Abstract
Shark is a cartilaginous fish that produces new antigen receptor (IgNAR) antibodies. This antibody is identified with a similar human heavy chain but dissimilar sequences. The variable domain (VNAR) of IgNAR is stable and small in size, these features are desirable for drug discovery. Previous study results revealed the effectiveness of VNAR as a single molecule or a combination molecule to treat diseases both in vivo and in vitro with promising clinical applications. We showed the first evidence of IgNAR alternative splicing from spotted bamboo shark (Chiloscyllium plagiosum), broadening our understanding of the IgNARs characteristics. In this review, we summarize the discoveries on IgNAR with a focus on its advantages for therapeutic development based on its peculiar biochemistry and molecular structure. Proper applications of IgNAR will provide a novel avenue to understand its special presence in cartilaginous fishes as well as designing a number of drugs for undefeated diseases.
Highlights
Most conventional antibodies (IgG) are heterodimers (Figure 1A) with two heavy chains (VHs) and two light chains (VLs) [1]
The unique features of VNAR may be useful for drug discovery; the isolated VNAR called V13 produced using phage display to select against a human recombinant vascular endothelial growth factor (VEGF165) cytokine was isolated from an immunized Heterodontus francisci shark
They founded this V13 VNAR penetrated the cornea without the need for an injection and without causing ocular surface abrasions or signs of discomfort in an animal model (probtures of VNAR may be useful for drug discovery; the isolated VNAR called V13 produced using phage display to select against a human recombinant vascular endothelial growth factor (VEGF165) cytokine was isolated from an immunized Heterodontus francisci shark
Summary
Most conventional antibodies (IgG) are heterodimers (Figure 1A) with two heavy chains (VHs) and two light chains (VLs) [1]. IgGs are distributed into antigen-binding fragment (Fab) and Fragment-crystallizable (Fc) portion. Fab portion contains one constant domain of the heavy chain (C1) and one constant domain of the light chain (CL), as well as one variable domain of heavy chain (VH) and one variable domain of light chain (VL). The variable domain of each chain is responsible for antigen interactions due to the existence of paratope (the antigen-binding site) [1,2]. The variable domains of IgG are linked by a flexible peptide into an antiparallel sheet (Figure 1A). The characteristic flexibility of the IgG is characterized by the hinge region in the middle part of the heavy chain [6].
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