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 IV mutation literature information.


  Influence of extracellular and cytoplasmic domains of M2 ion channel of influenza a virus on its activity.
 PMID: 17900218       2007       Acta virologica
Abstract: Mutational analysis of cytoplasmic domain of M2 protein showed that substitutions C50S, C50P, and H90S did not change the ion channel activity.


  Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
 PMID: 17917748       2007       Journal of molecular modeling
Abstract: It was found that the D92E mutation could result in weakened interactions of the carboxylate side chain with other phosphorylated residues, thereby activating phosphorylation of NS1.
Abstract: Virulent H5N1 strains of influenza virus often harbor a D92E point mutation in the nonstructural protein NS1.


  A single mutation in the PB1-F2 of H5N1 (HK/97) and 1918 influenza A viruses contributes to increased virulence.
 PMID: 17922571       2007       PLoS pathogens
Abstract: After comparing viruses from the Hong Kong 1997 H5N1 outbreak, one amino acid change (N66S) was found in the PB1-F2 sequence at position 66 that correlated with pathogenicity.
Abstract: In addition, both viruses with an S at position 66 (WH N66S and wt 1918) induced elevated levels of cytokines in the lungs of infected mice.
Abstract: In mice infected with WH N66S virus there was increased pathogenicity as measured by weight loss and decreased survival, and a 100-fold increase in virus replication when compared to mice infected with the WH virus.
Abstract: The 1918 pandemic strain A/Brevig Mission/18 was reconstructed with a pathogenicity-reducing mutation in PB1-F2 (S66N).


  Identification of a casein kinase II phosphorylation domain in NS1 protein of H5N1 influenza virus.
 PMID: 18188421       2007       Bioinformation
Abstract: This domain was formed due to the mutation at position 151 (T151I).
Result: Almost all the mutations in NS1 showed the change in secondary structure conformation of the mutated AA and those in contact with mutated AA, except for P223S mutation in A/chicken/Viet Nam/KG-076/2004 and L33I in A/chicken/Viet Nam/LD-080/2004, where only the conformation of residues in contact with these AAs was changed and not of that particular AA.
Result: Analysis of residue contacts in rna-binding domain structure (1NS1) at position 33 where the mutation I33L in A/chicken/Viet Nam/LD-080/2004 is observed, shows that the AAs VAL23, ALA30, PRO31, PHE32, ASP34, ARG35, LEU36 and ARG37 (Additional file RC at http://www.geocities.com/amubioinfo/InfluenzaAVirus.htm) are binding with LEU33 (Figure 1).
Result: In st


  Characterization of a mitochondrial-targeting signal in the PB2 protein of influenza viruses.
 PMID: 16242167       2006       Virology
Abstract: Recombinant influenza A/WSN/33 viruses expressing PB2 proteins with L7A and/or L10A mutations showed reduced viral titers, but unaffected levels of transcription, replication, and protein expression.
Abstract: The introduction of L7A and/or L10A mutations into recombinant viruses correlated with reduced mitochondrial membrane potential in infected cells, suggesting that mitochondrial localization of PB2 contributes to the preservation of mitochondrial function during influenza virus infection.


  Interaction between a 1998 human influenza virus N2 neuraminidase and monoclonal antibody Mem5.
 PMID: 16297424       2006       Virology
Abstract: The exceptions were E199A, E199Q, and K221R, in which binding was abrogated.
Abstract: We made mutations D147A, D147N, H150A, H197A, D198A, D198N, E199A, E199Q, K221R, A246K, D251N, and D251A.


  Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities.
 PMID: 16343533       2006       Journal of molecular biology
Abstract: Only one mutation of the NY variant (Asp190Glu) was sufficient to revert the HA receptor preference to that of classical avian strains.


  An avian influenza vaccine for humans targeting the polymerase B2 protein inside the capsid instead of hemagglutinin or neuramidase on the virus surface.
 PMID: 16403603       2006       Medical hypotheses
Abstract: Consequently, a publicly available database at the National Center for Biotechnology Information (NCBI) website, and the SYFPEITHI online computer algorithm, were used to generate a hypothesis about a peptide-based vaccine targeted at the E627K mutation in PB2 of the avian influenza virus.
Abstract: However, a recent study has revealed that the 1918 flu virus, like the H5N1 avian flu virus, has an E627K mutation in its polymerase B2 component, which is located inside the virus capsid.
Abstract: It seems reasonable to believe that the constancy, over more than 80 years, of the E627K mutation could be exploited to begin developing a vaccine now, rather than waiting for new mutations.


  Recovery of drug-resistant influenza virus from immunocompromised patients: a case series.
 PMID: 16479508       2006       The Journal of infectious diseases
Abstract: Virus variants recovered from 2 patients had mutations in the M2, NA (with a previously recognized Glu119Val NA substitution), and hemagglutinin genes.
Abstract: We describe a novel Asp198Asn NA mutation in an influenza B virus and its decreased susceptibility to both oseltamivir and zanamivir.


  Comparative activities of oseltamivir and A-322278 in immunocompetent and immunocompromised murine models of influenza virus infection.
 PMID: 16479509       2006       The Journal of infectious diseases
Abstract: A substitution in the neuraminidase (NA) active site (Arg292Lys) was detected in the cloned virus recovered from an oseltamivir-treated mouse.



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