Abstract: On the basis of the comparison among the antiviral activities associated with many Mx variations, a specific amino acid substitution at position 631 (Ser to Asn) was considered to determine the antivirally positive or negative Mx gene.
New insights into the spring-loaded conformational change of influenza virus hemagglutinin.
Abstract: We analyzed one double mutant, F63P/F70P, as an example.
Abstract: We observed that F63P/F70P undergoes key low-pH-induced conformational changes and binds tightly to target membranes.
Structural characterizations of fusion peptide analogs of influenza virus hemagglutinin. Implication of the necessity of a helix-hinge-helix motif in fusion activity.
PMID: 11937502
2002
The Journal of biological chemistry
Abstract: Also, the decrease in the C-terminal helix and the reduction of fusion activity in L17A demonstrates the importance of the C-terminal helix in fusion activity.
Abstract: E5 exhibits an activity similar to the native fusion peptide, whereas G13L and L17A, which are two point mutants of the E5 analog, possess much less fusion activity.
Abstract: Furthermore, the decrease of the hinge and the reduction of fusion activity in G13L reveal the importance of the hinge in fusion activity.
Abstract: To clarify how the fusion peptide exerts this specific function, we carried out biophysical studies of three fusion peptide analogs of influenza virus hemagglutinin HA2, namely E5, G13L, and L17A.
In vitro selection and characterization of influenza A (A/N9) virus variants resistant to a novel neuraminidase inhibitor, A-315675.
Abstract: By comparison, virus variants recovered from passaging against oseltamivir carboxylate (passage 14) harbored an E119V mutation and displayed a 6,000-fold-lower susceptibility to oseltamivir carboxylate and a 175-fold-lower susceptibility to zanamivir than did wild-type virus.
Abstract: However, by passage 10 (2.56 microM A-315675), two mutations (R233K, S339P) in the HA gene appeared in addition to the E119D mutation in the NA gene, resulting in a 310-fold-lower susceptibility to A-315675.
Abstract: Sequencing of the viral population identified an E119D mutation in the NA gene, but no mutations were observed in the hemagglutinin (
Structural studies of the resistance of influenza virus neuramindase to inhibitors.
PMID: 12014958
2002
Journal of medicinal chemistry
Abstract: Using influenza A/NWS/Tern/Australia/G70C/75 (H1N9), neuraminidase variants E119G and R292K have previously been selected by different inhibitors.
Influenza virus carrying neuraminidase with reduced sensitivity to oseltamivir carboxylate has altered properties in vitro and is compromised for infectivity and replicative ability in vivo.
Abstract: Pathogenicity of R292K influenza virus A/Sydney/5/97 was reduced in ferrets as measured by inflammatory and febrile responses at least in parallel to the decrease in replicative ability.
Abstract: The data indicate that the R292K NA mutation compromises viral fitness such that virus carrying this mutation is unlikely to be of significant clinical consequence in man.
Abstract: The infectivity and replicative abilities of R292K mutant virus were reduced by at least 2 logs in a mouse model of influenza infection and by 2 and 4 logs, respectively, in the ferret model.
Abstract: The predominant mutation seen is the substitution of arginine for lysine at position 292 of the viral NA.
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
Abstract: A substitution of the conserved histidine at position 274 for tyrosine in the NA active site has been selected via site directed mutagenesis, serial passage in culture under drug pressure in H1N1 and during the treatment of experimental H1N1 infection in man.
Abstract: Virus carrying H274Y NA enzyme selected in vivo has reduced sensitivity to oseltamivir carboxylate.
Abstract: Virus carrying a H274Y mutation is unlikely to be of clinical consequence in man.
A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs.
Abstract: A mutant with a histidine-to-alanine change at position 510 (H510A) in the PA protein of influenza A/WSN/33 virus showed a differential effect on transcription and replication.
Abstract: In vitro analyses of the H510A recombinant polymerase, by using transcription initiation, vRNA-binding, capped-RNA-binding, and endonuclease assays, suggest that the primary defect of this mutant polymerase is in its endonuclease activity.
Structure of antigenic sites on the haemagglutinin molecule of H5 avian influenza virus and phenotypic variation of escape mutants.
PMID: 12237433
2002
The Journal of general virology
Abstract: Mutants with the amino acid change K152N, as well as those with the change D126N, showed reduced lethality in mice.
Abstract: The substitution D126N, creating a new glycosylation site, was accompanied by an increase in the sensitivity of the mutants to normal mouse serum inhibitors.
Contacts between influenza virus N9 neuraminidase and monoclonal antibody NC10.
Abstract: Except for N200L and N329Q, the mutants were inhibited by NC10 to the same extent as wild-type NA although with less affinity.
Abstract: The K(d) for N329Q is sixfold higher than for wild-type NA in the inhibition test, but the same as wild-type in ELISA, indicating a change in disposition of the antibody but no loss of affinity.
Abstract: The enzyme activity (K(cat)) of N200L is 80% reduced, indicating a defect in folding or assembly; therefore, the loss in binding activity due to the missing sugar residue cannot be assessed.
Abstract: The mutations made were N200L (removing an N-linked oligosaccharide), N329Q, N345Q, S3
IV mutation literature information.
PMID: 
2002
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