AVM v1, released 02-OCT-22

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

Mutation detail:


Mutation site I1381S
Virus Human respiratory syncytial virus
Mutation level Amino acid Level
Gene/protein/region type L
Gene ID 1494467
Country -
Mutation type nonsynonymous mutation
Genotype/subtype/clade A
Sample Human
Variants -
Viral reference sequence P28887.1
Drug/antibody/vaccine -
Transmissibility -
Transmission mechanism -
Pathogenicity -
Pathogenicity mechanism -
Immune escape mutation Yes
Immune escape mechanism -
RT-PCR primers probes -

Protein detail:


Protein name Polymerase
Uniprot protein ID P28887
Protein length 2165 amino acids
Protein description The core polymerase in RSV is composed of two proteins, a 250 kDa polymerase subunit (L), which contains the RNA-dependent RNA polymerase, the polyribonucleotidyl transferase (PRNTase, capping), and the methyltransferase enzymatic domains essential for viral transcription and replication, and the 27 kDa phosphoprotein (P) accessory protein. . The L protein caps mRNA by a unique RNA-GDP polyribonucleotidyl transferase activity mapped to conserved region V (CRV). Methylation of the cap at the guanine-N-7 and ribose-2-O positions is catalyzed by a unique dual specificity methyltransferase activity that has been functionally mapped to region VI of the L protein.

Literature information:


Pubmed ID 31495574
Clinical information No
Disease -
Published year 2019
Journal Cell
Title Structure of the Respiratory Syncytial Virus Polymerase Complex
Author Morgan S.A. Gilman,Cheng Liu,Amy Fung,Ishani Behera,Paul Jordan
Evidence Viruses that escape inhibition by BI-D harbor mutations encoding one of three substitutions in residues surrounding the PRNTase active site (I1381S, L1421F, or E1269D).