AVM v1, released 02-OCT-22

A manually curated database of aerosol-transmitted virus mutations, human diseases, and drugs

Mutation detail:


Mutation site L132A/L133A
Virus Human respiratory syncytial virus
Mutation level Amino acid Level
Gene/protein/region type NS1
Gene ID 1494468
Country -
Mutation type nonsynonymous mutation
Genotype/subtype/clade -
Sample cell line
Variants -
Viral reference sequence P04544.1
Drug/antibody/vaccine -
Transmissibility -
Transmission mechanism -
Pathogenicity -
Pathogenicity mechanism -
Immune escape mutation -
Immune escape mechanism -
RT-PCR primers probes -

Protein detail:


Protein name Non-structural Protein 1
Uniprot protein ID P0DOE9
Protein length 139 amino acids
Protein description Non-structural Protein 1 plays a major role in antagonizing the type I IFN-mediated antiviral response by degrading or inhibiting multiple cellular factors required for either IFN induction or response pathways. Acts cooperatively with NS2 to repress activation and nuclear translocation of host IFN-regulatory factor IRF3. Also disrupts the association of IRF3 with CREBBP.Non-structural Protein 1 interacts with host mitochondrial-associated membrane (MAM) MAVS and prevents the interaction with DDX58/RIG-I (Probable). Interacts with TRIM25 to suppress TRIM25-mediated DDX58 ubiquitination and thereby DDX58-MAVS interaction. Together with NS2, participates in the proteasomal degradation of host STAT2, IRF3, IRF7, TBK1 and DDX58/RIG-I through a NS-degradasome involving CUL2 and Elongin-C. The degradasome requires an intact mitochondrial MAVS. Decreases the levels of host TRAF3 and IKBKE/IKK-epsilon.As functions other than disruptions of the type I IFN-mediated antiviral signaling pathways, induces host SOCS1 and SOCS3 expression. Suppresses premature apoptosis by an NF-kappa-B-dependent, interferon-independent mechanism and thus facilitates virus growth. Additionally, NS1 may serve some inhibitory role in viral transcription and RNA replication. Suppresses proliferation and activation of host CD103+ CD8+ cytotoxic T-lymphocytes and Th17 helper T-lymphocytes

Literature information:


Pubmed ID 28665409
Clinical information No
Disease -
Published year 2017
Journal Nature MICROBIOLOGY
Title Structural basis for human respiratory syncytial virus NS1-mediated modulation of host responses
Author Srirupa Chatterjee,Priya Luthra,Ekaterina Esaulova,Eugene Agapov,Benjamin C. Yen
Evidence Using circular dichroism (CD), we confirmed that the mutations Y125A, L132A/L133A, and 1-118 did not compromise the overall stability of the proteins