The interaction of Sendai virus glycoprotein-bearing recombinant vesicles with cell surfaces.
Biochim Biophys Acta
; 854(2): 157-68, 1986 Jan 29.
Article
in En
| MEDLINE
| ID: mdl-3002466
ABSTRACT
Sendai virus glycoproteins HN and F were purified by immunoaffinity chromatography from virions disrupted by beta-D-octylglucoside. The purified glycoproteins were reconstituted in recombinant vesicles with phosphatidylcholine or phosphatidylethanolamine and phosphatidylserine. P815 or EL-4 cells treated with glycoprotein HN/F-phosphatidylcholine recombinant vesicles acquired the glycoproteins and retained them in the plasma membrane for 4 h as demonstrated by surface immunofluorescence specific for each protein. Cells treated with glycoprotein HN-phosphatidylcholine recombinant vesicles initially bore glycoprotein HN on the surface but the protein eluted within 2 h. Surfaces of cells treated with glycoprotein F-phosphatidylcholine recombinant vesicles did not acquire the glycoprotein. Cells treated with glycoprotein HN-phosphatidylethanolamine phosphatidylserine recombinant vesicles or glycoprotein F-phosphatidylethanolamine phosphatidylserine recombinant vesicles in the presence of 5 mM Ca2+ acquired each protein for at least 2 h. Experiments showed that the acquired glycoproteins capped with antibody and that when glycoproteins HN and F were together on the surface they co-capped. Acquired viral glycoproteins did not co-cap with intrinsic H-2 glycoproteins.
Search on Google
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Viral Envelope Proteins
/
Parainfluenza Virus 1, Human
Limits:
Animals
Language:
En
Journal:
Biochim Biophys Acta
Year:
1986
Type:
Article