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PMID: 81316 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Virus-coded origin of a 32,000-dalton protein from avian retrovirus cores: structural relatedness of p32 and the beta polypeptide of the avian retrovirus DNA polymerase.

Journal of virology ·Vol. 28 ·No. 1 ·1978-10-00 ·Pages 279-91

Schiff RD, Grandgenett DP

Abstract

A 32,000-dalton protein (p32) located in avian retrovirus cores was immunoprecipitated from [35S]methionine-labeled avian myeloblastosis virus (AMV) propagated in cultured chicken embryo fibroblast cells by an antiserum preparation (sarc III) derived from tumor-bearing hamsters injected with cloned and passaged cells from an avian sarcoma virus-induced primary hamster tumor. Since sarc III serum apparently contained antibodies only to virus-coded proteins and not to chicken cellular proteins, the immunoprecipitation of p32 from AMV by sarc III serum strongly suggested that p32 is virus coded. The origin of p32 was more definitively established by demonstrating the existence of a structural relationship between p32 and the AMV DNA polymerase. AMV p32 cross-reacted with the beta polypeptide of AMV alphabeta DNA polymerase in radioimmunoprecipitation and radioimmunoprecipitation inhibition assays, indicating that p32 and beta share common antigenic determinants. This relationship was clarified by sodium do-decyl sulfate-polyacrylamide gel electrophoretic analysis of the peptides generated by limited proteolysis of 125I-labeled AMV DNA polymerase polypeptides and of 125I-labeled AMV p32 by chymotrypsin or Staphylococcus aureus V-8 protease. The peptides which appeared during proteolytic digestion of p32 were a subset of those produced by digestion of the beta polypeptide; however, p32 had no discernible peptides in common with the alpha polypeptide. Further, all of the peptides produced by limited proteolysis of beta were present in the digests of either p32 or alpha. Our findings suggest that p32 is apparently derived by cleavage of the beta polypeptide of AMV DNA polymerase, presumably at a site near or identical to that at which alpha is generated from beta by proteolytic cleavage.

MeSH Terms
Animals Avian Leukosis Virus/analysis Avian Myeloblastosis Virus/analysis,enzymology,immunology Chick Embryo Culture Techniques Epitopes Molecular Weight Peptides/analysis,immunology Protein Conformation RNA-Directed DNA Polymerase/analysis,immunology Viral Proteins/analysis,immunology
Chemicals
Epitopes Peptides Viral Proteins RNA-Directed DNA Polymerase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Schiff R D
Grandgenett D P
References (45)
45 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.28.1.279-291.1978
Published
1978-10-00
Pages
279-91
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC354267
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.28.1.279-291.1978 PMC Full Text View journal details
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