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  Afr. J. Biotechnol.

  Vol. 8 No. 12

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  Deffar K
  Zhu X

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African Journal of Biotechnology Vol. 8 (12), pp. 2645-2652, 17 June 2009

ISSN 1684-5315  © 2009 Academic Journals  

 

 

Review

 

Nanobodies - the new concept in antibody engineering

 

Khalissa Deffar1,2, Hengliang Shi1, Liang Li1, Xingzhi Wang1 and Xiaojuan Zhu1*

 

1Institute of Genetics and Cytology, Northeast Normal University, Key Laboratory of Molecular Epigenetics of Ministry of Education, Changchun, 130024, P. R. China.

2Faculty of Science, Department of Biology, Ferhat Abbas University, Setif, 19000, Algeria.

 

*Corresponding author. E-mail: zhuxj720@nenu.edu.cn. Tel: +86-431-85099769.

 

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; VH, variable domain of the heavy chain; VL, 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 hector scorpion; SPECT, single photon emission computed tomography; TNFα, tumour necrosis factor; NCC, neurocysticercosis and  DARPins, designed ankyrin repeat proteins.

 

Accepted 21 April, 2009

 
   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 that camelidae (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.

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