Critical Reviews™ in Immunology

ISSN for PRINT: 1040-8401

For Online Access

Best Paper Award Selection - Editorial Board Site

2006, Volume26

Issue 5

102 pages

Issue price - $142.00

Marianne Bruggemann
Laboratory of Developmental Immunology, The Babraham Institute, Babraham, Cambridge CB2 4AT, UK

Jennifer A. Smith
Laboratory of Developmental Immunology, The Babraham Institute, Babraham, Cambridge CB2 4AT, UK

Michael J. Osborn
Laboratory of Developmental Immunology, The Babraham Institute, Babraham, Cambridge CB2 4AT, UK

Daniel Corcos
Laboratory of Developmental Immunology, The Babraham Institute, Babraham, Cambridge CB2 4AT, UK

Xiangang Zou
Laboratory of Developmental Immunology, The Babraham Institute, Babraham, Cambridge CB2 4AT, UK

Viet Khong Nguyen
Department of Cellular and Molecular Interactions, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Belgium

Serge Muyldermans
Department of Cellular and Molecular Interactions, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Belgium

Antibodies expressed in mice, humans, and most mammals consist of paired heavy (H) and light (L) chains. Cellular release of single H-chains without L-chains is prevented by chaperone association and retention in the endoplasmic reticulum. Consequently, H-chain-only antibodies are absent, except in pathological conditions known as Heavy Chain Disease, where they occur in mutated form. An exception to this is found in the serum of Camelidae. Homodimeric H-chain antibodies in camelids lack the first constant region domain (CH1) of the H-chain but retain an otherwise intact H-chain polypeptide, thus maintaining antigen specificity and effector functions. In this review, we summarize how H-chain antibodies can be expressed in mice, and whether normal developmental processes leading to antibody expression without L-chain are retained.

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