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VL Ng, KM Hwang, GR Reyes, LD Kaplan, H Khayam-Bashi, WK Hadley and MS McGrath
Department of Laboratory Medicine, UCSF.
We observed a human immunodeficiency virus (HIV)-infected homosexual male
with AIDS related complex (ARC) who had a serum globulin level of 80 g/L.
Serum protein electrophoresis revealed a gamma globulin fraction of 40 g/L,
of which 50% (20 g/L) was contained within a paraprotein spike, comprised
predominantly of IgG kappa. This patient also had high titer anti-HIV
antibodies in his serum, which were Western blot reactive at a final
dilution of 1:500,000, and recognized gp120env, p66pol, p55gag, p53pol,
p41gag, and p24gag. Because paraproteins in the past have been shown to be
directed against specific antigens, we purified this patient's paraprotein
using a modified high performance liquid chromatography
(HPLC)-hydroxylapatite procedure and tested the purified paraprotein for
anti-HIV antibody activity. The purified paraprotein retained anti-HIV
antibody activity to a final dilution of 1:100,000, and recognized p66pol,
p55gag, p53pol, p41gag, and p24gag. The recognition of both "gag" and "pol"
gene products suggested that the purified paraprotein might not be
monoclonal in origin. Sodium dodecyl sulfate-polyacrylamide gel
electrophoresis (SDS-PAGE) demonstrated that the purified paraprotein
contained at least two immunoglobulin light chain species (Mol wt 30 to 33
Kd). Affinity chromatography of the purified paraprotein using a p24-
Sepharose 4B matrix separated the "gag" and "pol" antibody activities.
Immunoglobulin gene rearrangement analysis of a bone marrow aspirate (which
contained 15% plasma cells) failed to reveal a clonal population of
immunoglobulin producing cells. We conclude that this patient's paraprotein
accounted for most of the anti-HIV activity present in whole serum, and
that this paraprotein was not monoclonal in origin.
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