Journal of Experimental Medicine, Vol 156, 1010-1024, Copyright © 1982 by Rockefeller University Press
Immunoglobulin VH determinants defined by monoclonal antibodies
H Kubagawa, M Mayumi, JF Kearney and MD Cooper
Hybridoma clones secreting antibodies against common VH determinants were
readily produced by fusion of cells from mice immunized with isolated V mu
fragments of human immunoglobulins (Ig), but not with intact Ig molecules
or isolated heavy chains. Four monoclonal antibodies to the V mu fragments
of different IgM paraproteins were selected for analysis: MH-44 (mu kappa),
GB-24 (mu kappa), NF-11 (gamma 1 kappa), and SA-44 (gamma 1 kappa). Each
antibody reacted with the homologous V mu fragment, homologous mu chain,
and normal gamma chains, but not with the intact IgM molecules, intact IgG,
or isolated light chains, as determined by radioimmunoassay. The VH
reaction spectra with a panel of myeloma heavy chains showed overlapping
but distinctive patterns for the four antibodies. Each of the four
monoclonal anti-VH antibodies appeared to react with a different "hidden"
VH determinant that is not exposed on undenatured, intact Ig molecules and
differs from conventional VH subgroup determinants. In immunofluorescence
studies, the monoclonal anti-VH antibodies did not bind to surface Ig on
viable B lymphocytes, but visibly stained subpopulations of fixed B
lymphocytes, pre-B cells, and normal plasma cells. The mean frequencies of
VH+ plasma cells were 30% (MH-44), 17% (GB-24), 13% (NF-11), and 3%
(SA-44), and similar frequencies were obtained for the VH+ B cell
subpopulations. While subpopulations of B cells could be identified at all
stages in differentiation by immunofluorescence with the anti-VH
antibodies, neither resting nor activated T cells expressed these VH
determinants in detectable amounts.
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