Our Research Activities
i. Generation of Single Domain Heavy Chain Antibodies
In our experience with dromedary camels >75% of their immunoglobulins are antibodies devoid of light chains. These heavy-chain antibodies (HcAbs) interact with only one single variable domain. Despite the absence of light chain, these homodimeric antibodies exhibit a broad antigen-binding repertoire by enlarging their hypervarible regions. Our current research seeks to compare the properties of conventional and HcAbs targeting the same antigens and derived from the same animal in terms of specificity, affinity and sensitivity. Heterohybridoma technology is being explored to immortalize these antibodies of interest.
ii. Generation of VHH fragments antibodies
Recombinant VHH domains (VHHs) are inherently thermostable and exhibit the antigen-binding capacity of the camelid original heavy-chain antibody. VHHs have also been shown to be extremely plastic and capable of quantitative refolding. Small size (14-17 Kda) and increased plasticity provide VHHs with unique diagnostic and therapeutic potential.
Our platform generates phage-displayed libraries of camel-derived VHH fragments, enriched for species that selectively bind to specific immunoregulatory receptors expressed on the cell membrane, as well as to intracellular moieties.
iii. Modulation of sequences of VHH fragment antibodies
Sequences of VHH fragments derived from our routine platforms are modified to facilitate successful intracellular delivery and greater ability to cross the blood-brain-barrier.
iv. Scale-up of VHH fragment antibody expression
Various expression systems are explored to arrive at the optimal method to produce significant quantities of VHH fragment antibody protein.