Retrovirus-encoded transformation-specific polyproteins

Expression coordinated with malignant phenotype in cells from different germ layers

A. P. Chen, M. Essex, J. A. Shadduck, J. Y. Niederkorn, D. Albert

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

A transformation-associated polyprotein designated 'gag-x' was previously shown to be induced by the feline sarcoma virus (FeSV) after the nonproductive transformation of rat or mink cells. We found that this protein was also expressed in cells derived from the native species (cat) with or without the production of feline leukemia helper virus (FeLV) and that cats could mount a humoral antibody response to the transformation-specific (x) portion of the molecule. Such antisera also reacted with the feline oncornavirus-associated cell membrane antigen (FOCMA) by membrane immunofluorescence. Expression of the gag-x protein was coordinated with malignant phenotype in that both transformed cat fibroblasts and cultured cells from a FeSV-induced melanoma expressed antigenically indistinguishable proteins of the same size. These cells are derived from different embryonic germ layers, suggesting that such transformation-related proteins may function in a pleiotropic manner when introduced by a virus.

Original languageEnglish (US)
Pages (from-to)3915-3919
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume78
Issue number6 I
DOIs
StatePublished - 1981

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Polyproteins
Germ Layers
Feline Sarcoma Viruses
Retroviridae
gag Gene Products
Cats
Phenotype
Helper Viruses
Feline Leukemia Virus
Mink
Proteins
Antibody Formation
Fluorescent Antibody Technique
Immune Sera
Cultured Cells
Melanoma
Fibroblasts
Viruses
Membranes

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

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abstract = "A transformation-associated polyprotein designated 'gag-x' was previously shown to be induced by the feline sarcoma virus (FeSV) after the nonproductive transformation of rat or mink cells. We found that this protein was also expressed in cells derived from the native species (cat) with or without the production of feline leukemia helper virus (FeLV) and that cats could mount a humoral antibody response to the transformation-specific (x) portion of the molecule. Such antisera also reacted with the feline oncornavirus-associated cell membrane antigen (FOCMA) by membrane immunofluorescence. Expression of the gag-x protein was coordinated with malignant phenotype in that both transformed cat fibroblasts and cultured cells from a FeSV-induced melanoma expressed antigenically indistinguishable proteins of the same size. These cells are derived from different embryonic germ layers, suggesting that such transformation-related proteins may function in a pleiotropic manner when introduced by a virus.",
author = "Chen, {A. P.} and M. Essex and Shadduck, {J. A.} and Niederkorn, {J. Y.} and D. Albert",
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T1 - Retrovirus-encoded transformation-specific polyproteins

T2 - Expression coordinated with malignant phenotype in cells from different germ layers

AU - Chen, A. P.

AU - Essex, M.

AU - Shadduck, J. A.

AU - Niederkorn, J. Y.

AU - Albert, D.

PY - 1981

Y1 - 1981

N2 - A transformation-associated polyprotein designated 'gag-x' was previously shown to be induced by the feline sarcoma virus (FeSV) after the nonproductive transformation of rat or mink cells. We found that this protein was also expressed in cells derived from the native species (cat) with or without the production of feline leukemia helper virus (FeLV) and that cats could mount a humoral antibody response to the transformation-specific (x) portion of the molecule. Such antisera also reacted with the feline oncornavirus-associated cell membrane antigen (FOCMA) by membrane immunofluorescence. Expression of the gag-x protein was coordinated with malignant phenotype in that both transformed cat fibroblasts and cultured cells from a FeSV-induced melanoma expressed antigenically indistinguishable proteins of the same size. These cells are derived from different embryonic germ layers, suggesting that such transformation-related proteins may function in a pleiotropic manner when introduced by a virus.

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