H5N1 Oseltamivir-resistance detection by real-time PCR using two high sensitivity labeled TaqMan probes.
PMID: 17055070
2007
Journal of virological methods
Abstract: A single amino acid substitution, from histidine to tyrosine at position 274 of the neuraminidase gene has converted Oseltamivir sensitive H5N1 influenza A virus into a resistant strain.
Abstract: Overall, the assay based on real-time PCR with two labeled TaqMan probes described here should be useful for detecting Oseltamivir-resistant H274Y H5N1 influenza A virus in many species and various sources of specimens with high sensitivity and specificity.
Introductio
Method: MGB TaqMan probes were chosen from the region covering the drug resistant area (H274Y) and designed to be specific for both wild type and mutant.
Method: Oligonucleotides designed for H274Y mutagenesis.
Method: The series of H274Y mutations were sequenced and used as controls.
Avian-virus-like receptor specificity of the hemagglutinin impedes influenza virus replication in cultures of human airway epithelium.
Abstract: R1 harbored the original HA of the pandemic human virus A/Hong Kong/1/68 (H3N2), whereas R2 was the L226Q/S228G HA mutant with avian-virus-like receptor specificity.
Adaptation of an H7N7 equine influenza A virus in mice.
PMID: 17251573
2007
The Journal of general virology
Abstract: It was found that the PB2-E627K substitution in this equine virus contributed to increased viral protein expression and virus replication in mouse cells and enhanced brain invasiveness in mice.
Abstract: Of these mutations, the Glu-to-Lys substitution at position 627 of PB2 (PB2-E627K) increased virulence appreciably.
Abstract: These results demonstrate that the importance of the PB2-E627K substitution for mouse adaptation, which was identified previously in human H5N1 isolates, extends to equine influenza A virus.
Effect of gene constellation and postreassortment amino acid change on the phenotypic features of H5 influenza virus reassortants.
Abstract: A variant of the 7:1 reassortant selected by serial passages in eggs had an amino acid substitution in the hemagglutinin (N244D, H3 numbering).
[Reassortment and gene interactions in the crossing of low-pathogenic avian influenza H5 virus with human influenza virus].
Abstract: The Mx protein, which confers resistance to orthomyxovirus, has been detected in several organisms, and one nonsynonymous substitution (S631N) of the chicken Mx protein has been shown to affect resistant activities to the avian influenza virus in vitro.
Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus.
Abstract: Second, we generated a mutant recombinant virus, rMG96A, which possesses an Ala-->Thr mutation at residue 24 of the M1 protein, a substitution demonstrated to be involved in the morphology (filamentous or spherical) of the influenza C VLPs.
Molecular changes in the polymerase genes (PA and PB1) associated with high pathogenicity of H5N1 influenza virus in mallard ducks.
Abstract: The HA gene mutations and the PB1 gene K207R mutation did not alter the HP phenotype of the large-plaque virus, whereas constructs with the PA (T515A) and PB1 (Y436H) gene mutations were nonpathogenic in orally inoculated ducks.
Abstract: The PB1 (Y436H) construct was not efficiently transmitted in ducks, whereas the PA (T515A) construct replicated as well as the wild-type virus did and was transmitted efficiently.
Abstract: There were two differences in the hemagglutinin (HA) gene (K52T
Neuraminidase inhibitor-resistant recombinant A/Vietnam/1203/04 (H5N1) influenza viruses retain their replication efficiency and pathogenicity in vitro and in vivo.
Abstract: Although the H274Y and N294S mutations did not compromise the replication efficiency of VN1203 or PR8 viruses in vitro, these mutations slightly reduced the lethality of PR8 virus in mice.
Abstract: Four NA mutations (E119G, H274Y, R292K, and N294S) that have been reported to confer resistance to NA inhibitors were each introduced into recombinant A/Vietnam/1203/04 (VN1203) H5N1 influenza virus.
Abstract: However, the VN1203 virus carrying either the H274Y or N294S mutation exhibited lethality similar to that of the wild-type VN1203 virus.
IV mutation literature information.
PMID: 
2007
Journal of virological methods
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