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Presence of cross-reactive antibody between human immunodeficiency virus
(HIV) and platelet glycoproteins in HIV-related immune thrombocytopenic
purpura
A Bettaieb, P Fromont, F Louache, E Oksenhendler, W Vainchenker, N Duedari and P Bierling
Centre de Transfusion, INSERM U91, Hopital Henri Mondor, Creteil, France.
We previously reported the presence in platelet eluates of autoantibodies
directed against epitopes of the platelet glycoprotein (GP)IIb/IIIa complex
in acquired immunodeficiency syndrome (AIDS)-free human immunodeficiency
virus (HIV)-infected patients with immunologic thrombocytopenic purpura
(ITP). We investigated whether HIV antibodies recognized platelet membrane
antigens to determine whether the virus might be directly or indirectly
responsible for the thrombocytopenia in this context. Direct eluates of
platelets from 25 patients with HIV- related ITP contained IgG reacting
with HIV-GP160/120 and also, in 45% of patients, detectable antiplatelet
antibodies, immunochemically characterized as anti-GPIIb and/or anti-GPIIIa
in 5 patients. Furthermore, serum HIV-GP160/120 antibodies could be
absorbed on and eluted from platelets from normal non-HIV-infected healthy
blood donors (indirect eluates). In contrast, GP160/120 antibodies present
in the serum of nonthrombocytopenic HIV-infected patients were not
absorbable on normal platelets in most patients, suggesting a pathogenic
role in HIV-related ITP. We performed detailed studies of a patient with
the highest titer of both HIV-GP160/120 and GPIIb/IIIa antibodies in direct
and indirect platelet eluates. No antibody binding to GPIIb/IIIa- deficient
Glanzmann thrombasthenic platelets was detected. Furthermore,
binding/elution experiments conducted with insoluble recombinant GP160
(expressed in baculovirus) and purified platelet GPIIb/IIIa demonstrated
that the patient's IgG bound specifically, through the F(ab')2 portion, to
a common epitope of HIV-GP160/120 and platelet GPIIb/IIIa. This common
epitope was present on a recombinant GP160 expressed in baculovirus but
absent from another recombinant GP160 expressed in vaccinia virus,
suggesting that the cross-reactivity is dependent on the glycosylation or
conformational structure of the GP. We conclude that molecular mimicry
between HIV-GP160/120 and platelet GPIIb/IIIa may explain at least some
cases of ITP in AIDS-free HIV- infected patients.
Volume 80,
Issue 1,
pp. 162-169,
07/01/1992
Copyright © 1992 by The American Society of Hematology
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