Glycoprotein encoded by the Friend spleen focus-forming virus

S. Dresler, M. Ruta, M. J. Murray, David Kabat

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

The Friend spleen focus-forming virus (F-SFFV) released from cultured erythroleukemia cells (cell line F4-6/K) was cloned free of its helper lymphatic leukemia virus (F-MuLV). After allowing adsorption to Sc-1 fibroblasts at a low multiplicity of infection, the cells were seeded individually into wells of a microtiter test plate and the resulting colonies were grown into large cultures. Among 14 of these cell cultures that have been analyzed thoroughly, 6 contained F-SFFV alone, 1 contained F-MuLV plus F-SFFV, and 7 were uninfected. Each of the Sc-1 cell lines which had been infected with cloned F-SFFV contained a glycoprotein with an apparent molecular weight of 55,000 (gp 55) that was absent from the cell lines that lacked F-SFFV, gp55 was also present in Friend erythroleukemia cells and in fibroblasts infected with an F-SFFV that had been doubly cloned in another laboratory. These results indicate that gp55 is encoded by the F-SFFV genome, gp55 has the following additional properties. It can be immunoprecipitated with antiserum made to the F-MuLV virion envelope glycoprotein (gp75). Its unglycosylated polypeptide, formed in cells treated with 2-deoxy-D-glycose, has a molecular weight of approximately 45,000. Its tryptic peptide map contains peptides in common with F-MuLV gp75 but it also contains unique peptides. It appears to be absent or present in only low concentrations in erythroleukemia cell plasma membranes as determined by lactoperoxidase-catalyzed iodination, and it accumulates intracellularly in large amounts. In addition, it is absent from released virions. The majority of the cellular gp55 has an isoelectric point of 8.5 to 9.0. These results are consistent with the idea that an env gene recombination event was involved in the origin of F-SFFV.

Original languageEnglish (US)
Pages (from-to)564-575
Number of pages12
JournalJournal of Virology
Volume30
Issue number2
StatePublished - 1979

Fingerprint

Spleen Focus-Forming Viruses
glycoproteins
Glycoproteins
spleen
viruses
Leukemia, Erythroblastic, Acute
Peptides
cell lines
Cell Line
Virion
peptides
virion
fibroblasts
Fibroblasts
Molecular Weight
Cell Membrane
Lactoperoxidase
env Genes
iodination
cells

ASJC Scopus subject areas

  • Immunology

Cite this

Dresler, S., Ruta, M., Murray, M. J., & Kabat, D. (1979). Glycoprotein encoded by the Friend spleen focus-forming virus. Journal of Virology, 30(2), 564-575.

Glycoprotein encoded by the Friend spleen focus-forming virus. / Dresler, S.; Ruta, M.; Murray, M. J.; Kabat, David.

In: Journal of Virology, Vol. 30, No. 2, 1979, p. 564-575.

Research output: Contribution to journalArticle

Dresler, S, Ruta, M, Murray, MJ & Kabat, D 1979, 'Glycoprotein encoded by the Friend spleen focus-forming virus', Journal of Virology, vol. 30, no. 2, pp. 564-575.
Dresler S, Ruta M, Murray MJ, Kabat D. Glycoprotein encoded by the Friend spleen focus-forming virus. Journal of Virology. 1979;30(2):564-575.
Dresler, S. ; Ruta, M. ; Murray, M. J. ; Kabat, David. / Glycoprotein encoded by the Friend spleen focus-forming virus. In: Journal of Virology. 1979 ; Vol. 30, No. 2. pp. 564-575.
@article{93fa5a2cc4e849cfb097a4cf93e83539,
title = "Glycoprotein encoded by the Friend spleen focus-forming virus",
abstract = "The Friend spleen focus-forming virus (F-SFFV) released from cultured erythroleukemia cells (cell line F4-6/K) was cloned free of its helper lymphatic leukemia virus (F-MuLV). After allowing adsorption to Sc-1 fibroblasts at a low multiplicity of infection, the cells were seeded individually into wells of a microtiter test plate and the resulting colonies were grown into large cultures. Among 14 of these cell cultures that have been analyzed thoroughly, 6 contained F-SFFV alone, 1 contained F-MuLV plus F-SFFV, and 7 were uninfected. Each of the Sc-1 cell lines which had been infected with cloned F-SFFV contained a glycoprotein with an apparent molecular weight of 55,000 (gp 55) that was absent from the cell lines that lacked F-SFFV, gp55 was also present in Friend erythroleukemia cells and in fibroblasts infected with an F-SFFV that had been doubly cloned in another laboratory. These results indicate that gp55 is encoded by the F-SFFV genome, gp55 has the following additional properties. It can be immunoprecipitated with antiserum made to the F-MuLV virion envelope glycoprotein (gp75). Its unglycosylated polypeptide, formed in cells treated with 2-deoxy-D-glycose, has a molecular weight of approximately 45,000. Its tryptic peptide map contains peptides in common with F-MuLV gp75 but it also contains unique peptides. It appears to be absent or present in only low concentrations in erythroleukemia cell plasma membranes as determined by lactoperoxidase-catalyzed iodination, and it accumulates intracellularly in large amounts. In addition, it is absent from released virions. The majority of the cellular gp55 has an isoelectric point of 8.5 to 9.0. These results are consistent with the idea that an env gene recombination event was involved in the origin of F-SFFV.",
author = "S. Dresler and M. Ruta and Murray, {M. J.} and David Kabat",
year = "1979",
language = "English (US)",
volume = "30",
pages = "564--575",
journal = "Journal of Virology",
issn = "0022-538X",
publisher = "American Society for Microbiology",
number = "2",

