Fusion Injection of Rous Sarcoma Virus Proteins into Rous Sarcoma Virus-transformed, Non-producing Hamster Cells Causes Release of Infectious Virus

Frixen, U.; Helm, K. von der; Friis, Robert R.; Wille, Wolfgang; Willecke, Klaus

doi:10.1099/0022-1317-61-1-83

Cited by 2 publications

(2 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Another possibility is that a cellular component is required. This possibility is suggested by studies of RSV-infected mammalian cell lines, in which the gag precursor polypeptide is synthesized as a stable protein (11,36) yet no virus particles are formed (11). Infectious virus can be recovered from mammalian cell lines by fusion with chicken cells (33).…”

Section: Discussionmentioning

confidence: 99%

“…Infectious virus can be recovered from mammalian cell lines by fusion with chicken cells (33). Low levels of infectious virus also can be rescued by fusing the infected mammalian cells with red cell ghosts containing total AMV proteins (11), suggesting that components necessary for assembly may be carried by virions. A third possibility is that p19 associates with the membrane through electrostatic interactions with charged phospholipids, as has been inferred for the matrix, or M, protein of vesicular stomatitis virus (38,39).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Fine-structure analyses of lipid-protein and protein-protein interactions of gag protein p19 of the avian sarcoma and leukemia viruses by cyanogen bromide mapping

Pepinsky¹,

Vogt²

1984

J Virol

View full text Add to dashboard Cite

In avian sarcoma and leukemia viruses, the gag protein p19 functions structurally as a matrix protein, connecting internal components with the viral envelope. We have used a combination of in situ cross-linking and peptide mapping to localize within p19 the regions responsible for two major interactions in this complex, p19 with lipid and p19 with p19. Lipid-protein cross-links were localized near the amino terminus within the first 35 amino acids of the polypeptide. Homotypic protein-protein disulfide bridges were found to originate from near the carboxy terminus of p19, from cysteine residues at amino acids 111 and 153. These results suggest that p19 is divided into domains with distinct functions. The peptide maps constructed for p19, and for the related proteins p23 in avian sarcoma and leukemia viruses and p190 in recombinant avian sarcoma viruses, should serve as useful tools for other types of studies involving these proteins.

show abstract

Section: Discussionmentioning

confidence: 99%