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Blood, Vol. 93 No. 11 (June 1), 1999:
pp. 3624-3631
Inhibition of Cell Adhesion by Antibodies to Arg-Gly-Asp (RGD) in
Normal Immunoglobulin for Therapeutic Use (Intravenous Immunoglobulin,
IVIg)
Tchavdar L. Vassilev,
Michel D. Kazatchkine,
Jean-Paul Duong Van
Huyen,
Medina Mekrache,
Emmanuelle Bonnin,
Jean Claude Mani,
Chantal Lecroubier,
Dirk Korinth,
Dominique Baruch,
Folke Schriever, and
Srini V. Kaveri
From INSERM U430 and the Université Pierre et Marie Curie,
Hôpital Broussais, Paris, France; INSERM U143, Hôpital de
Bicêtre, Bicêtre, France; CNRS UMR 9921, Montpellier, the
Laboratoire d'Hematologie, Hôtel Dieu, Paris, France; and the
Biomedical Research Centre Virchow Klinikum, Humboldt University,
Berlin, Germany.
Intravenous immunoglobulin (IVIg) therapy is associated with a broad
range of immunomodulatory activities. Several of the postulated
mechanisms of IVIg action relate to the presence of antibodies to
molecules relevant for regulation of the immune response.
This article reports that IVIg contains antibodies to the Arg-Gly-Asp
(RGD) sequence, and the attachment site of a number of adhesive
extracellular matrix proteins, including ligands for  1, 3, and
5 integrins. Anti-RGD antibodies were identified in IVIg by
enzyme-linked immunosorbent assay and by using the BIAcore (BIAcore,
Uppsala, Sweden) technology. The affinity of anti-RGD antibodies to a
synthetic RGD-containing peptide and to fibronectin (Fn) was found to
be in the micromolar range. F(ab')2 fragments specific
for RGD were purified from IVIg by affinity chromatography. Anti-RGD
F(ab')2 antibodies inhibited adenosine diphosphate
induced  IIb/3 integrin-mediated platelet aggregation and the
adhesion of activated 41 integrin-expressing B cells to Fn.
Adhesion of unstimulated platelets to fibrinogen (Fg) involving both
the  -chain dodecapeptide sequence and the RGD sequence was inhibited
by anti-RGD antibodies. In addition, adhesion of thrombin-stimulated platelets to von Willebrand factor or Fg was completely inhibited by
affinity-purified anti-RGD antibodies. Our results suggest that the
presence of natural IgG antibodies to the RGD motif may contribute to
the immunomodulatory and anti-inflammatory effects of therapeutic
preparations of normal IgG.
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