Format

Send to

Choose Destination
Trends Biochem Sci. 2001 Apr;26(4):230-5.

Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains.

Author information

1
Vrije Universiteit Brussel, Vlaams Interuniversitair Instituut Biotechnologie, 65, B-1640 Sint Genesius Rode, Paardenstraat, Belgium. svmuylde@vub.ac.be

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.

PMID:
11295555
DOI:
10.1016/s0968-0004(01)01790-x
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center