![[feed]](/style/images/feed-icon-14x14.png){kind=icon}
Tools
Tools
| Item Type: | Article |
|---|---|
| Title: | Biochemical and immunological characterization of structural proteins from retrovirus-D/New England and comparison to Mason-Pfizer monkey virus and permanent human fibroblast virus |
| Creators Name: | Uckert, W., Wunderlich, V., Fiebach, H., Hertling, I., Stein, U., Kraft, R. and Desrosiers, R. |
| Abstract: | Biochemical and immunological properties of retrovirus-D/New England (here referred as R-D/NE) recently isolated at the New England Regional Primate Research Center, Southborough, Ma, from a rhesus monkey with acquired immune deficiency syndrome were investigated and compared to the prototype type D retroviruses Mason-Pfizer monkey virus (MPMV) and permanent human fibroblast virus (PMFV) isolated from a breast carcinoma of a rhesus monkey and a continuous human cell line, respectively. The polypeptide composition of R-D/NE propagated in a human lymphoid B cell line (Raji cells) has been investigated using SDS-polyacrylamide gel electrophoresis. Staining with Coomassie blue and labelling with (14)C amino acids revealed seven viral polypeptides with molecular weights of 4,000, 10,000, 12,000, 15,000, 18,000, 27,000, and 80,000 Da which were also shared by MPMV and PMFV. The 80,000 Da protein was shown to be a glycoprotein by incorporation of (3)H glucosamine. The 18,000 Da protein was identified as a phosphoprotein of R-D/NE. p 18 structural proteins of MPMV and PMFV represent phosphoproteins of their respective viruses as well. All three phosphorylated proteins contain O-phosphoserine as major phosphoamino acid. The comparison of tryptic peptide maps of the major internal structural proteins of R-D/NE, MPMV, and PMFV revealed a striking similarity among p 10/p 12 and p 15. proteins. A minor difference was detected among the tryptic peptide digests of p 4 and p 27 proteins. Antiserum against p 15 of MPMV showed a significantly weaker binding to R-D/NE than to MPMV and PMFV at high dilutions. compared to our earlier findings of a gp 70 might be due to the different host cell lines used for virus propagation. Summarizing our data, R-D/NE seems to resemble in many properties more PMFV, the type D retrovirus isolated from a permanent human cell line, than MPMV. This is supported by our recent results obtained by restriction endonuclease site analysis of covalently closed circular DNA of R-D/NE, PMFV and MPMV. |
| Keywords: | Amino Acid Sequence, Amino Acids, Glycoproteins, Molecular Weight, Peptides, Phosphoproteins, Radioimmunoassay, Retroviridae, Retroviridae Proteins, Viral Antigens, Viral Proteins, Viral Structural Proteins, Animals |
| Source: | Archives of Virology |
| ISSN: | 0304-8608 |
| Publisher: | Springer |
| Volume: | 94 |
| Number: | 3-4 |
| Page Range: | 267-82 |
| Date: | September 1987 |
| Official Publication: | https://doi.org/10.1007/BF01310719 |
| PubMed: | View item in PubMed |
Repository Staff Only: item control page
