The immunoglobulin constant region contributes to affinity and specificity

Marcela Torres; Arturo Casadevall

doi:10.1016/j.it.2007.11.004

The immunoglobulin constant region contributes to affinity and specificity

Marcela Torres, Arturo Casadevall

Research output: Contribution to journal › Review article › peer-review

95 Scopus citations

Abstract

A central dogma in immunology is that antibody specificity is solely the result of variable (V)-region interactions with an antigen. However, this view is not tenable in light of numerous reports that constant heavy (C_H) domains can affect binding affinity and specificity and V-region structure. Kinetic and thermodynamic proof for the occurrence of this phenomenon is now available. C_H-region effects on affinity and specificity suggest new mechanisms for generating antibody diversity and polyreactivity (multispecificity) that impact current views on idiotype regulation, autoimmunity, and B cell selection and change our understanding of vaccine responses.

Original language	English (US)
Pages (from-to)	91-97
Number of pages	7
Journal	Trends in Immunology
Volume	29
Issue number	2
DOIs	https://doi.org/10.1016/j.it.2007.11.004
State	Published - Feb 2008
Externally published	Yes

ASJC Scopus subject areas

Immunology and Allergy
Immunology

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10.1016/j.it.2007.11.004

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title = "The immunoglobulin constant region contributes to affinity and specificity",

abstract = "A central dogma in immunology is that antibody specificity is solely the result of variable (V)-region interactions with an antigen. However, this view is not tenable in light of numerous reports that constant heavy (CH) domains can affect binding affinity and specificity and V-region structure. Kinetic and thermodynamic proof for the occurrence of this phenomenon is now available. CH-region effects on affinity and specificity suggest new mechanisms for generating antibody diversity and polyreactivity (multispecificity) that impact current views on idiotype regulation, autoimmunity, and B cell selection and change our understanding of vaccine responses.",

author = "Marcela Torres and Arturo Casadevall",

note = "Funding Information: We thank Joshua D. Nosanchuk for critical review of the manuscript. This work was funded by NIH grants AI033142, AI033774, AI052733, and HL059842. ",

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AU - Casadevall, Arturo

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N2 - A central dogma in immunology is that antibody specificity is solely the result of variable (V)-region interactions with an antigen. However, this view is not tenable in light of numerous reports that constant heavy (CH) domains can affect binding affinity and specificity and V-region structure. Kinetic and thermodynamic proof for the occurrence of this phenomenon is now available. CH-region effects on affinity and specificity suggest new mechanisms for generating antibody diversity and polyreactivity (multispecificity) that impact current views on idiotype regulation, autoimmunity, and B cell selection and change our understanding of vaccine responses.

AB - A central dogma in immunology is that antibody specificity is solely the result of variable (V)-region interactions with an antigen. However, this view is not tenable in light of numerous reports that constant heavy (CH) domains can affect binding affinity and specificity and V-region structure. Kinetic and thermodynamic proof for the occurrence of this phenomenon is now available. CH-region effects on affinity and specificity suggest new mechanisms for generating antibody diversity and polyreactivity (multispecificity) that impact current views on idiotype regulation, autoimmunity, and B cell selection and change our understanding of vaccine responses.

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The immunoglobulin constant region contributes to affinity and specificity

Abstract

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