literature

IV mutation literature information.

Nuclear Magnetic Resonance and Molecular Dynamics Simulation of the Interaction between Recognition Protein H7 of the Novel Influenza Virus H7N9 and Glycan Cell Surface Receptors.

PMID: 27933797 2016 Biochemistry

3Introduction: As an example, the H1N1 virus responsible for the 1918 ""Spanish flu"" pandemic (SC18, ""South Carolina 1918"") propagated as efficiently between ferrets by aerosol as it did between humans, but a single mutation (D225G) and a double mutation (D225G/D190E) of amino acids in the H1 receptor binding site (RBS) yielded two artificial viruses, NY18 and AV18, respectively, the former being transmitted inefficiently and the latter unable to do so, while its lethality and replicati

Introduction: At the molecular level, the H1 (SC18) specificity switch was explained by observing that the D225G mutation on H1 removed crucial hydrogen bonds between the RBS and the LSTc nonreducing end, while the additional mutation (D190E) further reduced the extent of contact between its reducing end and the surface of helix 190.

A PB1 T296R substitution enhance polymerase activity and confer a virulent phenotype to a 2009 pandemic H1N1 influenza virus in mice.

PMID: 26453960 2015 Virology

Abstract: Analysis of the variants genomes revealed 6 amino acid changes in the PB1 (T296R), PA (I94V), HA (H3 numbering; N159D, D225G, and R226Q), and NP (D375N).

Molecular Characterisation of the Haemagglutinin Glycan-Binding Specificity of Egg-Adapted Vaccine Strains of the Pandemic 2009 H1N1 Swine Influenza A Virus.

PMID: 26056814 2015 Molecules (Basel, Switzerland)

Result: LSTc (alpha2,6) binding, however, is rescued in the D225G/Q226R double mutant HA model, where we notice positive residue scoring at those positions.

Result: Similar to our findings, this group also noted the receptor affinities of the D225G mutant HA were higher than that of the wild type A/California/04/09 HA.

Result: The glycan binding specificity of the virus particles and purified recombinant A/California/07/09 HAs harboring the RBS mutations D225G, Q226R, D225G/Result: The preference for the lower respiratory tract may also account for the lower frequency at which the D225G variant is transmitted.

Molecular basis of the receptor binding specificity switch of the hemagglutinins from both the 1918 and 2009 pandemic influenza A viruses by a D225G substitution.

PMID: 23514882 2013 Journal of virology

Abstract: A single D225G mutation in both H1s switches receptor binding specificity from alpha2,6 linkage binding to dual receptor binding.

Abstract: Here, we show via H1-ligand complex structures that the D225G substitution results in a loss of a salt bridge between amino acids D225 and K222, enabling the key residue Q226 to interact with the avian receptor, thereby obtaining dual receptor binding.

Virulence and transmissibility of H1N2 influenza virus in ferrets imply the continuing threat of triple-reassortant swine viruses.

PMID: 23019374 2012 Proc Natl Acad Sci U S A

Abstract: Although molecular analysis did not reveal known virulence markers, the Sw/1204 virus acquired mutations in hemagglutinin (HA) (Asp-225-Gly) and neuraminidase (NA) (Ser-315-Asn) proteins during the single ferret passage.

Treatment of oseltamivir-resistant influenza A (H1N1) virus infections in mice with antiviral agents.

PMID: 22809862 2012 Antiviral research

Discussion: One of the HA mutations, D225G, was associated with increased virulence in mice.

Both influenza hemagglutinin and polymerase acidic genes are important for delayed pandemic 2009 H1N1 virus clearance in the ferret model.

PMID: 22809692 2012 Virology

Result: HA K119N, G155E, S183P, R221K, D222G, and D225G lead to increased virulence in mice.

Isolation and phylogenetic analysis of pandemic H1N1/09 influenza virus from swine in Jiangsu province of China.

PMID: 21723574 2012 Research in veterinary science

Abstract: In addition, some of these viruses had D225G (3/8) mutations in the receptor binding sites of the hemagglutinin (HA) protein, indicating enhancement of their binding affinity to the sialic alpha2, 3Gal receptor.

In silico characterization of the functional and structural modules of the hemagglutinin protein from the swine-origin influenza virus A (H1N1)-2009.

PMID: 20602265 2010 Science China. Life sciences

Abstract: The D225G/E mutation in HA, which is found in some isolates, may confer dual binding specificity to the 2,3- and 2,6-receptor based on previously reported work.

A new common mutation in the hemagglutinin of the 2009 (H1N1) influenza A virus.

PMID: 20535229 2010 PLoS currents

Introduction: For the severe cases, no additional known mutation, such as HA-D239G (D222G or D225G in alternative numberings ), was found that could directly explain severity.

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