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Original article| Volume 113, ISSUE 3, P387-395, March 1989

Neutrophil chemiluminescence induced by opsonized group A streptococcal particles: An effective probe of intravenous immunoglobulin preparations

  • R. Rüfenacht
    Affiliations
    From the Institute for Clinical and Experimental Cancer Research and the Institute of Veterinary Virology, University of Bern Bern, Switzerland
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  • P. Chase
    Affiliations
    From the Institute for Clinical and Experimental Cancer Research and the Institute of Veterinary Virology, University of Bern Bern, Switzerland
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  • T.W. Jungi
    Affiliations
    From the Institute for Clinical and Experimental Cancer Research and the Institute of Veterinary Virology, University of Bern Bern, Switzerland
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  • A. Morell
    Correspondence
    Reprint requests: A. Morell, MD, Medical Department, Central Laboratory of the Swiss Red Cross Blood Transfusion Service, Wankdofstrasse 10, 3000 Bern 22, Switzerland.
    Affiliations
    From the Institute for Clinical and Experimental Cancer Research and the Institute of Veterinary Virology, University of Bern Bern, Switzerland
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      Abstract

      We compared the capacity of eight different intravenous immunoglobulin (IVIG) preparations to opsonize streptococcal group A particles and to induce lumlnolenhanced chemiluminescence in neutrophil granulocytes. Antibodies to the streptococcal group A carbohydrate (A-CHO) antigen exposed on the particles were present in all preparations at high concentrations. In some preparations, anti-A-CHO consisted predominantly of either immunoglobulin G1 (IgG1) or IgG2, whereas in others, both IgG subclasses were equally represented. Dilutions of the IVIGs and of a normal IgG reference preparation were adjusted for their anti-A-CHO content, incubated with streptococcal particles, and exposed to neutrophil granulocytes isolated from normal blood. The various IVIGs differed in their capacity to elicit chemlluminesence signals. Some preparations, particularly those consisting of chemically modified IgG molecules, showed little activity, whereas others were comparable to the reference preparation. We concluded that to some extent such differences could be related to the IgG subclass composition of the antibody. However, of greater importance were the manufacturing procedures by which both the antigen-binding fragment and crystalllzable fragment portions, and thus the functional integrity of the IgG molecules, were more or less severely affected.

      Abbreviations:

      A-CHO = streptococcal group A carbohydrate (), EDTA = ethylenediaminetetraacetic acid (), ELISA = enzyme-linked immunosorbent assay (), Fab = antigen-binding fragment (), Fc = crystallizable fragment (), HEPES = N-2-hydroxyethylpiperazine-N′-2-ethanesulfonic acid (), IgG = immunoglobulin G (), MG = intravenous immunoglobulin (), PBS = phosphate-buffered saline solution (), PMA = phorbol 12-myristate 13-acetate ()
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