Mutation detail:
Mutation site | V313Y |
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 ![]() |
Human |
Variants | - |
Viral reference sequence | GQ166232.1 |
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 | 21340741 |
Clinical information | No |
Disease | - |
Published year | 2011 |
Journal | Archives of Virology |
Title | Atypical characteristics of nucleoprotein of pandemic influenza virus H1N1 and their roles in reassortment restriction |
Author | Asawin Wanitchang, Prasatha Patarasirin, Juggragarn Jengarn Anan Jongkaewwattana |
Evidence | Notably, both the Y313V mutation of NPPR8 and the V313Y mutation of NPS-OIV resulted in a decrease in activity of the PR8 polymerase complex. These results clearly indicate that the presence of V313 in NPS-OIV did not occur by chance but in order to enhance the compatibility between NP and the polymerase complex of S-OIV. |