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Anti‐Interleukin‐6 Antibodies in Normal Human Serum
Author(s) -
HANSEN M. B.,
SVENSON M.,
DIAMANT M.,
BENDTZEN K.
Publication year - 1991
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1991.tb02552.x
Subject(s) - polyclonal antibodies , antibody , avidity , epitope , recombinant dna , microbiology and biotechnology , chemistry , biology , immunology , biochemistry , gene
High‐avidity IgG antibodies to the cytokine inlerleukin‐6 (IL‐6) were found in sera of apparently healthy adult individuals. These antibodies specifically interfered with an FLISA (enzyme‐linked immunosorbent assay) for IL‐6 in which specific polyclonal rabbit antibodies to human recombinant IL‐6 (rlL‐6) were used. Furthermore. using precipitation of 125 ‐I‐rIL‐6 with rabbit antibodies to human immunoglobulins (Ig). the sera of 7 out of 6S Danish blood donors were found to contain specific antibodies in substantial amounts. Judged by ELISA interference, gel filtration of sera incubated with 125 I‐rIL‐6 and second antibody precipitation of 125 I‐rIL‐6. IgG seemed to be the dominant IL‐6 binding protein in these normal sera. Using specific antibodies to human in light chains, it was found that the anti‐lL‐6 antibodies were of polyclonal origin. Moreover, there are at least two epitopes on the IL‐6 molecule, because more than one IgG bound lo some IL‐6 molecules at the same time, The anti‐IL‐6 antibodies did not cross‐react with a number of other human recombinant‐derived and native cytokines. The antibodies recognized native as well as rlL‐6. but preferentially monomeric lL‐6.