Abstract: An amino acid change at residue 122 from Trp to Arg and 179 from His to Arg resulted in the loss of hemadsorption activity of the HA protein.
Mutations in influenza A virus (H5N1) and possible limited spread, Turkey, 2006.
Abstract: Four novel amino acid changes (Q447L, N556K, and R46K in RNA polymerase and S133A in hemagglutinin) were detected in virus isolates from 2 siblings who died.
Method: All chicken and human isolates from the second epidemic had a unique mutation (I42T) in the M2 region.
Method: DQ323672) and contained a unique mutation (S133A) near receptor binding residue GVSSAC at positions 134 through 139.
Method: Enhanced pathogenic potential of all avian and human influenza virus isolates from the second outbreak was shown by mutation E627K in the PB2 region.
Method: In addition, unique amino acid changes found only in h
Infectivity studies of influenza virus hemagglutinin receptor binding site mutants in mice.
Abstract: Among the mutants examined was a virus containing a Y98F substitution at a conserved position in the receptor binding site that leads to a 20-fold reduction in binding.
Abstract: The capacity of the Y98F mutant to induce antibody responses and the structural locations of HA reversion mutations are examined.
Evaluation of a virus derived from MDCK cells infected persistently with influenza A virus as a potential live-attenuated vaccine candidate in the mouse model.
Abstract: Upon comparison with the parental influenza A E61-24-P15 strain used to establish persistent infection, amino acid exchanges were found in the M1 protein of IVpi-189 virus; arginine to glutamine at position 72 and threonine to alanine at position 139.
Synthesis of full length PB1-F2 influenza A virus proteins from 'Spanish flu' and 'bird flu'.
Abstract: As the native sequence of BF2 does not contain a cysteine residue two different mutants of BF2 (Y42C) and BF2 (S47C) with appropriate cysteine exchanges were produced.
Human-like receptor specificity does not affect the neuraminidase-inhibitor susceptibility of H5N1 influenza viruses.
Abstract: The triple N158S/Q226L/N248D HA mutation (which eliminates a glycosylation site at position 158) caused a switch from avian to human receptor specificity.
Abstract: To gain insight into how combinations of HA and NA mutations can affect the sensitivity of H5N1 virus to NA inhibitors, we also rescued viruses carrying the HA changes together with the H274Y NA substitution, which was reported to confer resistance to the NA inhibitor oseltamivir.
Result: A/Vietnam/1203/04 (H5N1) virus carrying the triple N158S/Q226L
Identification of the pore-lining residues of the BM2 ion channel protein of influenza B virus.
PMID: 18408016
2008
The Journal of biological chemistry
Abstract: It was found that mutation of transmembrane domain residues Ser(9), Ser(12), Phe(13), Ser(16), His(19), and Trp(23) to cysteine were most disruptive for ion channel function.
Single-amino-acid mutation in the HA alters the recognition of H9N2 influenza virus by a monoclonal antibody.
PMID: 18424263
2008
Biochemical and biophysical research communications
Abstract: Substitution of serine for asparagine at the same position (N145S) enables the CK/GX/10 to react with C/B3 in hemaglutinin inhibition, immunofluorescence and neutralization assays.
Abstract: We found that a single-amino-acid substitution of asparagine for serine at position 145 (S145N) in the HA protein prevents the reaction of CK/SD/6 virus with C/B3.
Application of bioinformatics-coupled experimental analysis reveals a new transport-competent nuclear localization signal in the nucleoprotein of influenza A virus strain.
Abstract: RESULTS: Comparison of the deduced aa sequence of NP of WS/33L strain with the published WS/33 NP sequences revealed that a single amino acid (aa) change (Met to Arg) at position 105 results in converting the flanking regions (between aa position 90-121, a 32-residue stretch) into two classical overlapping bipartite NLS (obpNLS).
Result: It is noteworthy that the obpNLS of NP-L is present in 9 other influenza virus strains (out of a total of 500 NP sequences screened) suggesting that the Met to Arg change (M105R) does occur naturally and that this single aa change results in the conversion of the region between aa 90 to 121 to a 32-residue obpNLS (Table 2).
Result: The analyses indicated that a single aa change (M105R) resulted i
In vitro evaluation of neuraminidase inhibitors using the neuraminidase-dependent release assay of hemagglutinin-pseudotyped viruses.
Abstract: The pseudotype virus release assay was used to determine the IC(50) values of Oseltamivir carboxylate, Zanamivir, and the novel phosphonate congeners of Oseltamivir against N1 group neuraminidases and their H274Y Oseltamivir carboxylate-resistant mutants.
IV mutation literature information.
PMID: 
2008
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