F0 is cleaved, releasing F1, F2, F(110-136)

Stable Identifier
R-HSA-9829200
Type
Reaction [transition]
Species
Homo sapiens
Related Species
Human respiratory syncytial virus A
Compartment
trans-Golgi network membrane
ReviewStatus
5/5
Locations in the PathwayBrowser
Expand all
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
F0 is cleaved, releasing F1, F2, F(110-136)
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
Human respiratory syncytial virus (hRSV) A fusion protein precursor F0 is cleaved shortly before or during transit to the host cell plasma membrane, resulting in three fragments: the F subunits, F1 and F2, and the p27 peptide. At both cleavage sites, motifs typically recognized by furin-like proteases are found. The actual responsible protease is unknown. Cleavage into F1 and F2 is necessary to form the F1-F2 subunit of the F trimer, which catalyzes both virion-cell and cell-cell membrane fusion (Elango et al, 1985; Collins & Mottet, 1991; Gonzalez-Reyes et al, 2001).
Literature References
PubMed ID Title Journal Year
2987829 Respiratory syncytial virus fusion glycoprotein: nucleotide sequence of mRNA, identification of cleavage activation site and amino acid sequence of N-terminus of F1 subunit

Coligan, JE, Elango, N, Venkatesan, S, Norrby, E, Satake, M, Camargo, E

Nucleic Acids Res 1985
11493675 Cleavage of the human respiratory syncytial virus fusion protein at two distinct sites is required for activation of membrane fusion

Albar, JP, Wiley, DC, Melero, JA, Ruiz-Argüello, MB, Skehel, JJ, García-Barreno, B, González-Reyes, L, Calder, L, López, JA

Proc Natl Acad Sci U S A 2001
1765771 Post-translational processing and oligomerization of the fusion glycoprotein of human respiratory syncytial virus

Collins, PL, Mottet, G

J Gen Virol 1991
Participants
Input
Output
Participates
as an event of
Catalyst Activity

serine-type endopeptidase activity of Furin-type peptidase [trans-Golgi network membrane]

Physical Entity
Furin-type peptidase [trans-Golgi network membrane] (Homo sapiens)
Activity
serine-type endopeptidase activity (GO:0004252)
Disease
Authored
Stephan, R  (2023-02-22)
Reviewed
Bergeron, HC  (2023-11-03)
Created
Stephan, R  (2023-02-24)
Cite Us!