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Antibody repertoire development in camelids

2005; Elsevier BV; Volume: 30; Issue: 1-2 Linguagem: Inglês

10.1016/j.dci.2005.06.010

1879-0089

Erwin De Genst, Dirk Saerens, Serge Muyldermans, Katja Conrath,

Glycosylation and Glycoproteins Research

The humoral immune response of the Camelidae is unique as these animals are the only known mammals that seem to possess functional homodimeric heavy-chain antibodies besides the classical heteromeric antibodies composed of heavy (H) and light (L) chains. By definition, the heavy-chain antibodies lack the L-chain, and it was noticed that their H-chain is devoid of the typical first constant domain (CH1) and contains a dedicated variable domain, referred to as VHH. The VHH exon is assembled from separate V–D–J gene segments. The recombined VHH region is subjected to somatic hypermutations; however, the timing and actual mechanism of the class switch from μ to the dedicated γ-isotype remains elusive. Interestingly, antigen-specific VHHs are easily retrieved after panning of a phage-displayed rearranged V-gene pool cloned from an immunised camelid. These single-domain antigen binding entities possess a number of biophysical properties that offer particular advantages in various medical and biotechnological applications.