Monoclonal antibodies to Epstein-Barr virus-induced, transformation-associated cell surface antigens

Binding patterns and effect upon virus-specific T-cell cytotoxicity

M. Rowe, J. E K Hildreth, A. B. Rickinson, James Hildreth

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Abstract

Spleen cells from mice immunized with Epstein-Barr virus-transformed lymphoblastoid cells (EB-LCL) were used to generate monoclonal antibodies to cell surface antigens associated with the EB virus-transformed state. Radioimmune and immunofluorescence binding assays identified two antibodies, MHM6 and AC2, which reacted consistently with all EB-LCL tested, with a subpopulation of cells in some but not all EB virus genome-positive Burkitt lymphoma lines, but with none of a range of EB virus genome-negative cell lines of lymphoma or leukaemia origin. While MHM6 appeared to bind an EB virus-related antigen, AC2 bound some other cell surface antigen which was also found on a small subpopulation of cells in lymphocyte cultures stimulated with phytohaemagglutinin or with pokeweed mitogen. MHM6 and AC2 recognized single polypeptides with apparent molecular weights of 45 kd and 80 kd respectively as shown by sodium dodecyl-sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of 125I-labelled cell surface polypeptides immuno-precipitated with these antibodies. These polypeptides were induced on experimentally-infected B cells within 24 h of the expression of the EB virus nuclear antigen, EBNA, at a time known to coincide with the appearance of the lymphocyte-detected membrane antigen, LYDMA. However, saturating concentrations of MHM6 and of AC2 were unable to protect EB-LCL target cells from lysis by LYDMA-specific cytotoxic T cells in a chromium-release assay.

Original languageEnglish (US)
Pages (from-to)373-381
Number of pages9
JournalInternational Journal of Cancer
Volume29
Issue number4
StatePublished - 1982
Externally publishedYes

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Surface Antigens
Human Herpesvirus 4
Monoclonal Antibodies
Viruses
T-Lymphocytes
Peptides
Genome
Lymphocytes
Antigens
Pokeweed Mitogens
Nuclear Antigens
Burkitt Lymphoma
Antibodies
Phytohemagglutinins
Chromium
Sodium Dodecyl Sulfate
Fluorescent Antibody Technique
Polyacrylamide Gel Electrophoresis
Lymphoma
Leukemia

ASJC Scopus subject areas

  • Cancer Research
  • Oncology

Cite this

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title = "Monoclonal antibodies to Epstein-Barr virus-induced, transformation-associated cell surface antigens: Binding patterns and effect upon virus-specific T-cell cytotoxicity",
abstract = "Spleen cells from mice immunized with Epstein-Barr virus-transformed lymphoblastoid cells (EB-LCL) were used to generate monoclonal antibodies to cell surface antigens associated with the EB virus-transformed state. Radioimmune and immunofluorescence binding assays identified two antibodies, MHM6 and AC2, which reacted consistently with all EB-LCL tested, with a subpopulation of cells in some but not all EB virus genome-positive Burkitt lymphoma lines, but with none of a range of EB virus genome-negative cell lines of lymphoma or leukaemia origin. While MHM6 appeared to bind an EB virus-related antigen, AC2 bound some other cell surface antigen which was also found on a small subpopulation of cells in lymphocyte cultures stimulated with phytohaemagglutinin or with pokeweed mitogen. MHM6 and AC2 recognized single polypeptides with apparent molecular weights of 45 kd and 80 kd respectively as shown by sodium dodecyl-sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of 125I-labelled cell surface polypeptides immuno-precipitated with these antibodies. These polypeptides were induced on experimentally-infected B cells within 24 h of the expression of the EB virus nuclear antigen, EBNA, at a time known to coincide with the appearance of the lymphocyte-detected membrane antigen, LYDMA. However, saturating concentrations of MHM6 and of AC2 were unable to protect EB-LCL target cells from lysis by LYDMA-specific cytotoxic T cells in a chromium-release assay.",
author = "M. Rowe and Hildreth, {J. E K} and Rickinson, {A. B.} and James Hildreth",
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T1 - Monoclonal antibodies to Epstein-Barr virus-induced, transformation-associated cell surface antigens

T2 - Binding patterns and effect upon virus-specific T-cell cytotoxicity

AU - Rowe, M.

AU - Hildreth, J. E K

AU - Rickinson, A. B.

AU - Hildreth, James

PY - 1982

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N2 - Spleen cells from mice immunized with Epstein-Barr virus-transformed lymphoblastoid cells (EB-LCL) were used to generate monoclonal antibodies to cell surface antigens associated with the EB virus-transformed state. Radioimmune and immunofluorescence binding assays identified two antibodies, MHM6 and AC2, which reacted consistently with all EB-LCL tested, with a subpopulation of cells in some but not all EB virus genome-positive Burkitt lymphoma lines, but with none of a range of EB virus genome-negative cell lines of lymphoma or leukaemia origin. While MHM6 appeared to bind an EB virus-related antigen, AC2 bound some other cell surface antigen which was also found on a small subpopulation of cells in lymphocyte cultures stimulated with phytohaemagglutinin or with pokeweed mitogen. MHM6 and AC2 recognized single polypeptides with apparent molecular weights of 45 kd and 80 kd respectively as shown by sodium dodecyl-sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of 125I-labelled cell surface polypeptides immuno-precipitated with these antibodies. These polypeptides were induced on experimentally-infected B cells within 24 h of the expression of the EB virus nuclear antigen, EBNA, at a time known to coincide with the appearance of the lymphocyte-detected membrane antigen, LYDMA. However, saturating concentrations of MHM6 and of AC2 were unable to protect EB-LCL target cells from lysis by LYDMA-specific cytotoxic T cells in a chromium-release assay.

AB - Spleen cells from mice immunized with Epstein-Barr virus-transformed lymphoblastoid cells (EB-LCL) were used to generate monoclonal antibodies to cell surface antigens associated with the EB virus-transformed state. Radioimmune and immunofluorescence binding assays identified two antibodies, MHM6 and AC2, which reacted consistently with all EB-LCL tested, with a subpopulation of cells in some but not all EB virus genome-positive Burkitt lymphoma lines, but with none of a range of EB virus genome-negative cell lines of lymphoma or leukaemia origin. While MHM6 appeared to bind an EB virus-related antigen, AC2 bound some other cell surface antigen which was also found on a small subpopulation of cells in lymphocyte cultures stimulated with phytohaemagglutinin or with pokeweed mitogen. MHM6 and AC2 recognized single polypeptides with apparent molecular weights of 45 kd and 80 kd respectively as shown by sodium dodecyl-sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of 125I-labelled cell surface polypeptides immuno-precipitated with these antibodies. These polypeptides were induced on experimentally-infected B cells within 24 h of the expression of the EB virus nuclear antigen, EBNA, at a time known to coincide with the appearance of the lymphocyte-detected membrane antigen, LYDMA. However, saturating concentrations of MHM6 and of AC2 were unable to protect EB-LCL target cells from lysis by LYDMA-specific cytotoxic T cells in a chromium-release assay.

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