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Protein L from Peptostreptococcus magnus binds to the kappa light chain variable domain

Nilson, B H LU ; Solomon, A; Björck, L LU and Akerström, B LU (1992) In Journal of Biological Chemistry 267(4). p.9-2234
Abstract

Protein L is an immunoglobulin light chain-binding protein expressed by some strains of the anaerobic bacterial species Peptostreptococcus magnus. The major variable region subgroups of human kappa and lambda light chains were tested for protein L binding; V kappa I, V kappa III, and V kappa IV bound protein L, whereas no binding occurred with proteins of the V kappa II subgroup or with any lambda light chain subgroups. Studies of the protein L binding capacity of naturally occurring VL fragments, and VL- and CL-related trypsin- and pepsin-derived peptides prepared from a kappa I light chain, localized the site of interaction to the VL domain. The affinity constant for the binding to an isolated V kappa I fragment was comparable to that... (More)

Protein L is an immunoglobulin light chain-binding protein expressed by some strains of the anaerobic bacterial species Peptostreptococcus magnus. The major variable region subgroups of human kappa and lambda light chains were tested for protein L binding; V kappa I, V kappa III, and V kappa IV bound protein L, whereas no binding occurred with proteins of the V kappa II subgroup or with any lambda light chain subgroups. Studies of the protein L binding capacity of naturally occurring VL fragments, and VL- and CL-related trypsin- and pepsin-derived peptides prepared from a kappa I light chain, localized the site of interaction to the VL domain. The affinity constant for the binding to an isolated V kappa I fragment was comparable to that for the native protein (Ka 0.9 x 10(9) M-1 and Ka 1.5 x 10(9) M-1, respectively). No binding occurred with CL-related fragments. Extensive reduction and alkylation of the V kappa fragment or the native kappa chain resulted in complete loss of protein L binding. Although it is possible, from comparative amino acid sequence data, to identify certain VL-framework region residues that account for the selective binding of protein L by kappa I, kappa III, and kappa IV proteins, our studies indicate that this interaction is essentially dependent upon the tertiary structural integrity of the kappa chain VL domain.

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keywords
Amino Acid Sequence, Bacterial Proteins, Chromatography, Liquid, Electrophoresis, Polyacrylamide Gel, Humans, Immunoglobulin Variable Region, Immunoglobulin kappa-Chains, Molecular Sequence Data, Pepsin A, Peptostreptococcus, Protein Conformation, Radioimmunoassay, Trypsin, X-Ray Diffraction, Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.
in
Journal of Biological Chemistry
volume
267
issue
4
pages
9 - 2234
publisher
ASBMB
external identifiers
  • scopus:0026788385
ISSN
0021-9258
language
English
LU publication?
yes
id
414acb31-c655-4d49-8050-775b7255451c
alternative location
http://www.jbc.org/content/267/4/2234.abstract
date added to LUP
2018-05-26 14:03:52
date last changed
2018-06-10 05:29:09
@article{414acb31-c655-4d49-8050-775b7255451c,
  abstract     = {<p>Protein L is an immunoglobulin light chain-binding protein expressed by some strains of the anaerobic bacterial species Peptostreptococcus magnus. The major variable region subgroups of human kappa and lambda light chains were tested for protein L binding; V kappa I, V kappa III, and V kappa IV bound protein L, whereas no binding occurred with proteins of the V kappa II subgroup or with any lambda light chain subgroups. Studies of the protein L binding capacity of naturally occurring VL fragments, and VL- and CL-related trypsin- and pepsin-derived peptides prepared from a kappa I light chain, localized the site of interaction to the VL domain. The affinity constant for the binding to an isolated V kappa I fragment was comparable to that for the native protein (Ka 0.9 x 10(9) M-1 and Ka 1.5 x 10(9) M-1, respectively). No binding occurred with CL-related fragments. Extensive reduction and alkylation of the V kappa fragment or the native kappa chain resulted in complete loss of protein L binding. Although it is possible, from comparative amino acid sequence data, to identify certain VL-framework region residues that account for the selective binding of protein L by kappa I, kappa III, and kappa IV proteins, our studies indicate that this interaction is essentially dependent upon the tertiary structural integrity of the kappa chain VL domain.</p>},
  author       = {Nilson, B H and Solomon, A and Björck, L and Akerström, B},
  issn         = {0021-9258},
  keyword      = {Amino Acid Sequence,Bacterial Proteins,Chromatography, Liquid,Electrophoresis, Polyacrylamide Gel,Humans,Immunoglobulin Variable Region,Immunoglobulin kappa-Chains,Molecular Sequence Data,Pepsin A,Peptostreptococcus,Protein Conformation,Radioimmunoassay,Trypsin,X-Ray Diffraction,Journal Article,Research Support, Non-U.S. Gov't,Research Support, U.S. Gov't, P.H.S.},
  language     = {eng},
  month        = {02},
  number       = {4},
  pages        = {9--2234},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Protein L from Peptostreptococcus magnus binds to the kappa light chain variable domain},
  volume       = {267},
  year         = {1992},
}