IV mutation literature information.


  Effect of a single mutation in neuraminidase on the properties of Influenza B virus isolates.
 PMID: 14689282       2004       Archives of virology
Abstract: Both subclones had a common mutation in segment 6 leading to a change from Asp to Asn at position 457 in the NA.


  PB2 amino acid at position 627 affects replicative efficiency, but not cell tropism, of Hong Kong H5N1 influenza A viruses in mice.
 PMID: 15016548       2004       Virology
Abstract: A single amino acid substitution, from glutamic acid to lysine at position 627 of the PB2 protein, converts a nonlethal H5N1 influenza A virus isolated from a human to a lethal virus in mice.


  An amino-acid substitution in the influenza-B NB protein affects ion-channel gating.
 PMID: 15042345       2004       The Journal of membrane biology
Abstract: Serine residues at positions 20 and 28, threonine at position 24 and cysteine at position 26 were replaced by alanine.
Abstract: Proton permeability of NB channels, as detected by fluorescence quenching, was also altered by the mutation S20A: channels were no longer proton-permeable.
Abstract: The other mutations, S28A, T24A and C26A, did not have any detectable effect on the activity or proton permeability of channels formed by NB.
Abstract: We found that the mutation S20A gave channels that did not gate and that remained open most of the time.


  A mutation in the HLA-B*2705-restricted NP383-391 epitope affects the human influenza A virus-specific cytotoxic T-lymphocyte response in vitro.
 PMID: 15113903       2004       Journal of virology
Abstract: Recently, an amino acid substitution (R384G) in an HLA-B*2705-restricted CTL epitope in the influenza A virus nucleoprotein (nucleoprotein containing residues 383 to 391 [NP(383-391)]; SRYWAIRTR, where R is the residue that was mutated) was associated with escape from CTL-mediated immunity.


  Sequence variation in the influenza A virus nucleoprotein associated with escape from cytotoxic T lymphocytes.
 PMID: 15163496       2004       Virus research
Abstract: Furthermore, T cell recognition was completely abrogated by the R384G mutation.


  "A ""universal"" human influenza A vaccine."
 PMID: 15163506       2004       Virus research
Abstract: Several adjuvants were tested in conjunction with intraperitoneal vaccine administration, while the non-toxic enterotoxin mutant LT(R192G) was used for intranasal vaccination.


  Binding of influenza viruses to sialic acids: reassortant viruses with A/NWS/33 hemagglutinin bind to alpha2,8-linked sialic acid.
 PMID: 15246273       2004       Virology
Abstract: Fucosylation of the third sugar and changing the linkage between second and third sugars had little effect on binding by NWS-Tok, but marked effects on A/NWS/33(P227H)(HA)-tern/Australia/G70c/75(NA) (NWS-G70c, H1N9) and NWS-Mem/98.
Abstract: The P227H mutation in A/NWS/33(P227H)(HA)-A/Memphis/31/98(NA) (NWS-Mem/98, H1N2) results in sevenfold lower affinity for 3' sialyllactose, but binding to 6' sialyllactosamine is unchanged.


  Functional compensation of a detrimental amino acid substitution in a cytotoxic-T-lymphocyte epitope of influenza a viruses by comutations.
 PMID: 15280506       2004       Journal of virology
Abstract: Introduction of one of the comutations associated with R384G, E375G, partially restored viral fitness and nucleoprotein functionality.
Abstract: Introduction of the R384G substitution in the nucleoprotein gene segment of influenza virus A/Hong Kong/2/68 by site-directed mutagenesis was detrimental to viral fitness.
Abstract: The arginine-to-glycine substitution at position 384 of the viral nucleoprotein is associated with escape from CTLs.


  Introduction of a temperature-sensitive phenotype into influenza A/WSN/33 virus by altering the basic amino acid domain of influenza virus matrix protein.
 PMID: 15331690       2004       Journal of virology
Abstract: Of multiple mutants analyzed, a double mutant, R101S-R105S, of RKLKR resulted in a temperature-sensitive phenotype.
Abstract: The R101S-R105S double mutant had a greatly reduced ratio of M1 to NP in viral particles and a weaker binding of M1 to RNPs.


  Resistant influenza A viruses in children treated with oseltamivir: descriptive study.
 PMID: 15337401       2004       Lancet (London, England)
Abstract: FINDINGS: We found neuraminidase mutations in viruses from nine patients (18%), six of whom had mutations at position 292 (Arg292Lys) and two at position 119 (Glu119Val), which are known to confer resistance to neuraminidase inhibitors.
Abstract: Sensitivity testing to oseltamivir carboxylate revealed that the neuraminidases of viruses that have an Arg292Lys, Glu119Val, or Asn294Ser mutation were about 10(4)-10(5)-fold, 500-fold, or 300-fold more resistant than their pretreatment neuraminidases, respectively.
Abstract: We also identified another mutation (Asn294Ser) in one patient.



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