General Information of the Molecule (ID: Mol02068)
Name
Fusion glycoprotein F0 (F) ,Respiratory syncytial virus
Synonyms
F
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Molecule Type
Protein
Gene Name
F
Sequence
MELLILKANAITTILTAVTFCFASGQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIE
LSNIKENKCNGTDAKVKLIKQELDKYKNAVTELQLLMQSTPPTNNRARRELPRFMNYTLN
NAKKTNVTLSKKRKRRFLGFLLGVGSAIASGVAVSKVLHLEGEVNKIKSALLSTNKAVVS
LSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVN
AGVTTPVSTYMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYV
VQLPLYGVIDTPCWKLHTSPLCTTNTKEGSNICLTRTDRGWYCDNAGSVSFFPQAETCKV
QSNRVFCDTMNSLTLPSEINLCNVDIFNPKYDCKIMTSKTDVSSSVITSLGAIVSCYGKT
KCTASNKNRGIIKTFSNGCDYVSNKGMDTVSVGNTLYYVNKQEGKSLYVKGEPIINFYDP
LVFPSDEFDASISQVNEKINQSLAFIRKSDELLHNVNAGKSTTNIMITTIIIVIIVILLS
LIAVGLLLYCKARSTPVTLSKDQLSGINNIAFSN
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Function
[Fusion glycoprotein F0]: Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins.
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Uniprot ID
FUS_HRSVA
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Kingdom: Orthornavirae
Phylum: Negarnaviricota
Class: Monjiviricetes
Order: Mononegavirales
Family: Pneumoviridae
Genus: .
Species: .
Type(s) of Resistant Mechanism of This Molecule
  ADTT: Aberration of the Drug's Therapeutic Target
Drug Resistance Data Categorized by Drug
Approved Drug(s)
1 drug(s) in total
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Palivizumab
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Drug Resistance Data Categorized by Their Corresponding Mechanisms
       Aberration of the Drug's Therapeutic Target (ADTT) Click to Show/Hide
Disease Class: Respiratory trac infection [1]
Resistant Disease Respiratory trac infection [ICD-11: CA45.0]
Resistant Drug Palivizumab
Molecule Alteration Missense mutation
p.N262D
Experimental Note Discovered Using In-vivo Testing Model
In Vitro Model Schistosoma haematobium strain 6185
Mechanism Description Clinical isolates N262D, K272E/M/Q, and S275F/L were reported as possessing mutations in the F protein region palivizumab-binding site (amino acids 258-275) and exhibiting resistance to palivizumab neutralization, while laboratory induced isolates N268I, and K272N/T/M/Q have also been reported.
Disease Class: Respiratory trac infection [1]
Resistant Disease Respiratory trac infection [ICD-11: CA45.0]
Resistant Drug Palivizumab
Molecule Alteration Missense mutation
p.N268I
Experimental Note Discovered Using In-vivo Testing Model
In Vitro Model Schistosoma haematobium strain 6185
Mechanism Description Clinical isolates N262D, K272E/M/Q, and S275F/L were reported as possessing mutations in the F protein region palivizumab-binding site (amino acids 258-275) and exhibiting resistance to palivizumab neutralization, while laboratory induced isolates N268I, and K272N/T/M/Q have also been reported.
Disease Class: Respiratory trac infection [1]
Resistant Disease Respiratory trac infection [ICD-11: CA45.0]
Resistant Drug Palivizumab
Molecule Alteration Missense mutation
p.K272E
Experimental Note Discovered Using In-vivo Testing Model
In Vitro Model Schistosoma haematobium strain 6185
Mechanism Description Clinical isolates N262D, K272E/M/Q, and S275F/L were reported as possessing mutations in the F protein region palivizumab-binding site (amino acids 258-275) and exhibiting resistance to palivizumab neutralization, while laboratory induced isolates N268I, and K272N/T/M/Q have also been reported.
Disease Class: Respiratory trac infection [1]
Resistant Disease Respiratory trac infection [ICD-11: CA45.0]
Resistant Drug Palivizumab
Molecule Alteration Missense mutation
p.K272M
Experimental Note Discovered Using In-vivo Testing Model
In Vitro Model Schistosoma haematobium strain 6185
Mechanism Description Clinical isolates N262D, K272E/M/Q, and S275F/L were reported as possessing mutations in the F protein region palivizumab-binding site (amino acids 258-275) and exhibiting resistance to palivizumab neutralization, while laboratory induced isolates N268I, and K272N/T/M/Q have also been reported.
