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On the interaction between protein L and immunoglobulins of various mammalian species

De Château, M; Nilson, B H LU ; Erntell, M; Myhre, E LU ; Magnusson, C G LU ; Åkerström, B LU and Björck, L LU (1993) In Scandinavian Journal of Immunology 37(4). p.399-405
Abstract

Protein L, a cell wall molecule of certain strains of the anaerobic bacterial species Peptostreptococcus magnus, shows high affinity for human immunoglobulin (Ig) light chains. In the present study protein L was tested against a panel of human myeloma proteins of the IgG, IgM, IgA and IgE classes, and strong binding was seen with antibodies carrying kappa light chains. A high degree of specificity for Ig was demonstrated in binding experiments with human plasma proteins. Apart from human Ig, strong protein L-binding activity was also detected in the serum of 12 out of 23 tested additional mammalian species, including other primates and rodents. Subsequent analysis with purified Ig samples demonstrated the binding of protein L to Ig of... (More)

Protein L, a cell wall molecule of certain strains of the anaerobic bacterial species Peptostreptococcus magnus, shows high affinity for human immunoglobulin (Ig) light chains. In the present study protein L was tested against a panel of human myeloma proteins of the IgG, IgM, IgA and IgE classes, and strong binding was seen with antibodies carrying kappa light chains. A high degree of specificity for Ig was demonstrated in binding experiments with human plasma proteins. Apart from human Ig, strong protein L-binding activity was also detected in the serum of 12 out of 23 tested additional mammalian species, including other primates and rodents. Subsequent analysis with purified Ig samples demonstrated the binding of protein L to Ig of important laboratory animal species such as the mouse, the rat and the rabbit. The affinity constants for the interactions between protein L and polyclonal IgG of these species were 2.6 x 10(9), 3.9 x 10(8) and 7.4 x 10(7), respectively. In non-human species, the binding of protein L was also found to be mediated through Ig light chains, and the results demonstrate the potential value of protein L as an immunochemical tool.

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keywords
Animals, Bacterial Proteins, Binding Sites, Blood Proteins, Goats, Humans, Immunoglobulin Light Chains, Immunoglobulin kappa-Chains, Mice, Nerve Tissue Proteins, Peptostreptococcus, Rabbits, Rats, Species Specificity, Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
in
Scandinavian Journal of Immunology
volume
37
issue
4
pages
7 pages
publisher
Wiley-Blackwell
external identifiers
  • scopus:0027536968
ISSN
0300-9475
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language
English
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yes
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6cbf7ed7-92f8-4bc8-85c8-cb53a78ad499
date added to LUP
2018-05-26 14:01:18
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2018-06-03 05:07:03
@article{6cbf7ed7-92f8-4bc8-85c8-cb53a78ad499,
  abstract     = {<p>Protein L, a cell wall molecule of certain strains of the anaerobic bacterial species Peptostreptococcus magnus, shows high affinity for human immunoglobulin (Ig) light chains. In the present study protein L was tested against a panel of human myeloma proteins of the IgG, IgM, IgA and IgE classes, and strong binding was seen with antibodies carrying kappa light chains. A high degree of specificity for Ig was demonstrated in binding experiments with human plasma proteins. Apart from human Ig, strong protein L-binding activity was also detected in the serum of 12 out of 23 tested additional mammalian species, including other primates and rodents. Subsequent analysis with purified Ig samples demonstrated the binding of protein L to Ig of important laboratory animal species such as the mouse, the rat and the rabbit. The affinity constants for the interactions between protein L and polyclonal IgG of these species were 2.6 x 10(9), 3.9 x 10(8) and 7.4 x 10(7), respectively. In non-human species, the binding of protein L was also found to be mediated through Ig light chains, and the results demonstrate the potential value of protein L as an immunochemical tool.</p>},
  author       = {De Château, M and Nilson, B H and Erntell, M and Myhre, E and Magnusson, C G and Åkerström, B and Björck, L},
  issn         = {0300-9475},
  keyword      = {Animals,Bacterial Proteins,Binding Sites,Blood Proteins,Goats,Humans,Immunoglobulin Light Chains,Immunoglobulin kappa-Chains,Mice,Nerve Tissue Proteins,Peptostreptococcus,Rabbits,Rats,Species Specificity,Comparative Study,Journal Article,Research Support, Non-U.S. Gov't},
  language     = {eng},
  number       = {4},
  pages        = {399--405},
  publisher    = {Wiley-Blackwell},
  series       = {Scandinavian Journal of Immunology},
  title        = {On the interaction between protein L and immunoglobulins of various mammalian species},
  url          = {http://dx.doi.org/},
  volume       = {37},
  year         = {1993},
}