Amino Acid Sequences of Plant and Animal Viral Proteins

Oroszlan, Stephen; Gilden, Raymond V.

doi:10.1007/978-1-4684-3453-8_1

Cited by 2 publications

(4 citation statements)

References 90 publications

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“…8, arrow). Amino acid residues in the pp2O sequence were identical to residues in the RSV sequence at 11 of 28 compared positions. The probability of observing this degree of amino acid sequence homology by random selection was calculated to be less than 1 in 107 from an alignment score of 5.22 given by the ALIGN program (6).…”

Section: Discussionmentioning

confidence: 88%

“…39:1611, 1980). These observations suggest that the enzyme catalyzing the proteolytic cleavages of D-type gag precursor polyproteins may show a substrate specificity similar to that of other mammalian and avian C-type retrovirus proteases (7,27,28,30,49).…”

Section: Lanementioning

confidence: 79%

“…The N-terminal amino acid sequences of the p12 protein from R-D/W and the p12 protein from MPMV were nearly identical to each other except for substitutions in MPMV of an alanine for serine at position 14, a glutamic acid for glycine at position 24, and an alanine for glutamine at position 28 (Fig. 7).…”

Section: Lanementioning

confidence: 82%

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Purification and N-terminal amino acid sequence comparisons of structural proteins from retrovirus-D/Washington and Mason-Pfizer monkey virus

Henderson¹,

Sowder²,

Smythers³

et al. 1985

J Virol

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A new D-type retrovirus originally designated SAIDS-D/Washington and here referred to as retrovirus-D/Washington (R-D/W) was recently isolated at the University of Washington Primate Center, Seattle, Wash., from a rhesus monkey with an acquired immunodeficiency syndrome and retroperitoneal fibromatosis. To better establish the relationship of this new D-type virus to the prototype D-type virus, Mason-Pfizer monkey virus (MPMV), we have purified and compared six structural proteins from each virus. The proteins purified from each D-type retrovirus include p4, p10, p12, p14, p27, and a phosphoprotein designated ppl8 for MPMV and pp2O for R-D/W. Amino acid analysis and N-terminal amino acid sequence analysis show that the p4, p12, p14, and p27 proteins of R-D/W are distinct from the homologous proteins of MPMV but that these proteins from the two different viruses share a high degree of amino acid sequence homology. The plO proteins from the two viruses have similar amino acid compositions, and both are blocked to N-terminal Edman degradation. The phosphoproteins from the two viruses each contain phosphoserine but are different from each other in amino acid composition, molecular weight, and N-terminal amino acid sequence. The data thus show that each of the R-D/W proteins examined is distinguishable from its MPMV homolog and that a major difference between these two D-type retroviruses is found in the viral phosphoproteins. The N-terminal amino acid sequences of D-type retroviral proteins were used to search for sequence homologies between D-type and other retroviral amino acid sequences. An unexpected amino acid sequence homology was found between R-D/W pp2O (a gag protein) and a 28-residue segment of the env precursor polyprotein of Rous sarcoma virus. The N-terminal amino acid sequences of the D-type major gag protein (p27) and the nucleic acid-binding protein (p14) show only limited amino acid sequence homology to functionally homologous proteins of C-type retroviruses.

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Section: Discussionmentioning

confidence: 88%

Section: Lanementioning

confidence: 79%

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Purification and N-terminal amino acid sequence comparisons of structural proteins from retrovirus-D/Washington and Mason-Pfizer monkey virus

Henderson¹,

Sowder²,

Smythers³

et al. 1985

J Virol

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show abstract

“…The above pulse-chase experiments with avian and murine retrovirus-infected cells strongly suggested that a proteinase was involved in cleavage of the Gag and probably Gag-Pol polyproteins. Further, the knowledge that identical N-terminal amino acids of MuLV p30 (Pro-Leu-Arg) occurred in the p30s of several murine retroviruses and that Pro was found as the invariant N-terminus of the CA protein of other retroviruses suggested that such a proteinase has a high degree of specificity (OROSZLAN et al 1975;OROSZLAN et al 1978;OROSZLAN and GILDEN 1979;OROSZLAN and GILDEN 1980). The observation that the retroviral polyproteins undergo proteolytic processing was followed by reports that both avian and murine retroviruses contain a proteolytic factor as part of the virus particle.…”

Section: Introduction and Historical Perspectivementioning

confidence: 97%