N-linked glycosylation at site 158 of the HA protein of H5N6 highly pathogenic avian influenza virus is important for viral biological properties and host immune responses.
Abstract: We have shown earlier that lack of glycosylation at position 158 of the hemagglutinin (HA) glycoprotein due to the T160A mutation is a key determinant of the dual receptor binding property of clade 2.3.4.4 H5NX subtypes.
Introduction: Compared to the surface Hemagglutinin (HA
Result: We conducted a PCR-based site-directed mutagenesis to generate several viruses with a single amino acid change at 160, including T160A in RHX (RHX-160A) and A160T in RY6 (RY6-160T).
Discussion: reported that addition of an N158D mutation to an HA protein containing N224K/Q226L increases virus stability.
Identification of Important N-Linked Glycosylation Sites in the Hemagglutinin Protein and Their Functional Impact on DC-SIGN Mediated Avian Influenza H5N1 Infection.
PMID: 33451024
2021
International journal of molecular sciences
Abstract: Furthermore, combined mutations (N27Q&N39Q) significantly waned the interaction on either H5N1-PVs or -RG infection in cis and in trans (p < 0.01).
Abstract: Human recombinant DC-SIGN (rDC-SIGN) coated ELISA showed that H5N1-PVs bound to DC-SIGN, however, mutation on the N27Q, N39Q, and Method: The pHW1203-HA with different N-linked glycosylation mutations including N26Q, N27Q, N39Q, N170Q, N181Q, N209Q, N302Q, N500Q, N599Q and other combination of mutations were generated.
Can molecular dynamics explain decreased pathogenicity in mutant camphecene-resistant influenza virus?
PMID: 33480324
2021
Journal of biomolecular structure & dynamics
Abstract: Specifically, camphecene causes a significant mutation in HA (V615L).
Mutations during the adaptation of H7N9 avian influenza virus to mice lungs enhance human-like sialic acid binding activity and virulence in mice.
Abstract: Sequence analysis showed that the two viruses differed by 27 amino acids distributed among six genes, containing changes in PB2 (E627K, D701N) and HA (Q226L) genes.
Characterization of the low-pathogenic H7N7 avian influenza virus in Shanghai, China.
Abstract: Mutations were found in HA (A135 T, T136S, and T160 A [H3 numbering]), M1 (N30D and T215 A), NS1 (P42S and D97 E), PB2 (R389 K), and PA (N383D) proteins; these mutations have been shown to be related to mammalian adaptation and changes in virulence of AIVs.
Discussion: In this study, no key amino acid mutations were found in PB2, especially the E627 K and D701 N mutations, which have b
Design, synthesis, and bioassay of 4-thiazolinone derivatives as influenza neuraminidase inhibitors.
PMID: 33540229
2021
European journal of medicinal chemistry
Abstract: In addition, D41 showed low toxicity and greater potency than reference compounds Oseltamivir and Amantadine against N1-H275Y variant in cellular assays.
Pathogenesis and genetic characteristics of a novel reassortant low pathogenic avian influenza A(H7N6) virus isolated in Cambodia in 2019.
PMID: 34347386
2021
Transboundary and emerging diseases
Abstract: Although avian-origin A(H7Nx) LPAIVs do not contain the critical mammalian-adaptive substitution (E627K) in PB2, the lethality and morbidity of the A(H7N6) virus in BALB/c mice were similar to those of A(H7N9) viruses, suggesting potential for interspecies transmission.
Structural and Thermodynamic Analysis of the Resistance Development to Pimodivir (VX-787), the Clinical Inhibitor of Cap Binding to PB2 Subunit of Influenza A Polymerase.
Result: A considerably less negative Eint of the pimodivir: PB2-F404Y complex can be indicative of the less negative enthalpic term measured by isothermal titration calorimetry (ITC).
Result: Additionally, the H357N and F404Y mutations considerably increased the binding affinity of the inhibitor.
Result: Compared to WT, the M431I mutant had minor difference in the thermodynamic parameters of pimodivir binding.
Result: For the F404Y single mutant, the enthalpy change for pimodivir binding was substantially affected and was 4.8 kcal.mol-1 less favorable than the WT value.
Result: For the H357N mutant, the enthalpic and entropic contributions were less favorable of 0.5 kcal.mol-1 and 2.5 kcal.mol-1, respectively.
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.
Investigation of genetic variation: Neuraminidase gene of influenza A virus H1N1/pdm09, Shiraz, Iran (2015-2016).
IV mutation literature information.
PMID: 
2021
Veterinary research
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