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

PLoS Currents ◽  
2010 ◽  
Vol 2 ◽  
pp. RRN1162 ◽  
Author(s):  
Sebastian Maurer-Stroh ◽  
Raphael Tze Chuen Lee ◽  
Frank Eisenhaber ◽  
Lin Cui ◽  
Shiau Pheng Phuah ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
H1n1 Influenza ◽  
Common Mutation ◽  
2009 H1n1

scholarly journals Inactivated pandemic 2009 H1N1 influenza A virus human vaccines have different efficacy after homologous challenge in the ferret model

2020 ◽  
Vol 15 (1) ◽  
pp. 142-153
Author(s):  
Beatriz Vidaña ◽  
Sharon M. Brookes ◽  
Helen E. Everett ◽  
Fanny Garcon ◽  
Alejandro Nuñez ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
H1n1 Influenza ◽  
2009 H1n1 ◽  
Homologous Challenge

scholarly journals Tropism of Pandemic 2009 H1N1 Influenza a Virus

2012 ◽  
Vol 3 ◽  
Author(s):  
Ririn Ramadhany ◽  
Mayo Yasugi ◽  
Shota Nakamura ◽  
Tomo Daidoji ◽  
Yohei Watanabe ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
H1n1 Influenza ◽  
2009 H1n1

Different Efficacy of Inactivated Pandemic 2009 H1N1 Influenza A Virus Vaccines after Homologous Infection in Ferrets

2017 ◽  
Vol 156 (1) ◽  
pp. 82
Author(s):  
A. Vidaña ◽  
F. Garcon ◽  
A. Nuñez ◽  
D. Major ◽  
I.H. Brown ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
H1n1 Influenza ◽  
2009 H1n1

The Susceptibility of Isolates of Pandemic 2009 H1N1 Influenza A Virus to Russian Domestic Antivirals

2010 ◽  
Vol 86 (1) ◽  
pp. A37
Author(s):  
Irina Leneva ◽  
Alesya Romanovskaya ◽  
Elena Burtseva ◽  
Mike Eropkin ◽  
Alexander Shestopalov
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
H1n1 Influenza ◽  
2009 H1n1

Performance of five FDA-approved rapid antigen tests in the detection of 2009 H1N1 influenza A virus

2012 ◽  
Vol 84 (11) ◽  
pp. 1699-1702 ◽  
Author(s):  
Deena E. Sutter ◽  
Sue A. Worthy ◽  
Donna M. Hensley ◽  
Ashley M. Maranich ◽  
Donna M. Dolan ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
H1n1 Influenza ◽  
2009 H1n1 ◽  
Antigen Tests

scholarly journals Intermonomer Interactions in Hemagglutinin Subunits HA1 and HA2 Affecting Hemagglutinin Stability and Influenza Virus Infectivity

2015 ◽  
Vol 89 (20) ◽  
pp. 10602-10611 ◽  
Author(s):  
Wei Wang ◽  
Christopher J. DeFeo ◽  
Esmeralda Alvarado-Facundo ◽  
Russell Vassell ◽  
Carol D. Weiss
Keyword(s):  
Influenza Virus ◽  
Influenza A Virus ◽  
Influenza A ◽  
Seasonal Influenza ◽  
Virus Entry ◽  
H1n1 Influenza ◽  
Fusion Peptide ◽  
Virus Infectivity ◽  
Influenza Virus Hemagglutinin ◽  
2009 H1n1

ABSTRACTInfluenza virus hemagglutinin (HA) mediates virus entry by binding to cell surface receptors and fusing the viral and endosomal membranes following uptake by endocytosis. The acidic environment of endosomes triggers a large-scale conformational change in the transmembrane subunit of HA (HA2) involving a loop (B loop)-to-helix transition, which releases the fusion peptide at the HA2 N terminus from an interior pocket within the HA trimer. Subsequent insertion of the fusion peptide into the endosomal membrane initiates fusion. The acid stability of HA is influenced by residues in the fusion peptide, fusion peptide pocket, coiled-coil regions of HA2, and interactions between the surface (HA1) and HA2 subunits, but details are not fully understood and vary among strains. Current evidence suggests that the HA from the circulating pandemic 2009 H1N1 influenza A virus [A(H1N1)pdm09] is less stable than the HAs from other seasonal influenza virus strains. Here we show that residue 205 in HA1 and residue 399 in the B loop of HA2 (residue 72, HA2 numbering) in different monomers of the trimeric A(H1N1)pdm09 HA are involved in functionally important intermolecular interactions and that a conserved histidine in this pair helps regulate HA stability. An arginine-lysine pair at this location destabilizes HA at acidic pH and mediates fusion at a higher pH, while a glutamate-lysine pair enhances HA stability and requires a lower pH to induce fusion. Our findings identify key residues in HA1 and HA2 that interact to help regulate H1N1 HA stability and virus infectivity.IMPORTANCEInfluenza virus hemagglutinin (HA) is the principal antigen in inactivated influenza vaccines and the target of protective antibodies. However, the influenza A virus HA is highly variable, necessitating frequent vaccine changes to match circulating strains. Sequence changes in HA affect not only antigenicity but also HA stability, which has important implications for vaccine production, as well as viral adaptation to hosts. HA from the pandemic 2009 H1N1 influenza A virus is less stable than other recent seasonal influenza virus HAs, but the molecular interactions that contribute to HA stability are not fully understood. Here we identify molecular interactions between specific residues in the surface and transmembrane subunits of HA that help regulate the HA conformational changes needed for HA stability and virus entry. These findings contribute to our understanding of the molecular mechanisms controlling HA function and antigen stability.

scholarly journals Monoclonal Antibody Kit for Identification of the Novel 2009 H1N1 Influenza A Virus

2010 ◽  
Vol 48 (8) ◽  
pp. 2677-2682 ◽  
Author(s):  
A. D. Higgins ◽  
C. J. Shaw ◽  
J. G. Johnson ◽  
A. Navarro ◽  
N. A. Chapman ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Influenza A Virus ◽  
Influenza A ◽  
H1n1 Influenza ◽  
The Novel ◽  
2009 H1n1
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