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Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
The structure of the F protein shows that there are profound conformational differences between the pre- and postfusion states, involving transformations in secondary and tertiary structure, and the positions and structural transitions of key parts of the fusion machinery, including the hydrophobic fusion peptide and two helical heptad repeat regions, clarify the mechanism of membrane fusion mediated by the Fprotein.
Influenza Virus Assembly and Lipid Raft Microdomains: a Role for the Cytoplasmic Tails of the Spike Glycoproteins
Examination of purified virions indicated reduced amounts of DIG-associated lipids in the envelope of HAt− and NAt− viruses, indicating that deletion of both the HA and NA cytoplasmic tails results in reduced DIG association and changes in both virus polypeptide and lipid composition.
Influenza A virus M2 protein: monoclonal antibody restriction of virus growth and detection of M2 in virions
The monoclonal antibody, when included in a plaque assay overlay, considerably showed the growth of some influenza virus strains and is a specific effect for the M2 antibody as determined by an analysis of recombinants with defined genome composition and by the observation that competition by an N-terminal peptide prevents the antibody restriction of virus growth.
Influenza A virus NS1 protein binds p85β and activates phosphatidylinositol-3-kinase signaling
The report that NS1 binds directly to p85β, a regulatory subunit of phosphatidylinositol-3-kinase (PI3K), but not to the related p85α subunit suggests that activation of PI3K signaling in influenza A virus-infected cells is important for efficient virus replication.
A new influenza virus virulence determinant: The NS1 protein four C-terminal residues modulate pathogenicity
Viruses containing NS1 sequences from the 1918 H1N1 and H5N1 highly pathogenic avian influenza (HPAI) viruses demonstrated increased virulence in infected mice compared with wt A/WSN/33 virus, suggesting the NS1 protein C terminus may interact with PDZ-binding protein(s) and modulate pathogenicity through alternative mechanisms.