• DOI:10.1042/BST0310716
• Corpus ID: 10322322

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
        }
}

• N. G. Housden, S. Harrison, +4 authors M. Gore
• Published 1 June 2003
• Biology, Medicine
• Biochemical Society transactions

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 function of these proteins in vivo is not clear but it is thought that they enable the bacteria to evade the host's immune system. Two binding sites for kappa -chain on a single Ig-binding domain from Protein L have recently been reported and we give evidence that one site has a 25-55-fold higher affinity for kappa -chain than the second site.