Abstract：
:The fusion (F) glycoprotein of respiratory syncytial virus (RSV) is synthesized as a nonfusogenic precursor protein (F(0)), which during its migration to the cell surface is activated by cleavage into the disulfide-linked F(1) and F(2) subunits. In the present study, soluble secreted human furin produced by a recombinant baculovirus cleaved RSV F(0) into proteins the size of F(1) and F(2). Furthermore, cleavage of F(0) was partially inhibited in the furin defective LoVo cell line, in calcium depleted HEp-2 cells, and in HEp-2 cells treated with the furin inhibitor decanoyl-R-V-K-R-chloromethylketon. These findings strongly suggest an important role for furin in activation of the RSV F protein. The F(0) protein could not be detected on the surface of cells, in which F protein activation was inhibited, and RSV particles did not appear to be released from these cells. It thus seems that in contrast to the F proteins of most other paramyxoviruses, the RSV F(0) protein is very inefficient in reaching the cell surface or is unable to reach the cell surface and therefore cannot be incorporated into virus particles.
journal_name
Virus Resjournal_title
Virus researchauthors
Bolt G,Pedersen LO,Birkeslund HHdoi
10.1016/s0168-1702(00)00149-0subject
Has Abstractpub_date
2000-06-01 00:00:00pages
25-33issue
1eissn
0168-1702issn
1872-7492pii
S0168-1702(00)00149-0journal_volume
68pub_type
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