Human monoclonal antibody against glycoproteins of human immunodeficiency virus

Toru Sugano, Yasuhiko Masuho, Yoh ichi Matsumoto, Douglas Lake, Charles Gschwind, Eskild A. Petersen, Evan M. Hersh

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


We have established a program to make human monoclonal antibodies to the human immunodeficiency virus (HIV). Lymphocytes of lymph nodes from patients with the acquired immunodeficiency syndrome (AIDS) related complex (ARC) spontaneously produced antibodies to HIV in vitro and their antibody production was suppressed by culturing them in the presence of HIV antigens. Therefore, in vitro stimulation with HIV antigens was not done but rather, donor lymph node or spleen lymphocytes were directly fused with mouse myeloma cells. One of the hybridomas thus generated has been stably producing human monoclonal antibody (MAb) of the IgGl isotype with a kappa chain. This antibody, MAb86, bound to the surface membrane of HIV-infected cells but not to that of uninfected cells at all. MAb86 reacted in Western blot with both viral glycoproteins of 120,000 daltons (gpl20) and 41,000 daltons (gp41). While not neutralizing alone, a combination of MAb86 with another human IgGl MAb against gpl20 showed viral neutralization. Based on these data it seems likely that this approach will result in human MAbs capable of viral neutralization and antibody-dependent cytotoxicity. These may have value for the prevention and/or treatment of AIDS.

Original languageEnglish (US)
Pages (from-to)1105-1112
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Sep 30 1988
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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