Abstract: After five sequential passages in MDCK cells, the M2 protein of viruses cultivated with amantadine alone mutated at positions V27A and S31N/I.
Molecular changes associated with adaptation of human influenza A virus in embryonated chicken eggs.
Abstract: Changing 2 NA residues (E119Q, Q136K) did not improve growth, and adaptation did not result in the HA changes H183L, D188Y, and V226A found by others.
Abstract: During adaptation, 6 amino acid substitutions occurred: 4 in HA (G186V, S219F, V226I, V309I) and 2 in NA (E119Q, Q136K).
Abstract: Two HA substitutions (G186V, V226I) were sufficient
The primary function of RNA binding by the influenza A virus NS1 protein in infected cells: Inhibiting the 2'-5' oligo (A) synthetase/RNase L pathway.
Abstract: Pretreatment of A549 cells with IFN-beta for 6 h did not inhibit replication of WT Udorn virus, whereas replication of R38A mutant virus was inhibited 1,000-fold.
Abstract: This R38A mutant virus is highly attenuated, and the mutant NS1A protein, like the WT protein, is localized in the nucleus.
Abstract: Using the R38A mutant virus, we establish that dsRNA binding by the NS1A protein does not inhibit production of IFN-beta mRNA.
Neuraminidase inhibitor-resistant and -sensitive influenza B viruses isolated from an untreated human patient.
PMID: 16641465
2006
Antimicrobial agents and chemotherapy
Abstract: Here, we describe the analysis of a mixed viral population that contained a novel D197E amino acid substitution that was responsible for this reduction.
Amantadine resistance among porcine H1N1, H1N2, and H3N2 influenza A viruses isolated in Germany between 1981 and 2001.
Abstract: S31N and/or L27A are well-known amino acid substitutions in M2 that confer amantadine resistance.
Abstract: Additionally, L27A was detected in two H1N1 strains.
Abstract: All resistant strains contained the AA substitutions G16E, S31N, and R77Q in the membrane protein 2 (M2).
[Antigenic and genetic study of influenza virus (H1N1) circulated in China in 2004-2005].
PMID: 16816857
2006
Zhonghua shi yan he lin chuang bing du xue za zhi
Abstract: The HA1 sequence data showed that the H1N1 virus had the following amino acid mutations such as 54 K > R, 90 T > K, 101 Y > H, 149 R > K, 169 V > A, 190 D > N, 212 R > K, 219 K > R, 245 W > R, 246 Y > F, 258 T > N, 318 V > A and the 54 and 190 amino acids located in antigenic group of HA1.
Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding.
Abstract: K102A, on the other hand, resulted in a significant decrease in both cap binding and viral RNA promoter-binding activity and consequently inhibited both transcription and replication.
Abstract: Both the D108A and K134A mutations completely inhibited endonuclease activity in vitro, explaining their selective defect in transcription.
Abstract: Mutation K102A caused a general decrease both in transcription and replication in vivo, whereas mutations D108A and K134A selectively inhibited transcription.
Abstract: Three further PA mutations, K102A, D108A, and K134A, were investigated in detail.
Mutations conferring zanamivir resistance in human influenza virus N2 neuraminidases compromise virus fitness and are not stably maintained in vitro.
PMID: 16891631
2006
The Journal of antimicrobial chemotherapy
Abstract: E119V viruses were stable and grew to similar titres as wild-type virus, consistent with their isolation from oseltamivir-treated patients.
Abstract: Mutations conferring oseltamivir resistance in N1 (H274Y) and B (R152K) NAs also conferred resistance in recombinant G70C N9 NA expressed in insect cells.
Abstract: RESULTS: H3N2 viruses generated by reverse genetics with H274Y, R292K E119V and E119D mutations were rescued.
Abstract: The G70C N9 NA may a
In silico analysis of genes nucleoprotein, neuraminidase and hemagglutinin: a comparative study on different strains of influenza A (Bird flu) virus sub-type H5N1.
Abstract: A mutant influenza virus (A/Udorn/72) expressing NS1 with the Y89F amino acid substitution exhibited a small-plaque phenotype, and grew more slowly in tissue culture than WT virus.
IV mutation literature information.
PMID: 
2006
Antiviral research
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