Protein L from Peptostreptococcus magnus binds to the kappa light chain variable domain
(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.
(Less)
- author
- Nilson, B H LU ; Solomon, A ; Björck, L LU and Akerström, B LU
- organization
- publishing date
- 1992-02-05
- 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
- 2024-09-03 20:15:28
@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}}, }