Recombinant Influenza A virus Nucleoprotein (NP)

1. Taking these observations together, TRIM41 is a constitutively expressed intrinsic influenza A virus restriction factor that targets viral NP for ubiquitination and protein degradation. PMID: 29899090
2. Structure of importin-alpha bound to a non-classical nuclear localization signal of the influenza A virus nucleoprotein has been reported. PMID: 26456934
3. Immunoprecipitation studies revealed influenza A virus NS1 and NP as direct interaction partners of DDX3. PMID: 26792746
4. Residue 88 of NP interacts with polymerase PB2 and contributes to influenza A virus replication. PMID: 25043584
5. HMGB1 protein binds to influenza virus nucleoprotein and promotes viral replication. PMID: 22696656
6. These results indicate that the PB2, PA, NP, and M segments play a more important role than the remaining four viral RNAs during the genome-packaging process. PMID: 22532680
7. Data suggest that the flexibility of loops 1 and 2 is required for RNA sampling and binding which likely involve conformational change(s) of the nucleoprotein. PMID: 22272272
8. These findings demonstrate that replication of the virus genome is followed by its encapsidation by NP in collaboration with its chaperone UAP56. PMID: 21507964
9. Because the authors showed that NP lacking RNA-binding activity binds directly to the viral polymerase, it is likely that a direct interaction between NP and the viral polymerase results in a modification of the polymerase in favor of unprimed initiation. PMID: 18945782
10. The authors identified a late-acting defect in NP that, separate from its function in RNA synthesis, indicates a role for the polypeptide in virion assembly, most likely involving M1 as a partner. PMID: 18987140
11. respective conserved amino acids in NP may thus be critical for the assembly and/or incorporation of sets of eight viral-RNA segments PMID: 19225007

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KEGG: vg:956531