AVM

Protein name	Nuclear Export Protein
Uniprot protein ID	C3W610
Protein length	121 amino acids
Protein description	NEP can be divided into a protease-sensitive N-terminal domain (amino acids 1-53) and a protease-resistant C-terminal domain (amino acids 54-121), the crystal structure of which has been solved. NEP mediates the nuclear export of encapsidated genomic RNAs (ribonucleoproteins, RNPs). Acts as an adapter between viral RNPs complexes and the nuclear export machinery of the cell. Possesses no intrinsic RNA-binding activity, but includes a C-terminal M1-binding domain. This domain is believed to allow recognition of RNPs to which the M1 protein is bound. Because the M1 protein is not available in large quantities until the later stages of infection, such an indirect recognition mechanism probably ensures that genomic RNPs are not exported from the nucleus before sufficient quantities of viral mRNA and progeny genomic RNA have been synthesized. Furthermore, the RNPs enters the cytoplasm only when they have associated with the M1 protein that is necessary to guide them to the plasma membrane. May down-regulate viral RNA synthesis when overproduced.

Pubmed ID	27776172
Clinical information	Yes
Disease	-
Published year	2016
Journal	PLoS One
Title	Fatal Cases of Seasonal Influenza in Russia in 2015-2016
Author	T Ilyicheva,A Durymanov,I Susloparov,N Kolosova,N Goncharova
Evidence	all strains with a detected nucleotide sequence of NS gene we registered the following mutations: NS1-N205S and NS2(NEP)-T48A which increase virulence due to inhibition of IFN-dependent mechanism of the antiviral response in the infected cells (INF inhibition in culture).