AVM

Mutation site	K272M
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	cell line
Variants	-
Viral reference sequence	M74568.1
Drug/antibody/vaccine	-
Transmissibility	promote
Transmission mechanism	It is tempting to speculate that this may partially explain the observed increase in replicative fitness of the palivizumab escape mutant MP4 (change of K272 to M) as this mutation had increased fusion activity (2.3 fold relative to WT).
Pathogenicity	-
Pathogenicity mechanism	-
Immune escape mutation	-
Immune escape mechanism	-
RT-PCR primers probes	-

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.

Pubmed ID	17623075
Clinical information	No
Disease	-
Published year	2007
Journal	Virology Journal
Title	Relationship between the loss of neutralizing antibody binding and fusion activity of the F protein of human respiratory syncytial virus
Author	Changbao Liu, Nicole D Day, Patrick J Branigan, Lester L Gutshall, Robert T Sarisky
Evidence	Table 1