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Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus

Authors :
Housden, N.G.
Harrison, S.
Roberts, S.E.
Beckingham, J.A.
Graille, M.
Stura, E.
Gore, M.G.
Source :
Biochemical Society Transactions; June 2003, Vol. 31 Issue: 3 p716-718, 3p
Publication Year :
2003

Abstract

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 CH2-CH3 heavy chains, while Protein L binds exclusively to the VL domain of the κ-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 κ-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 κ-chain than the second site.

Details

Language :
English
ISSN :
03005127 and 14708752
Volume :
31
Issue :
3
Database :
Supplemental Index
Journal :
Biochemical Society Transactions
Publication Type :
Periodical
Accession number :
ejs51267420
Full Text :
https://doi.org/10.1042/bst0310716