Abstract

Nanobodies are antibody-derived therapeutic proteins that contain the unique structural and functional properties of naturally occurring heavy-chain antibodies. The Nanobody technology was originally developed following the discovery thatcamelidae (camels and llamas) possess fully functional antibodies that lack light chains. These heavy-chain antibodies contain a single variable domain (VHH) and two constant domains (CH₂ and CH₃). Importantly, the cloned and isolated VHH domain is a perfectly stable polypeptide harboring the full antigen-binding capacity of the original heavy-chain antibody. These newly discovered VHH domains with their unique structural and functional properties form the basis of a new generation of therapeutic antibodies which were named Nanobodies. The aim of this paper is to show the properties of Nanobodies, their production and expression, applications and their clinical status.

Key words: Nanobodies, camelidae, antibody engineering, Nanoclone.

Abbreviation

Abbreviations: HcAb’s, Heavy-chain antibodies; VHH, variable domain of heavy-chain antibody; mAbs, monoclonal antibodies; FDA, food and drug administration;Fab, fragment-antigen binding; Fc, fragment crystalline; scFv, single-chain variable fragment; V_H, variable domain of the heavy chain; V_L, variable domain of the light chain; IgG, immunoglobulin class G; V-NAR, variable region of new or nurse shark antigen receptor; Ag, antigen; CDR, complementarity-determining regions; CH,constant heavy domain; CEA, carcinoembryonic antigen; PSA, prostate-specific antigen; EGFR, epidermal growth factor receptor; Aah, Androctonus autralis hectorscorpion; SPECT, single photon emission computed tomography; TNFα, tumour necrosis factor; NCC, neurocysticercosis and  DARPins, designed ankyrin repeat proteins.