Abstract: Genetic and functional analyses of Sib272 and Sib272PF revealed that amino acid substitutions, F3L of the HA2 subunit and T379K of the PB1, were responsible for plaque formation of Sib272PF by enhancing fusion and polymerase activities, respectively.
Interactions between histidine and tryptophan residues in the BM2 proton channel from influenza B virus.
Abstract: RESULTS: The emergence of NA oseltamivir-resistance mutation R292K was detected by 12 days of oseltamivir treatment with 44,286-fold increase in oseltamivir IC50.
Abstract: Sequential HA mutations R228S and A138S were identified and associated with a shift in the HA receptor binding pattern reflected by loss of the ability to agglutinate chicken erythrocytes.
Amino acid residues in the fusion peptide pocket regulate the pH of activation of the H5N1 influenza virus hemagglutinin protein.
Abstract: Four mutations to residues in the fusion peptide pocket, Y23H and H24Q in the HA1 subunit and E105K and N114K in the HA2 subunit, and a K58I mutation in the HA2 coiled-coil domain significantly altered the pH of activation of the H5 HA protein.
Abstract: Introduction of Y23H, H24Q, K58I, and N114K mutations into recombinant viruses resulted in virus-expressed HA proteins with similar shifts in the pH of fusion.
Kinetics of immune responses to influenza virus-like particles and dose-dependence of protection with a single vaccination.
Abstract: In this study, we have investigated the detailed kinetics of immune responses and protective efficacy after a single intranasal immunization with different doses of VLPs alone or in the presence of an Escherichia coli mutant heat-labile enterotoxin [mLT(R192G)] or cholera toxin subunit B as adjuvants.
Recognition of mannosylated ligands and influenza A virus by human surfactant protein D: contributions of an extended site and residue 343.
Abstract: A mutant with valine at 343 (R343V) showed enhanced binding to mannan relative to wild type and R343A.
Abstract: Although hNCRDs show negligible binding to influenza A virus (IAV), R343V showed markedly enhanced viral neutralizing activity.
Abstract: Both proteins showed efficient recognition of linear and branched subdomains of high-mannose glycans on carbohydrate microarrays, and R343V showed increased binding to a subset of the oligosaccharides.
Abstract: Crystallographic analysis of an R343V complex with 1,2-DM showed a novel mode of binding.
Introduction: Our experiments demonstrate greatly enhanced anti-viral activity of R343V associated with utilization of a modified carbohydrate binding site for alpha1-2 linked mannoses, which are commonly
Morbidity and mortality associated with nosocomial transmission of oseltamivir-resistant influenza A(H1N1) virus.
Abstract: CONCLUSION: Seasonal oseltamivir-resistant influenza A(H1N1) viruses with NA gene H274Y mutation are transmitted and retain significant pathogenicity and lethality in high-risk patients.
Abstract: CONTEXT: The sudden emergence and rapid spread of oseltamivir-resistant influenza A(H1N1) viruses with neuraminidase (NA) gene H274Y amino acid substitution is the hallmark of global seasonal influenza since January 2008.
Abstract: DESIGN, SETTING, AND PATIENTS: Descriptive outbreak investigation of 2 hematopoietic stem cell transplant recipients and an elderly patient who developed hospital-acquired influenza A virus infection following exposure to an index patient with community-acquired H274Y-mutated influenza A(H1N1) virus in
Computational studies of H5N1 influenza virus resistance to oseltamivir.
Abstract: Detailed analyses indicated that conformational change of E276 in the Pocket 1 region of NA is a key source of drug resistance in the H274Y mutant but not in the N294S mutant.
Abstract: We examined two resistant NA mutations, H274Y and N294S, and one non-drug-resistant mutation, E119G.
Oseltamivir-resistant influenza virus A (H1N1), Europe, 2007-08 season.
Abstract: Neuraminidase genes of ORVs possessing the H275Y substitution formed a homogeneous subgroup closely related to, but distinguishable from, those of oseltamivir-sensitive influenza viruses A (H1N1).
Abstract: Oseltamivir-resistant influenza viruses A (H1N1) (ORVs) with H275Y mutation in the neuraminidase emerged independently of drug use.
Result: A degree of heterogeneity was observed, especially among ORVs from the United Kingdom; however, the NA sequences in these smaller clusters, represented by, for example, A/Scotland/5/2008 (and A/Hawaii/21/2007) or A/England/654/2007, are not distinguished from those of OSVs by any common amino acid differences other than H275Y.
Result: Although the D344N substitution in PMID: 19342184
2009
Veterinary microbiology
Abstract: Functions affected include nuclear localization signals and sites of protein and RNA interaction, while others are known determinants of pathogenicity and host specificity such as the viral polymerase PB2 E627K substitution.
IV mutation literature information.
PMID: 
2009
Virus research
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