AVM

Mutation site	K394H
Virus	Human respiratory syncytial virus
Mutation level	Amino acid Level
Gene/protein/region type	F
Gene ID	1494475
Country	USA,China
Mutation type	nonsynonymous mutation
Genotype/subtype/clade	A
Sample	Human
Variants	-
Viral reference sequence	KT992094.1
Drug/antibody/vaccine	JNJ-53718678,BMS-433771,AK-0529,TMC-353121,GS-5806,LF-8,Ribavirin
Transmissibility	-
Transmission mechanism	-
Pathogenicity	-
Pathogenicity mechanism	-
Immune escape mutation	Yes
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	34379500
Clinical information	No
Disease	-
Published year	2021
Journal	Journal of virology
Title	Mechanism of Cross-Resistance to Fusion Inhibitors Conferred by the K394R Mutation in Respiratory Syncytial Virus Fusion Protein
Author	Wei Tang,Yueyue Li,Qiaoyun Song,Ziqin Wang,Manmei Li
Evidence	Both K394R and K394H mutations in F protein exhibited considerable resistance to JNJ-53718678, BMS-433771, AK-0529, TMC-353121, and LF-6, and show only slight resistance to GS-5806 (Fig. 6C to F).