Mutation detail:
Mutation site | E22A |
Virus | Human respiratory syncytial virus |
Mutation level ![]() |
Amino acid Level |
Gene/protein/region type | N |
Gene ID | 1494470 |
Country | - |
Mutation type ![]() |
nonsynonymous mutation |
Genotype/subtype/clade | A |
Sample ![]() |
Human |
Variants | - |
Viral reference sequence | AY911262.1 |
Drug/antibody/vaccine | - |
Transmissibility ![]() |
- |
Transmission mechanism | - |
Pathogenicity ![]() |
- |
Pathogenicity mechanism | - |
Immune escape mutation | - |
Immune escape mechanism | - |
RT-PCR primers probes | - |
Protein detail:
Protein name | Nucleoprotein |
Uniprot protein ID | P03418 |
Protein length | 391 amino acids |
Protein description | Nucleoprotein Encapsidates the viral RNA genome by forming a left-handed helical nucleocapsid that protects the RNA from nucleases. RNA replication depends on the availability of soluble nucleoprotein. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. Together with the phosphoprotein, sequesters host NF-kappa-B in inclusion bodies (IBs) thereby inhibiting this host defense pathway. May also act as a modulator of the innate immune response by sequestration of host IFIH1/MDA5 and MAVS into IBs. |
Literature information:
Pubmed ID | 25568210 |
Clinical information | No |
Disease | - |
Published year | 2015 |
Journal | Journal of virology |
Title | Identification and Characterization of the Binding Site of the Respiratory Syncytial Virus Phosphoprotein to RNA-Free Nucleoprotein |
Author | Marie Galloux,Gaelle Gabiane,Julien Sourimant,Charles-Adrien Richard,Patrick England |
Evidence | Mutations F4A, F8A, G10A, F20A, L21A, and I24A totally or nearly abrogated the interaction of GST-P[1-40] with Nmono(Fig. 5). The substitutions E7A and K25A attenuated partially the interaction compared to the wild-type P[1-40]. The other mutations and mo |