Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus.

  title={Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus.},
  author={Nicholas G. Housden and Steven L Harrison and S E Roberts and Jennifer A. Beckingham and Marc Graille and Enrico A. Stura and Michael G. Gore},
  journal={Biochemical Society transactions},
  volume={31 Pt 3},
Protein L is a multidomain cell-wall protein isolated from Peptostreptococcus magnus. It belongs to a group of proteins that contain repeated domains that are able to bind to Igs without stimulating an immune response, the most characterized of this group being Protein A ( Staphylococcus aureus ) and Protein G ( Streptococcus ). Both of these proteins bind predominantly to the interface of C(H)2-C(H)3 heavy chains, while Protein L binds exclusively to the V(L) domain of the kappa -chain. The… 

Figures, Tables, and Topics from this paper

Identification of a Phage-Encoded Ig-Binding Protein from Invasive Neisseria meningitidis
The results show that TspB mediated IgG binding and aggregate/biofilm formation triggered by factors in human serum may provide protection against immune responses, which is in accordance with the association of prophage DNA carrying ORF6 with invasive meningococcal strains.
Crystal Structure of a Mucus-binding Protein Repeat Reveals an Unexpected Functional Immunoglobulin Binding Activity*
Mub repeats were able to interact in vitro with a large repertoire of mammalian Igs, including secretory IgA, consistent with the current model that antibody responses against commensal flora are of broad specificity and low affinity.
Chicken anti-protein L for the detection of small amounts of protein L in the presence of IgG.
A sandwich ELISA for detection of protein L in the presence or absence of mouse IgG utilizing specific chicken IgY antibodies is developed, which can be used to detect protein L at a concentration of 0.3 ng/mL inThe presence of IgG.
Tailoring the binding properties of SpA Ig binding domains by in vitro molecular evolution
Background: Staphylococcus aureus protein A (SpA) is a bacterial immunoglobulin (Ig)-binding protein (IBP) and has fundamental applications in medical and biological sciences associated with IgG. In
MBOVPG45_0375 Encodes an IgG-Binding Protein and MBOVPG45_0376 Encodes an IgG-Cleaving Protein in Mycoplasma bovis
Reconstructing recombinant MBOVPG45_0375 in the Escherichia coli expression system and demonstrating that r0375 can bind to IgG non-immunologically rather than specific binding similar to interaction of antigen and antibody offer a new insight into the interaction between M. bovis and its host.
A synthetic Protein G adsorbent based on the multi-component Ugi reaction for the purification of mammalian immunoglobulins.
The use of the solid phase multi-component Ugi reaction to generate a low cost, rationally designed, affinity ligand to mimic Protein G for the purification of mammalian immunoglobulins, including the heavy-chain only camelid IgGs, with effective elution at neutral pH is described.
Rationally designed ligands for use in affinity chromatography: an artificial protein L.
The concepts of rational design and solid-phase combinatorial chemistry were used for the discovery of a synthetic PpL mimic affinity ligand, and this chapter represents a general approach with the potential to be applied to different systems and target proteins.
An artificial protein L for the purification of immunoglobulins and fab fragments by affinity chromatography.
Ligand 8/7, which emerged as the lead from a de novo designed combinatorial library of ligands, inhibits the interaction of PpL with IgG and Fab by competitive ELISA and shows negligible binding to Fc.
In vitro molecular evolution of AL NEIBMs improved immunoglobulin (Ig) binding and antibody detection.
The present study demonstrates that the binding properties of AL were successfully improved through phage-based molecular evolution, which could substantially contribute to the use of AL in antibody detection, and provides an example of successful protein engineering through in vitro molecular evolution.
Bioaffinity sorbent based on immobilized protein A Staphylococcus aureus: development and application
Aim. The obtaining of bioaffinity sorbent based on the immobilized protein A of S. aureus (SPA) using two cellulose-binding domains (CBD), and its application for purification of antibodies. Methods.


Bacterial immunoglobulin-binding proteins—future trends
The driving force for any practical application involving bacterial immunoglobulin-binding proteins will be directed toward identifying the problem, determining the limitations of current reagents, and modifying or finding new reagents that will achieve the desired result.
The Department of Biochemistry is internationally recognized for its research and education and offers a world-class interdisciplinary research environment in a beautiful mountain setting. As part of
  • 1995
J. Mol. Biol. Eur. J. Biochem. Structure J. Biol. Chem. Biochem. J
  • J. Mol. Biol. Eur. J. Biochem. Structure J. Biol. Chem. Biochem. J
  • 1995
Biochemistry J. Biol. Chem. Mol. Microbiol
  • Biochemistry J. Biol. Chem. Mol. Microbiol
  • 1992
J. Mol. Biol
  • J. Mol. Biol
  • 1992