Mutation detail:
Mutation site | R38Q |
Virus | Influenzavirus A H1N1 |
Mutation level ![]() |
Amino acid Level |
Gene/protein/region type | NP |
Gene ID | 23308125 |
Country | Saudi Arabia |
Mutation type ![]() |
nonsynonymous mutation |
Genotype/subtype/clade | - |
Sample ![]() |
Human |
Variants | - |
Viral reference sequence | NC_026436.1 |
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 | 30799182 |
Clinical information | Yes |
Disease | - |
Published year | 2019 |
Journal | J Infect Public Health |
Title | Atypical influenza A(H1N1)pdm09 strains caused an influenza virus outbreak in Saudi Arabia during the 2009-2043 pandemic season |
Author | Anis Khan,Mohammed A AlBalwi,Ibraheem AlAbdulkareem,Abdulrahman AlMasoud,Abdulrahman AlAsiri |
Evidence | The internal proteins of Saudi A(H1N1)pdm09 isolates analyzed revealed substitutions P224S in PA, V100I, and L122Q in NP, I123V inNS1 andN31 inM2, which were commonto all Saudiisolates with available sequences in the specific regions. The other noteworthy substitutions included amino acid change in M2 protein E14G in 12/18 (66.6%) and an insertion of 8 amino acids in 15/18 (83.3%) cases between amino acid positions 151-152 in the NS1 protein (Table 4). Minor variations detected in internal genes included E188G (2/9; 22.2%), V400A (2/16; 12.5%), T588I (3/16; 18.7%) in PB2,V113A (2/16; 12.5%)in PB1, M579I(3/14; 21.4%), D478N (2/14; 14.3%), E610D (2/14; 14.3%) in PA, R38Q (2/5; 40%), V362A (2/17; 11.7%), and K400R (2/17; 11.7%) in NP (Table 14). |