AVM v1, released 02-OCT-22

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

Mutation detail:


Mutation site L138F
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 M74568.1
Drug/antibody/vaccine -
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 22184728
Clinical information No
Disease -
Published year 2012
Journal Journal Of Infectious Diseases
Title Natural polymorphisms and resistance-associated mutations in the fusion protein of respiratory syncytial virus (RSV): effects on RSV susceptibility to palivizumab
Author Qing Zhu, Nita K Patel, Josephine M McAuliffe, Wei Zhu, Leslie Wachter
Evidence Table 1