Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus

N. G. Housden; S. Harrison; S. E. Roberts; J. A. Beckingham; M. Graille; E. Stura; M. G. Gore

doi:10.1042/BST0310716

Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus

N. G. Housden, S. Harrison, S. E. Roberts, J. A. Beckingham, M. Graille, E. Stura, M. G. Gore

Research output: Contribution to journal › Article › peer-review

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 C_H2-C_H3 heavy chains, while Protein L binds exclusively to the V_L 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.

Original language	English
Pages (from-to)	716-718
Number of pages	3
Journal	Biochemical Society Transactions
Volume	31
Issue number	3
DOIs	https://doi.org/10.1042/BST0310716
Publication status	Published - 1 Jun 2003
Externally published	Yes

Keywords

Dissociation constant
Immunoglobulin
Mutant
Sequence

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10.1042/BST0310716

Cite this

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title = "Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus",

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.",

keywords = "Dissociation constant, Immunoglobulin, Mutant, Sequence",

author = "Housden, \{N. G.\} and S. Harrison and Roberts, \{S. E.\} and Beckingham, \{J. A.\} and M. Graille and E. Stura and Gore, \{M. G.\}",

year = "2003",

month = jun,

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doi = "10.1042/BST0310716",

language = "English",

volume = "31",

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journal = "Biochemical Society Transactions",

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TY - JOUR

T1 - Immunoglobulin-binding domains

T2 - Protein L from Peptostreptococcus magnus

AU - Housden, N. G.

AU - Harrison, S.

AU - Roberts, S. E.

AU - Beckingham, J. A.

AU - Graille, M.

AU - Stura, E.

AU - Gore, M. G.

PY - 2003/6/1

Y1 - 2003/6/1

N2 - 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.

AB - 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.

KW - Dissociation constant

KW - Immunoglobulin

KW - Mutant

KW - Sequence

U2 - 10.1042/BST0310716

DO - 10.1042/BST0310716

M3 - Article

C2 - 12773190

AN - SCOPUS:0038540555

SN - 0300-5127

VL - 31

SP - 716

EP - 718

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

IS - 3

ER -

Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus

Abstract

Keywords

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