Disease Class: Respiratory trac infection [1]
Resistant Disease Respiratory trac infection [ICD-11: CA45.0]
Resistant Drug Palivizumab
Molecule Alteration Missense mutation
p.K272Q
Experimental Note Discovered Using In-vivo Testing Model
In Vitro Model Schistosoma haematobium strain 6185
Mechanism Description Clinical isolates N262D, K272E/M/Q, and S275F/L were reported as possessing mutations in the F protein region palivizumab-binding site (amino acids 258-275) and exhibiting resistance to palivizumab neutralization, while laboratory induced isolates N268I, and K272N/T/M/Q have also been reported.
Disease Class: Respiratory trac infection [1]
Resistant Disease Respiratory trac infection [ICD-11: CA45.0]
Resistant Drug Palivizumab
Molecule Alteration Missense mutation
p.S275F
Experimental Note Discovered Using In-vivo Testing Model
In Vitro Model Schistosoma haematobium strain 6185
Mechanism Description Clinical isolates N262D, K272E/M/Q, and S275F/L were reported as possessing mutations in the F protein region palivizumab-binding site (amino acids 258-275) and exhibiting resistance to palivizumab neutralization, while laboratory induced isolates N268I, and K272N/T/M/Q have also been reported.
Disease Class: Respiratory trac infection [1]
Resistant Disease Respiratory trac infection [ICD-11: CA45.0]
Resistant Drug Palivizumab
Molecule Alteration Missense mutation
p.S275L
Experimental Note Discovered Using In-vivo Testing Model
In Vitro Model Schistosoma haematobium strain 6185
Mechanism Description Clinical isolates N262D, K272E/M/Q, and S275F/L were reported as possessing mutations in the F protein region palivizumab-binding site (amino acids 258-275) and exhibiting resistance to palivizumab neutralization, while laboratory induced isolates N268I, and K272N/T/M/Q have also been reported.
Disease Class: Respiratory trac infection [1]
Resistant Disease Respiratory trac infection [ICD-11: CA45.0]
Resistant Drug Palivizumab
Molecule Alteration Missense mutation
p.K272N
Experimental Note Discovered Using In-vivo Testing Model
In Vitro Model Schistosoma haematobium strain 6185
Mechanism Description Clinical isolates N262D, K272E/M/Q, and S275F/L were reported as possessing mutations in the F protein region palivizumab-binding site (amino acids 258-275) and exhibiting resistance to palivizumab neutralization, while laboratory induced isolates N268I, and K272N/T/M/Q have also been reported.
Disease Class: Respiratory trac infection [1]
Resistant Disease Respiratory trac infection [ICD-11: CA45.0]
Resistant Drug Palivizumab
Molecule Alteration Missense mutation
p.K272T
Experimental Note Discovered Using In-vivo Testing Model
In Vitro Model Schistosoma haematobium strain 6185
Mechanism Description Clinical isolates N262D, K272E/M/Q, and S275F/L were reported as possessing mutations in the F protein region palivizumab-binding site (amino acids 258-275) and exhibiting resistance to palivizumab neutralization, while laboratory induced isolates N268I, and K272N/T/M/Q have also been reported.
Disease Class: Respiratory trac infection [1]
Resistant Disease Respiratory trac infection [ICD-11: CA45.0]
Resistant Drug Palivizumab
Molecule Alteration Missense mutation
p.K272M
Experimental Note Discovered Using In-vivo Testing Model
In Vitro Model Schistosoma haematobium strain 6185
Mechanism Description Clinical isolates N262D, K272E/M/Q, and S275F/L were reported as possessing mutations in the F protein region palivizumab-binding site (amino acids 258-275) and exhibiting resistance to palivizumab neutralization, while laboratory induced isolates N268I, and K272N/T/M/Q have also been reported.
Disease Class: Respiratory trac infection [1]
Resistant Disease Respiratory trac infection [ICD-11: CA45.0]
Resistant Drug Palivizumab
Molecule Alteration Missense mutation
p.K272Q
Experimental Note Discovered Using In-vivo Testing Model
In Vitro Model Schistosoma haematobium strain 6185
Mechanism Description Clinical isolates N262D, K272E/M/Q, and S275F/L were reported as possessing mutations in the F protein region palivizumab-binding site (amino acids 258-275) and exhibiting resistance to palivizumab neutralization, while laboratory induced isolates N268I, and K272N/T/M/Q have also been reported.
References
Ref 1 Neutralizing epitopes of RSV and palivizumab resistance in Japan .Fukushima J Med Sci. 2017 Dec 19;63(3):127-134. doi: 10.5387/fms.2017-09. Epub 2017 Sep 1. 10.5387/fms.2017-09

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