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

Ohlin, Mats LU and Borrebaeck, C. A K LU (1996) In Pathogens and Disease 13(2). p.161-168
Abstract

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... (More)

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.

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author
organization
publishing date
type
Contribution to journal
publication status
published
keywords
Antibody variable domain, Antibody-binding molecule, Escherichia coli, Superantigen
in
Pathogens and Disease
volume
13
issue
2
pages
8 pages
publisher
Wiley-Blackwell
external identifiers
  • Scopus:0030007515
ISSN
0928-8244
DOI
10.1111/j.1574-695X.1996.tb00230.x
language
English
LU publication?
yes
id
3b0e4bb8-b4d6-49df-bc08-f92ce337cead
date added to LUP
2016-04-19 14:08:10
date last changed
2016-04-22 13:29:16
@misc{3b0e4bb8-b4d6-49df-bc08-f92ce337cead,
  abstract     = {<p>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.</p>},
  author       = {Ohlin, Mats and Borrebaeck, C. A K},
  issn         = {0928-8244},
  keyword      = {Antibody variable domain,Antibody-binding molecule,Escherichia coli,Superantigen},
  language     = {eng},
  number       = {2},
  pages        = {161--168},
  publisher    = {ARRAY(0x8975b78)},
  series       = {Pathogens and Disease},
  title        = {Low affinity, antibody binding of an Escherichia coli-derived component},
  url          = {http://dx.doi.org/10.1111/j.1574-695X.1996.tb00230.x},
  volume       = {13},
  year         = {1996},
}