The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Carl Borrebaeck

Carl Borrebaeck

Professor

Carl Borrebaeck

Low affinity, antibody binding of an Escherichia coli-derived component

Author

  • Mats Ohlin
  • C. A K Borrebaeck

Summary, in English

This investigation describes the detection of a component in Escherichia coli capable of binding a large proportion of human antibody variable domains including otherwise highly monospecific antibodies induced by an in vivo antibody response. This interaction is of low affinity, but cross-linking of IgG molecules by, e.g. anti-immunoglobulin preparations, provides a sufficient degree of multivalency to promote a high avidity interaction. This binding which occurs both with K and h light chain-containing antibodies, appears to involve the variable region of human antibodies making it a superantigen-like activity. This is proposed based on the facts that: (i) different human antibodies of IgG1 isotype appear to bind to different extents suggesting that variable domain differences determine the binding activity; and (ii) addition of soluble antigen abrogates the interaction with the E. coli-derived molecule. Future studies of the nature and possible in vivo consequences of these interactions are warranted since any superantigen activity associated with this binding might affect the human immune response occurring as a consequence of E. coli infections.

Department/s

  • Department of Immunotechnology

Publishing year

1996-02

Language

English

Pages

161-168

Publication/Series

FEMS Immunology and Medical Microbiology

Volume

13

Issue

2

Document type

Journal article

Publisher

Wiley-Blackwell

Keywords

  • Antibody variable domain
  • Antibody-binding molecule
  • Escherichia coli
  • Superantigen

Status

Published

ISBN/ISSN/Other

  • ISSN: 0928-8244