AVM v1, released 02-OCT-22

A manually curated database of aerosol-transmitted virus mutations, human diseases, and drugs

Mutation detail:


Mutation site S407A
Virus Influenzavirus A H1N1
Mutation level Amino acid Level
Gene/protein/region type NP
Gene ID 23308125
Country -
Mutation type nonsynonymous mutation
Genotype/subtype/clade -
Sample cell line
Variants -
Viral reference sequence LC333186.1
Drug/antibody/vaccine -
Transmissibility -
Transmission mechanism -
Pathogenicity -
Pathogenicity mechanism -
Immune escape mutation -
Immune escape mechanism -
RT-PCR primers probes -

Protein detail:


Protein name Nucleocapsid Protein
Uniprot protein ID C3W621
Protein length 498 amino acids
Protein description NP encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.

Literature information:


Pubmed ID 28758638
Clinical information No
Disease -
Published year 2017
Journal elife
Title Influenza virus recruits host protein kinase C to control assembly and activity of its replication machinery
Author Arindam Mondal,Anthony R Dawson,Gregory K Potts,Elyse C Freiberger,Steven F Baker
Evidence Residual phosphorylation detected on the NP S165A/S407A mutant may reflect phosphorylation at one of the other previously identified phospho-sites (Hutchinson et al., 2012;Mondal et al., 2015), and our quantitative mass spectrometry suggest that some of these sites could also be targets of PKCs (see below).