Mutation detail:
Mutation site | S498N |
Virus | Influenzavirus A H1N1 |
Mutation level ![]() |
Amino acid Level |
Gene/protein/region type | NP |
Gene ID | 23308125 |
Country | India |
Mutation type ![]() |
nonsynonymous mutation |
Genotype/subtype/clade | clade 6B |
Sample ![]() |
Human |
Variants | - |
Viral reference sequence | FJ966084.1 |
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 | 27997573 |
Clinical information | No |
Disease | - |
Published year | 2016 |
Journal | PLoS One |
Title | Genetic Characterization of Circulating 2015 A(H1N1)pdm44 Influenza Viruses from Eastern India |
Author | Anupam Mukherjee,Mukti Kant Nayak,Shanta Dutta,Samiran Panda,Biswa Ranjan Satpathi |
Evidence | a number of new mutations were observed in the NP (S498N), NS (NS1: K131E and N205S; NEP: N29S), PA (V100I, N321K, I330V and R362K), PB1 (G154D), and PB2 (R54K, M66I, D195N, R293K and V731I) sequences |