Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus.

@article{Housden2003ImmunoglobulinbindingDP,
  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},
  year={2003},
  volume={31 Pt 3},
  pages={
          716-8
        }
}
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 and Tables from this paper

Identification of a Phage-Encoded Ig-Binding Protein from Invasive Neisseria meningitidis
TLDR
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*
TLDR
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.
Neisseria meningitidis Protein from Invasive Identification of a Phage-Encoded Ig-Binding
TLDR
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.
Chicken anti-protein L for the detection of small amounts of protein L in the presence of IgG.
TLDR
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
TLDR
This study demonstrates a successful example of functional protein engineering via in vitro molecular evolution and provides a useful approach to remold the Ig binding property of SpA for application purposes.
Rationally designed ligands for use in affinity chromatography: an artificial protein L.
TLDR
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.
Bioaffinity sorbent based on immobilized protein A Staphylococcus aureus: development and application
TLDR
The designed bioaffinity sorbent provides obtaining pure polyand monoclonal antibodies in functionally active form and can be useful for the fractionation of mouse immunoglobulin G.
...
...

References

SHOWING 1-5 OF 5 REFERENCES
Biochemistry
  • F. Young
  • Education
    The Indian Medical Gazette
  • 1955
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
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