AVM v1, released 02-OCT-22

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

Mutation detail:


Mutation site K394R
Virus Human respiratory syncytial virus
Mutation level Amino acid Level
Gene/protein/region type F
Gene ID 1494475
Country -
Mutation type nonsynonymous mutation
Genotype/subtype/clade A
Sample Human
Variants -
Viral reference sequence KF713490.1
Drug/antibody/vaccine triazole-1
Transmissibility -
Transmission mechanism -
Pathogenicity -
Pathogenicity mechanism -
Immune escape mutation -
Immune escape mechanism -
RT-PCR primers probes -

Protein detail:


Protein name Fusion protein
Uniprot protein ID P03420
Protein length 574 amino acids
Protein description F protein is a class I fusion protein composed of 574 amino acids (AA). With a molecular weight of a 50 kDa C-terminal fragment F1 and a 20 kDa N-terminal fragment F2, the protein acquires a trimer of heterodimers. At AA positions 109 and 136, two furin cleavages take place. This feature releases a glycopeptide and thus reveals the hydrophobic site at F1 fragment. F1 and F2 are linked by a cysteine-rich region at two positions: between AA70 and AA212, and between AA37 and AA439. Other Frelated features involve N-glycosylation in F1 at AA position 500, and in F2 at AA positions 27 and 70. F protein is highly conserved, with only 25 AA differences between RSV subtypes A and B.

Literature information:


Pubmed ID 33782012
Clinical information No
Disease -
Published year 2021
Journal Antimicrobial Agents and Chemotherapy
Title Discovery of a Novel Respiratory Syncytial Virus Replication Inhibitor
Author Li Wang,Qihui Zhu,Kunlun Xiang,Yaling Zhang,Baocun Li
Evidence Because the K394R mutation in the fusion protein confers resistance to at least two fusion inhibitors with different structures, BMS-433771 and TMC353121, the CPE assay with this mutant virus (designated F_K394R) was used as a counterscreen assay to poten