Lymphoma-selective antibody Lym-1 recognizes a discontinuous epitope on the light chain of HLA-DR10

Larry M. Rose, Angelo H. Gunasekera, Sally J. DeNardo, Gerald L Denardo, Claude F. Meares

Research output: Contribution to journalArticle

58 Scopus citations

Abstract

The selectivity of Lym-1 for malignant B lymphocytes makes this monoclonal antibody a promising candidate for the delivery of toxic agents to malignant B cells. The original immunogen used for the development of Lym-1 was Raji Burkitt's lymphoma cell nuclei [Epstein A.L., Marder R.J., Winter J.N., Stathopoulos E., Chen F.M., Parker J.W., Taylor C.R. (1987) Cancer Res 47: 830]. The Lym-1 antigen was characterized at that time as a polymorphic HLA-DR variant. We prepared an affinity column using immobilized Lym-1 to isolate the Lym-1 antigen from Raji cell lysate. Immunological characterization of the immunoaffinity-purified Lym-1 antigen on Western blots led to the conclusion that the antigen is the β chain of HLA-DR10. This was confirmed by Edman sequencing of the isolated polypeptide chain. Western blots further show that the Lym-1 epitope is only recognized if the β chain disulfide bonds are intact. These results imply that Lym-1 binds a discontinuous epitope on the β chain of HLA-DR10.

Original languageEnglish (US)
Pages (from-to)26-30
Number of pages5
JournalCancer Immunology Immunotherapy
Volume43
Issue number1
DOIs
StatePublished - 1996

Keywords

  • B cell lymphocytic cancer antigen
  • HLA-DR10
  • Lym-1
  • Radioimmunotherapy
  • Tumor-selective antibodies

ASJC Scopus subject areas

  • Cancer Research
  • Immunology
  • Oncology

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