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The interaction between different domains of staphylococcal protein A and human polyclonal IgG, IgA, IgM and F(ab')2: separation of affinity from specificity

Ljungberg, Ulla K; Jansson, Birger; Niss, Ulf; Nilsson, Rune LU ; Sandberg, Bengt E B and Nilsson, Björn (1993) In Molecular Immunology 30(14). p.1279-1285
Abstract
Binding properties of staphylococcal protein A (SpA) to different human immunoglobulins have been investigated. In this analysis, intact SpA as well as SpA-derived fragments containing one to five IgG-binding domains of different compositions, were used. The affinity binding constants of the different proteins to human polyclonal IgG, IgA, IgM and F(ab')2-fragments as well as their binding capacity to the immunoglobulin molecules were determined. The results show that although all the proteins bound to IgG, regardless of size or composition, the binding strength differed significantly. Proteins containing five domains have a stronger affinity for IgG than those containing one or two. There were no marked differences in binding strength... (More)
Binding properties of staphylococcal protein A (SpA) to different human immunoglobulins have been investigated. In this analysis, intact SpA as well as SpA-derived fragments containing one to five IgG-binding domains of different compositions, were used. The affinity binding constants of the different proteins to human polyclonal IgG, IgA, IgM and F(ab')2-fragments as well as their binding capacity to the immunoglobulin molecules were determined. The results show that although all the proteins bound to IgG, regardless of size or composition, the binding strength differed significantly. Proteins containing five domains have a stronger affinity for IgG than those containing one or two. There were no marked differences in binding strength between different domains. However, the binding ability to IgA and IgM showed a marked difference between the various SpA-derived proteins of different compositions. This discrepancy was correlated to differences in their relative binding properties to isolated F(ab')2-fragments of IgG. Hence, we conclude that the binding affinity is mainly affected by the number of domains, whereas the binding specificity is to a large extent determined by which domains are selected. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Immunology
volume
30
issue
14
pages
1279 - 1285
publisher
Pergamon
external identifiers
  • pmid:8413328
  • scopus:0027488503
ISSN
1872-9142
DOI
10.1016/0161-5890(93)90044-C
language
English
LU publication?
yes
id
5ddd5a42-75a7-4f33-832f-fc17b1ea074c (old id 1106999)
date added to LUP
2008-07-30 09:10:18
date last changed
2017-08-13 04:22:55
@article{5ddd5a42-75a7-4f33-832f-fc17b1ea074c,
  abstract     = {Binding properties of staphylococcal protein A (SpA) to different human immunoglobulins have been investigated. In this analysis, intact SpA as well as SpA-derived fragments containing one to five IgG-binding domains of different compositions, were used. The affinity binding constants of the different proteins to human polyclonal IgG, IgA, IgM and F(ab')2-fragments as well as their binding capacity to the immunoglobulin molecules were determined. The results show that although all the proteins bound to IgG, regardless of size or composition, the binding strength differed significantly. Proteins containing five domains have a stronger affinity for IgG than those containing one or two. There were no marked differences in binding strength between different domains. However, the binding ability to IgA and IgM showed a marked difference between the various SpA-derived proteins of different compositions. This discrepancy was correlated to differences in their relative binding properties to isolated F(ab')2-fragments of IgG. Hence, we conclude that the binding affinity is mainly affected by the number of domains, whereas the binding specificity is to a large extent determined by which domains are selected.},
  author       = {Ljungberg, Ulla K and Jansson, Birger and Niss, Ulf and Nilsson, Rune and Sandberg, Bengt E B and Nilsson, Björn},
  issn         = {1872-9142},
  language     = {eng},
  number       = {14},
  pages        = {1279--1285},
  publisher    = {Pergamon},
  series       = {Molecular Immunology},
  title        = {The interaction between different domains of staphylococcal protein A and human polyclonal IgG, IgA, IgM and F(ab')2: separation of affinity from specificity},
  url          = {http://dx.doi.org/10.1016/0161-5890(93)90044-C},
  volume       = {30},
  year         = {1993},
}