Abstract: The structure of the K627E mutated domain shows no structural differences but the charge reversal disrupts a striking basic patch on the domain surface.
Method: For the very high resolution native 627-domain and K627E structures individual atomic anisotropic B-factors were refined.
Method: The mutation K627E in the 538-693 protein was made by PCR
Result: The structure of the K627E mutant domain is essentially identical (RMSD of 0.34 A for all Calpha atoms of residues 539-675), with the Glu627 side-chain (not visible beyond Cgamma) again pointing into solvent.
Result: To assess the structural impact of the typically avian glutamate at this position, the K627E mutation was engineered into the 538-693 construct, the corresponding protein crystallized and its structure also determined.
Emergence of amantadine-resistant H3N2 avian influenza A virus in South Korea.
PMID: 18845822
2008
Journal of clinical microbiology
Abstract: We found a relatively high frequency of unique amantadine-resistant H3N2 and H9N2 avian influenza viruses (Val27Ile on M2 protein) isolated from live poultry markets in South Korea and confirmed that a Val27Ile single substitution in the M2 protein is enough to acquire the amantadine resistance phenotype by using reverse-genetically created human-avian reassortant viruses.
An in-depth analysis of the biological functional studies based on the NMR M2 channel structure of influenza A virus.
PMID: 18996090
2008
Biochemical and biophysical research communications
Abstract: To clarify this kind of confusion, an in-depth analysis was performed for these functional studies, particularly for the mutations D44N, D44A and N44D on position 44, and the mutations on positions 27-38.
Post-reassortment amino acid change in the hemagglutinin of a human-avian influenza H5N1 reassortant virus alters its antigenic specificity.
Abstract: In this report we demonstrated that the post-reassortment amino acid substitution N244D altered the antigenic specificity of HA as revealed by the loss of reactivity with an anti-H5 monoclonal antibody in hemagglutination-inhibition (HI) test.
Abstract: The variant reassortant had an amino acid substitution in the hemagglutinin N244D (H3 numbering).
The human H5N1 influenza A virus polymerase complex is active in vitro over a broad range of temperatures, in contrast to the WSN complex, and this property can be attributed to the PB2 subunit.
PMID: 19008377
2008
The Journal of general virology
Abstract: The E627K mutation in the avian PB2 was not required for this effect.
Method: The E627K mutation was introduced by site-directed mutagenesis (Quick-Change mutagenesis kit, Stratagene).
Result: 5b and d, respectively) and found, that an E627K mutation slightly shifted the temperature optimum from 37 C to 39 C.
Result: Interestingly, in both assays an E627K mutation in the avian PB2 resulted in a slight increase in activity.
Discussion: The E627K mutation in the avian PB2 led to only a slight increase in thermotolerance.
Analysis of a point mutation in H5N1 avian influenza virus hemagglutinin in relation to virus entry into live mammalian cells.
Abstract: Our results revealed that replacing aspartic acid at residue 94 with asparagine enhanced virus fusion activity and increased the binding of HA to sialic acid alpha2,6 galactose, while it decreased pseudotyped virus entry into cells expressing the avian type receptor, sialic acid alpha2,3 galactose.
[Role of amino acid residues at positions 322 and 329 of hemagglutinin in virulence of H5N1 avian influenza virus].
Abstract: All recombinant viruses carrying HA gene from Y with Q322L and/or K329-mutations and other seven genes from S were completely attenuated in terms of virulence to ducks whereas all recombinant viruses carrying HA gene from Y with same mutations and other seven genes from Y gained significant virulence.
Abstract: Recombinant viruses with S virus backbone were completely attenuated in terms of their virulence to ducks when position 322 (L322Q) and/or position 329 (-329K) of HA gene had been mutated.
Abstract: Recombinant viruses with Y virus backbone significantly increased their virulence to ducks when position 322 (Q322L) and/or position 329 (K329-) of HA gene had been mutated.
Abstract: The critical role that L322 and -3
[Site-directed modification of caspase cleavage site regions in avian influenza virus proteins].
Abstract: Mutation Gly16 --> Asp in avian virus NP made this protein (NPgd) sensitive to caspases, like human virus NP, and permitted its cleavage in infected cells.
Single mutation induced H3N2 hemagglutinin antibody neutralization: a free energy perturbation study.
PMID: 19367871
2008
The journal of physical chemistry. B
Abstract:
Abstract: A recent experiment shows that a single mutation in H3N2 HA, T131I, increases the antibody-antigen dissociation constant Kd by a factor of approximately 4000 (equivalent to a binding affinity decrease of approximately 5 kcal/mol), thus introducing an escape of the antibody (Ab) neutralization.
Abstract: As for further validation, we have also modeled another mutation, S157L, with experimental binding affinity available (Kd increasing approximately 500 times), and found a binding affinity decrease of 4.1 +/- 1.0 kcal/mol, which is again in excellent agreement with experiment.
Abstract: Detailed analysis reveals that this large binding affinity decrease in the T131I mutant is mainly due to the displacement of two bridge water molecules otherwise present in the wild-type HA/Ab interface.
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
PMID: 26621436
2008
Journal of chemical theory and computation
Abstract: Notably, in every case, the simulation results correctly predict that loss of binding occurs as a result of the R292K mutation.
Abstract: Per-residue binding footprints reveal that changes in DeltaDeltaEcoul for R292K-wildtype at position 292 parallel the change in experimental fold resistance energies (DeltaDeltaGR292K-WT) with S03 < S00 < S02 < S01.
Abstract: The goal is to elucidate which structural and energetic properties change as a result of a mutation at position R292K.
IV mutation literature information.
PMID: 
2008
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