Mutation detail:
Mutation site | W104G |
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 | GQ117080.1 |
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 | 21094080 |
Clinical information | No |
Disease | - |
Published year | 2011 |
Journal | J Clin Virol |
Title | Investigation of causes of oseltamivir chemoprophylaxis failures during influenza A (H1N1-2018) outbreaks |
Author | Vernon J Lee,Jonathan Yap,Sebastian Maurer-Stroh,Raphael T C Lee,Frank Eisenhaber |
Evidence | From the whole genome sequencing, several mutations at the HA (T220S, E275V, T333A, D240G);PB2 (K660R, L607V, V292I);NS1 (F103S), and NP (W104G) gene segments were detected, but none of them were likely to result in anti-viral resistance. |