EA3 viruses, PB1-Q621R and NP-R351K were detected at high frequencies (> 90%) among EA swine influenza viruses isolated from 1979 to 2018.
Result: Among the 12 amino acid differences found in the HA protein of RG-EA2 and EA3 viruses, HA1-N121T, HA1-Y138H, HA1-N207Y, HA1-K311Q, HA2-A65S, and HA2-D158N (H1 num
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.
Identification of Chebulinic Acid and Chebulagic Acid as Novel Influenza Viral Neuraminidase Inhibitors.
Abstract: Moreover, oseltamivir-resistance mutation NA/H274Y of NA is susceptible to CHLA or CHLI, suggesting a different mechanism of action for CHLA and CHLI.
Method: Oseltamivir-resistant influenza A/H1N1/pdm(09) virus containing NA/H274Y was provided by Beijing CDC, China, influenza A/Brisbane/10/2007(H3N2) was provided by Chinese Academy of Medical Sciences, and influenza B-Yamagata-like and B-Victoria-like strains were provided by Shandong CDC (Jinan, China).
Result: To compare the antiviral potency of CHLA and CHLI with the marketed NA inhibitor oseltamivir carboxylate, a yield reduction assay was performed with six influenza virus strains, including A/H1N1/PR8, A/H3N2/NY, A/H3N2/Brisbane, B-Yamagate, B-Victoria, and an oseltamivir-resistant A/H1N1pdm(09), which conta
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.
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.
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.
IV mutation literature information.
PMID: 
2021
Journal of virology
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