Sendai-viral HN and F glycoproteins as probes of plasma-membrane protein catabolism in HTC cells. Studies with fusogenic reconstituted Sendai-viral envelopes
| Autor: | E. Ellen Billett, R T Earl, Mayer Rj, I M Hunneyball |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
Azides
Leupeptins Hemagglutinins Viral Deoxyglucose Protein degradation Membrane Fusion Biochemistry Ammonium Chloride Cell Line Liver Neoplasms Experimental Viral Envelope Proteins Viral envelope Animals Sodium Azide Molecular Biology chemistry.chemical_classification HN Protein biology Vesicle Membrane Proteins Cell Biology biology.organism_classification Sendai virus Transmembrane protein Parainfluenza Virus 1 Human Transplantation Membrane protein chemistry DNA Viral Glycoprotein Viral Fusion Proteins Research Article |
| Zdroj: | Biochemical Journal. 241:801-807 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj2410801 |
| Popis: | Reconstituted Sendai-viral envelopes (RSVE) were produced by the method of Vainstein, Hershkovitz, Israel & Loyter [(1984) Biochim. Biophys. Acta 773, 181-188]. RSVE are fusogenic unilamellar vesicles containing two transmembrane glycoproteins: the HN (haemagglutinin-neuraminidase) protein and the F (fusion) factor. The fate of the viral proteins after fusion-mediated transplantation of RSVE into hepatoma (HTC) cell plasma membranes was studied to probe plasma-membrane protein degradation. Both protein species are degraded at similar, relatively slow, rates (t1/2 = 67 h) in HTC cells fused with RSVE in suspension. Even slower degradation rates for HN and F proteins (t1/2 = 93 h) were measured when RSVE were fused with HTC cells in monolayer. Lysosomal degradation of the transplanted viral proteins is strongly implicated by the finding that degradation of HN and F proteins is sensitive to inhibition by 10 mM-NH4Cl (81%) and by 50 micrograms of leupeptin/ml (70%). |
| Databáze: | OpenAIRE |
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