}

TY - JOUR

T1 - Glycoprotein encoded by the Friend spleen focus-forming virus

AU - Dresler, S.

AU - Ruta, M.

AU - Murray, M. J.

AU - Kabat, David

PY - 1979

Y1 - 1979

N2 - The Friend spleen focus-forming virus (F-SFFV) released from cultured erythroleukemia cells (cell line F4-6/K) was cloned free of its helper lymphatic leukemia virus (F-MuLV). After allowing adsorption to Sc-1 fibroblasts at a low multiplicity of infection, the cells were seeded individually into wells of a microtiter test plate and the resulting colonies were grown into large cultures. Among 14 of these cell cultures that have been analyzed thoroughly, 6 contained F-SFFV alone, 1 contained F-MuLV plus F-SFFV, and 7 were uninfected. Each of the Sc-1 cell lines which had been infected with cloned F-SFFV contained a glycoprotein with an apparent molecular weight of 55,000 (gp 55) that was absent from the cell lines that lacked F-SFFV, gp55 was also present in Friend erythroleukemia cells and in fibroblasts infected with an F-SFFV that had been doubly cloned in another laboratory. These results indicate that gp55 is encoded by the F-SFFV genome, gp55 has the following additional properties. It can be immunoprecipitated with antiserum made to the F-MuLV virion envelope glycoprotein (gp75). Its unglycosylated polypeptide, formed in cells treated with 2-deoxy-D-glycose, has a molecular weight of approximately 45,000. Its tryptic peptide map contains peptides in common with F-MuLV gp75 but it also contains unique peptides. It appears to be absent or present in only low concentrations in erythroleukemia cell plasma membranes as determined by lactoperoxidase-catalyzed iodination, and it accumulates intracellularly in large amounts. In addition, it is absent from released virions. The majority of the cellular gp55 has an isoelectric point of 8.5 to 9.0. These results are consistent with the idea that an env gene recombination event was involved in the origin of F-SFFV.

AB - The Friend spleen focus-forming virus (F-SFFV) released from cultured erythroleukemia cells (cell line F4-6/K) was cloned free of its helper lymphatic leukemia virus (F-MuLV). After allowing adsorption to Sc-1 fibroblasts at a low multiplicity of infection, the cells were seeded individually into wells of a microtiter test plate and the resulting colonies were grown into large cultures. Among 14 of these cell cultures that have been analyzed thoroughly, 6 contained F-SFFV alone, 1 contained F-MuLV plus F-SFFV, and 7 were uninfected. Each of the Sc-1 cell lines which had been infected with cloned F-SFFV contained a glycoprotein with an apparent molecular weight of 55,000 (gp 55) that was absent from the cell lines that lacked F-SFFV, gp55 was also present in Friend erythroleukemia cells and in fibroblasts infected with an F-SFFV that had been doubly cloned in another laboratory. These results indicate that gp55 is encoded by the F-SFFV genome, gp55 has the following additional properties. It can be immunoprecipitated with antiserum made to the F-MuLV virion envelope glycoprotein (gp75). Its unglycosylated polypeptide, formed in cells treated with 2-deoxy-D-glycose, has a molecular weight of approximately 45,000. Its tryptic peptide map contains peptides in common with F-MuLV gp75 but it also contains unique peptides. It appears to be absent or present in only low concentrations in erythroleukemia cell plasma membranes as determined by lactoperoxidase-catalyzed iodination, and it accumulates intracellularly in large amounts. In addition, it is absent from released virions. The majority of the cellular gp55 has an isoelectric point of 8.5 to 9.0. These results are consistent with the idea that an env gene recombination event was involved in the origin of F-SFFV.

UR - http://www.scopus.com/inward/record.url?scp=0018776144&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0018776144&partnerID=8YFLogxK

M3 - Article

VL - 30

SP - 564

EP - 575

JO - Journal of Virology

JF - Journal of Virology

SN - 0022-538X

IS - 2

ER -