Title | Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains. |
Publication Type | Journal Article |
Year of Publication | 2001 |
Authors | Muyldermans, S., C. Cambillau, and L. Wyns |
Journal | Trends Biochem Sci |
Volume | 26 |
Issue | 4 |
Pagination | 230-5 |
Date Published | 2001 Apr |
ISSN | 0968-0004 |
Keywords | Amino Acid Sequence, Antigen-Antibody Reactions, Binding Sites, Antibody, Complementarity Determining Regions, Humans, Immunoglobulin Fragments, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid |
Abstract | The antigen-binding site of antibodies from vertebrates is formed by combining the variable domains of a heavy chain (VH) and a light chain (VL). However, antibodies from camels and llamas are an important exception to this in that their sera contain, in addition, a unique kind of antibody that is formed by heavy chains only. The antigen-binding site of these antibodies consists of one single domain, referred to as VHH. This article reviews the mutations and structural adaptations that have taken place to reshape a VH of a VH-VL pair into a single-domain VHH with retention of a sufficient variability. The VHH has a potent antigen-binding capacity and provides the advantage of interacting with novel epitopes that are inaccessible to conventional VH-VL pairs. |
Alternate Journal | Trends Biochem. Sci. |
PubMed ID | 11295555 |
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