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A common theme in interaction of bacterial immunoglobulin-binding proteins with immunoglobulins illustrated in the equine system

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A common theme in interaction of bacterial immunoglobulin-binding proteins with immunoglobulins illustrated in the equine system. / Lewis, Melanie J.; Meehan, Mary; Owen, Peter; Woof, Jennifer M. (Lead / Corresponding author).

In: Journal of Biological Chemistry, Vol. 283, No. 25, 20.06.2008, p. 17615-17623.

Research output: Contribution to journalArticle

Harvard

Lewis, MJ, Meehan, M, Owen, P & Woof, JM 2008, 'A common theme in interaction of bacterial immunoglobulin-binding proteins with immunoglobulins illustrated in the equine system' Journal of Biological Chemistry, vol 283, no. 25, pp. 17615-17623., 10.1074/jbc.M709844200

APA

Lewis, M. J., Meehan, M., Owen, P., & Woof, J. M. (2008). A common theme in interaction of bacterial immunoglobulin-binding proteins with immunoglobulins illustrated in the equine system. Journal of Biological Chemistry, 283(25), 17615-17623. 10.1074/jbc.M709844200

Vancouver

Lewis MJ, Meehan M, Owen P, Woof JM. A common theme in interaction of bacterial immunoglobulin-binding proteins with immunoglobulins illustrated in the equine system. Journal of Biological Chemistry. 2008 Jun 20;283(25):17615-17623. Available from: 10.1074/jbc.M709844200

Author

Lewis, Melanie J.; Meehan, Mary; Owen, Peter; Woof, Jennifer M. (Lead / Corresponding author) / A common theme in interaction of bacterial immunoglobulin-binding proteins with immunoglobulins illustrated in the equine system.

In: Journal of Biological Chemistry, Vol. 283, No. 25, 20.06.2008, p. 17615-17623.

Research output: Contribution to journalArticle

Bibtex - Download

@article{36d0f5cb99324edcbefe85c00ee8591d,
title = "A common theme in interaction of bacterial immunoglobulin-binding proteins with immunoglobulins illustrated in the equine system",
keywords = "FC-ALPHA-RI, STREPTOCOCCUS-EQUI, SUBSP EQUI, FIBRINOGEN-BINDING, STAPHYLOCOCCUS-AUREUS, COMPLEMENT ACTIVATION, CLASSICAL PATHWAY, MUCOSAL ANTIBODY, IMMUNE-RESPONSES, IGG SUBCLASSES",
author = "Lewis, {Melanie J.} and Mary Meehan and Peter Owen and Woof, {Jennifer M.}",
year = "2008",
doi = "10.1074/jbc.M709844200",
volume = "283",
number = "25",
pages = "17615--17623",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - A common theme in interaction of bacterial immunoglobulin-binding proteins with immunoglobulins illustrated in the equine system

A1 - Lewis,Melanie J.

A1 - Meehan,Mary

A1 - Owen,Peter

A1 - Woof,Jennifer M.

AU - Lewis,Melanie J.

AU - Meehan,Mary

AU - Owen,Peter

AU - Woof,Jennifer M.

PY - 2008/6/20

Y1 - 2008/6/20

N2 - <p>The M protein of Streptococcus equi subsp. equi known as fibrinogen-binding protein (FgBP) is a cell wall-associated protein with antiphagocytic activity that binds IgG. Recombinant versions of the seven equine IgG subclasses were used to investigate the subclass specificity of FgBP. FgBP bound predominantly to equine IgG4 and IgG7, with little or no binding to the other subclasses. Competitive binding experiments revealed that FgBP could inhibit the binding of staphylococcal protein A and streptococcal protein G to both IgG4 and IgG7, implicating the Fc interdomain region in binding to FgBP. To identify which of the two IgG Fc domains contributed to the interaction with FgBP, we tested two human IgG1/IgA1 domain swap mutants and found that both domains are required for full binding, with the CH3 domain playing a critical role. The binding site for FgBP was further localized using recombinant equine IgG7 antibodies with single or double point mutations to residues lying at the CH2-CH3 interface. We found that interaction of FgBP with equine IgG4 and IgG7 was able to disrupt C1q binding and antibody-mediated activation of the classical complement pathway, demonstrating an effective means by which S. equi may evade the immune response. The mode of interaction of FgBP with IgG fits a common theme for bacterial Ig-binding proteins. Remarkably, for those interactions studied in detail, it emerges that all the Ig-binding proteins target the CH2-CH3 domain interface, regardless of specificity for IgG or IgA, streptococcal or staphylococcal origin, or host species (equine or human).</p>

AB - <p>The M protein of Streptococcus equi subsp. equi known as fibrinogen-binding protein (FgBP) is a cell wall-associated protein with antiphagocytic activity that binds IgG. Recombinant versions of the seven equine IgG subclasses were used to investigate the subclass specificity of FgBP. FgBP bound predominantly to equine IgG4 and IgG7, with little or no binding to the other subclasses. Competitive binding experiments revealed that FgBP could inhibit the binding of staphylococcal protein A and streptococcal protein G to both IgG4 and IgG7, implicating the Fc interdomain region in binding to FgBP. To identify which of the two IgG Fc domains contributed to the interaction with FgBP, we tested two human IgG1/IgA1 domain swap mutants and found that both domains are required for full binding, with the CH3 domain playing a critical role. The binding site for FgBP was further localized using recombinant equine IgG7 antibodies with single or double point mutations to residues lying at the CH2-CH3 interface. We found that interaction of FgBP with equine IgG4 and IgG7 was able to disrupt C1q binding and antibody-mediated activation of the classical complement pathway, demonstrating an effective means by which S. equi may evade the immune response. The mode of interaction of FgBP with IgG fits a common theme for bacterial Ig-binding proteins. Remarkably, for those interactions studied in detail, it emerges that all the Ig-binding proteins target the CH2-CH3 domain interface, regardless of specificity for IgG or IgA, streptococcal or staphylococcal origin, or host species (equine or human).</p>

KW - FC-ALPHA-RI

KW - STREPTOCOCCUS-EQUI

KW - SUBSP EQUI

KW - FIBRINOGEN-BINDING

KW - STAPHYLOCOCCUS-AUREUS

KW - COMPLEMENT ACTIVATION

KW - CLASSICAL PATHWAY

KW - MUCOSAL ANTIBODY

KW - IMMUNE-RESPONSES

KW - IGG SUBCLASSES

UR - http://ukpmc.ac.uk/articles/PMC2427354

UR - http://www.scopus.com/inward/record.url?scp=47749136972&partnerID=8YFLogxK

U2 - 10.1074/jbc.M709844200

DO - 10.1074/jbc.M709844200

M1 - Article

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 25

VL - 283

SP - 17615

EP - 17623

ER -

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