An ITAM in a Nonenveloped Virus Regulates Activation of NF-kappa B, Induction of Beta Interferon, and Viral Spread
JOURNAL OF VIROLOGY, 88(5), 2572–2583.
MeSH headings : Amino Acid Sequence; Animals; Cell Line; Enzyme Activation; Humans; Immunoreceptor Tyrosine-Based Activation Motif; Interferon-beta / metabolism; Intracellular Signaling Peptides and Proteins / metabolism; Mice; Molecular Sequence Data; Myocytes, Cardiac / metabolism; Myocytes, Cardiac / virology; NF-kappa B / metabolism; Phosphorylation; Protein Binding; Protein-Tyrosine Kinases / metabolism; Reoviridae / pathogenicity; Reoviridae / physiology; Sequence Alignment; Syk Kinase; Tyrosine / metabolism; Viral Proteins / chemistry; Viral Proteins / metabolism; Viral Tropism
TL;DR:
It is demonstrated for the first time that μ2 is phosphorylated, contains a functional ITAM, and activates NF-κB, and the results suggest that the cell type-specific effect of the μ2 ITAM on viral spread reflects the celltype-specific effects of NF-β and IFN-β.
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