Abstract: The results demonstrate that the amino acid change S145F (H3 numbering) in the hemagglutinin ensuring the resistance to a monoclonal antibody can be deleterious to virulence, and that the damaging effect on virulence may be compensated for by additional amino acid changes in position 186 in the hemagglutinin arising in the course of virus passaging in mice.
Novel pandemic influenza A(H1N1) viruses are potently inhibited by DAS181, a sialidase fusion protein.
Abstract: As inhibition was also observed with oseltamivir-resistant IFV (H274Y), DAS181 may be active against the antigenically novel pandemic influenza A(H1N1) virus should it acquire the H274Y mutation.
Abstract: Furthermore, DAS181 antiviral activity against pandemic influenza A(H1N1) strains was comparable to that observed against seasonal influenza virus including the H274Y oseltamivir-resistant influenza virus.
Method: The seasonal A/Hawaii/31/2007 (H1N1) and closely related A/Hawaii/21/2007 (H274Y) (H1N1) virus isolates, and the 2009 pandemic A(H1N1) virus isolates A/California/04/2009, A/Mexico/4604/2009, and A/Mexico/4108/2009 were obtained from Dr.
Discussion: Because the pandemic influenza A(H1N1) virus, or any other emerging strain of influenza, could potentially gain the oseltamivir-resistance mutation (
Inhibition of neuraminidase inhibitor-resistant influenza virus by DAS181, a novel sialidase fusion protein.
Discussion: An NA mutation (I222V) was observed in two of the zanamivir-resistant 2009 seasonal IFV strains, in addition to the well described H274Y mutation.
Discussion: Drug sensitivity analysis was not performed on these viral isolates, therefore the significance of the I222V mutation in patients is unclear.
Discussion: Examination of the HA sequence of pandemic 2009 IFV finds that nearly all isolates have a lysine (K) at amino acid 163, yet exhibit normal zanamivir sensitivity.
Discussion: Finally, an IFV A/Victoria/3/75 passaged with peramivir and found to be strongly pan-NAI resistant (oseltamivir, zanamivir, peramivir) in vitro , correlating with a single PMID: 19905033
2009
Biochemistry
Introduction: Although the S31N mutation was observed in more then 90% of influenza A cases in certain years, other amantadine insensitive phenotypes like L26F and V27A were isolated from influenza A patients with the emerging frequencies of 8-67%.
Introduction: Naturally occurring point mutations of the pore lining residues located outside of the H37xxxW41 motif, such as L26F, V27A, A30T, S31N and G34E result in the formation of amantadine-insensitive influenza A virus phenotypes.
Introduction: The current study shows that a novel compound, spiran amine 8, is a potent inhibitor of the L26F and V27A amantadine resistant mutants of the A/
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
Abstract: All 49 analyzed H1N1 virus isolates obtained during the 2008-2009 season, but none of the isolates obtained during the 2007-2008 season, contained the H274Y mutation.
Abstract: BACKGROUND: Influenza A virus subtype H1N1 with the H274Y mutation emerged and spread worldwide.
Abstract: The H274Y neuraminidase mutation status was determined by sequencing the neuraminidase segment.
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
Abstract: Genome annotations of this virus identified a stop mutation replacing serine at codon 12 (S12Stop) of the PB1-F2 protein, a virulence factor in influenza A viruses.
Introduction: The N66S mutation contributed to the high pathogenicity of the 1918 pandemic A/Brevig Mission/18 virus, and its replacement (S66N) attenuated this virus in mice.
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
Abstract: Fortunately, the current pandemic A(H1N1) 2009 virus, which is circulating globally, remains largely sensitive to both NAIs, although a small number of oseltamivir-resistant viruses have been isolated from patients to date, again with the H274Y mutation.
Abstract: Recently, however, significant levels of oseltamivir-resistant influenza A(H1) seasonal influenza viruses have also been encountered, which has been associated with a single amino acid change in the viral neuraminidase (H274Y).
Prediction of avian influenza A binding preference to human receptor using conformational analysis of receptor bound to hemagglutinin.
Abstract: RESULTS: Molecular dynamics simulation was employed to study the interactions between receptor models and hemagglutinin prote
Introduction: A Kan-1 derived strain with further HA mutations L129V and A134V is considered a quasi-species which exhibited higher selectivity toward human cell type receptor.
Introduction: A Sing-97 descendent that infected a human in 2004, A/Thailand/1(KAN-1)/2004 (abbreviated as Kan-1), has a single mutation in the HA binding pocket (S129L).
Introduction: The H5 HA X-ray structure from A/Duck/Singapore/3/97 (abbreviated as Sing-97) shows preferential binding to Siaalpha(2,3)Gal receptor, owing to Q222L and G224S mutations.
[An analysis on genetic characterization of HA1 gene of influenza virus subtype H3N2 circulated from 2001 to 2006 in Liaoning local area].
PMID: 20104769
2009
Zhonghua shi yan he lin chuang bing du xue za zhi
Abstract: Compared with WHO 2004-2006 H3N2 vaccine A/California/7/2004, 12 bases had changed, 4 positions had amino acid substitution in 62 * > E, 182 T > 1,224 S > A,225 C > Y.
The molecular epidemiology of influenza viruses: a lesson from a highly epidemic season.
IV mutation literature information.
PMID: 
2009
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