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

Nilson, B H LU orcid ; 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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organization
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type
Contribution to journal
publication status
published
subject
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
American Society for Biochemistry and Molecular Biology
external identifiers
  • scopus:0026788385
  • pmid:1733930
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
2024-04-15 08:26:38
@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}},
  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.}},
  language     = {{eng}},
  month        = {{02}},
  number       = {{4}},
  pages        = {{9--2234}},
  publisher    = {{American Society for Biochemistry and Molecular Biology}},
  series       = {{Journal of Biological Chemistry}},
  title        = {{Protein L from Peptostreptococcus magnus binds to the kappa light chain variable domain}},
  url          = {{http://www.jbc.org/content/267/4/2234.abstract}},
  volume       = {{267}},
  year         = {{1992}},
}