Species specificity in the binding of IgG to macrophages.

Immunology ·Vol. 37 ·No. 4 ·1979-08-00 ·Pages 835-40

Leslie RG, Niemetz AH

Abstract

The binding of human IgG1 and IgG3 and rabbit IgG to guinea-pig peritoneal macrophages was examined, and differences between the species, in terms of their binding mechanisms, were characterized. Rabbit IgG bound with high affinity (Kass = 3.11 +/- 0.45 x 10(6) M-1) to a finite number of receptor sites per cell (1.26 +/- 0.29 x 10(6)) and competitively inhibited the binding of guinea-pig IgG2. Heterogeneity in binding, with distinct high and low affinity components, was observed when human IgG3 was reacted with guinea-pig macrophages, while human IgG1 exhibited only low affinity binding. Neither human IgG subclass competed effectively with guinea-pig IgG2 for its cell receptor. Thus, rabbit IgG appeared to cross-react with a macrophage receptor for guinea-pig immunoglobulin, whereas the human IgG subclasses bound to macrophage membrane components that remained undefined.

MeSH Terms

Animals Antibody Affinity Antigen-Antibody Reactions Binding Sites, Antibody Binding, Competitive Cross Reactions Guinea Pigs Humans Immunoglobulin G/immunology Macrophages/immunology Rabbits Receptors, Immunologic Species Specificity

Chemicals

Immunoglobulin G Receptors, Immunologic

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Leslie R G

Niemetz A H

References (13)

13 references, click to expand

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Article Info

Journal

Immunology

Abbr.

Immunology

ISSN

0019-2805

Published

1979-08-00

Pages

835-40

Language

English

Region

England

NLM ID

0374672

PMCID

PMC1457146

Subset

External Links

PubMed source PMC Full Text View journal details

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Species specificity in the binding of IgG to macrophages.

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