Further evidence from tryptic peptide analysis for heterogeneity among type D retroviruses

Uckert, Wolfgang; Hertling, I; Denner, Joachim

doi:10.1007/bf01309302

Cited by 7 publications

(3 citation statements)

References 23 publications

(16 reference statements)

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“…Previously we were able to use the technique of tryptic peptide analysis to distinguish between the low-molecular-weight proteins of different type D retroviruses (26). To further characterize the proteins of R-D/NE we compared tryptic peptide maps of p 4, p 10/p 12, p 15, and p 27 to those of MPMV and PMFV.…”

Section: Discussionmentioning

confidence: 99%

“…Viral structural proteins were sliced from the gel and tryptic peptide analysis of ~2~I labelled proteins were performed on cellulose thin layer chromatography plates (10 × 10 cm) (Merck, Federal Republic of Germany) as described previously (26).…”

Section: Tryptic Peptide Analysis Of Proteinsmentioning

confidence: 99%

“…These viruses resemble MPMV in many respects but can be clearly distinguished by their different glycoprotein pattern (28) and tryptic peptide maps of tow-molecular-weight proteins (26). lgecently, type D retroviruses have been isolated from several macaque species at several Primate Centers in the U.S. (5,15,16,23).…”

Section: Introductionmentioning

confidence: 99%

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Biochemical and immunological characterization of structural proteins from retrovirus-D/New England and comparison to Mason-Pfizer monkey virus and permanent human fibroblast virus

Uckert¹,

Wunderlich²,

Fiebach³

et al. 1987

Archives of Virology

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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 14C 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 3H glucosamine. The 18,000 Da protein was identified as a phosphoprotein of R-D/NE. p18 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.

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Section: Discussionmentioning

confidence: 99%

Section: Tryptic Peptide Analysis Of Proteinsmentioning

confidence: 99%