Respiratory syncytial virus F protein

{{Infobox nonhuman protein

| Name = Fusion glycoprotein F0

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| Organism = Human respiratory syncytial virus B (strain B1)

| TaxID = 79692

| Symbol = F

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| EntrezGene = 1489825

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| RefSeqmRNA = NC_001781.1

| RefSeqProtein = NP_056863.1

| UniProt = O36634

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| Chromosome = Genomic

| EntrezChromosome = NC_001781.1

| GenLoc_start = 5367

| GenLoc_end = 7836

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Fusion glycoprotein F0 of the human respiratory syncytial virus (RSV) is a critical fusion glycoprotein that facilitates entry of the virus into host cells by mediating the fusion of the viral and cellular membranes. This class I fusion protein is synthesized as an inactive precursor (F0), which undergoes cleavage to form two disulfide linked subunits, F1 and F2, that are essential for its fusion activity.{{cite book | vauthors = McDonald TP, Sugrue RJ | title = Glycovirology Protocols | chapter = The use of two-dimensional SDS-PAGE to analyze the glycan heterogeneity of the respiratory syncytial virus fusion protein | series = Methods in Molecular Biology | location = Clifton, N.J. | publisher = Humana Press | volume = 379 | pages = 97–108 | date = 2007 | pmid = 17502673 | doi = 10.1007/978-1-59745-393-6_7 | isbn = 978-1-58829-590-3 }} The RSV F protein exists in two conformations: a metastable prefusion form and a stable postfusion form, with the prefusion form being a major target for neutralizing antibodies due to its role in viral entry. The structural transitions of the F protein during the fusion process are crucial for its function, making it a significant focus in the development of vaccines and antiviral therapies against RSV infections.{{cite journal | vauthors = Li X, Yu X, Du Z, Zhang L, Wang Y, Wu Y, Lin Y, He Y | title = Prevention of respiratory syncytial virus from 1991 to 2024: a systematic review and bibliometrics analysis | journal = Translational Pediatrics | volume = 13 | issue = 10 | pages = 1858–1869 | date = October 2024 | pmid = 39524391 | pmc = 11543136 | doi = 10.21037/tp-24-271 | doi-access = free }}