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Non-immune IgG F(ab')2 binding to group C and G streptococci is mediated by structures on gamma chains.

Abstract：

:The present investigation was designed to determine whether the heavy or the light immunoglobulin chain is involved in the non-immune binding of IgG F(ab')2 fragments to specific surface receptors on human group C and G streptococci. Purified human polyclonal IgG was mildly reduced with dithiothreitol and alkylated with iodoacetamide. Light (L) and heavy (H) chains were separated. Intact IgG and purified L and H chains of polyclonal immunoglobulin G were tested in an inhibition assay for non-immune IgG F(ab')2-mediated binding to group C and G streptococci. H chains inhibited the uptake of isotope-labelled IgG F(ab')2 fragments. Isolated L chains were non-reactive. Intact IgG molecules were more potent inhibitors than isolated H chains tested in equimolar concentrations. These results indicate that the non-immune interaction between human group C and G streptococci and F(ab')2 fragments of human IgG is mediated by reactive sites exposed on the immunoglobulin G H chains. The observation that intact IgG on a molar basis was more inhibitory than purified gamma chains suggests that the L chains may contribute to the reactivity, presumably by passive stabilization of the immunoglobulin molecule.

journal_name

Scand J Immunol

journal_title

Scandinavian journal of immunology

authors

Erntell M,Myhre EB,Kronvall G

doi

10.1111/j.1365-3083.1985.tb01414.x

subject

Has Abstract

pub_date

1985-02-01 00:00:00

pages

151-7

issue

2

eissn

0300-9475

issn

1365-3083

journal_volume

21

pub_type

杂志文章

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