Antibody with high affinity and specificity to antigen has widely used as a tool to combat various diseases. The variable domain of immunoglobulin new antigen receptor (VNAR) naturally found in shark contains autonomous function as single-domain antibody. Due to its excellent characteristics, the small, non-complex, and highly stable have made shark VNAR can acquires the antigen-binding capability that might not be reached by conventional antibody. Phage display technology enables shark VNAR to be presented on the surface of phage, allowing the exploration of shark VNAR as an alternative antibody format to target antigens from various infectious diseases. The application of phage-displayed shark VNAR in antibody library and biopanning eventually leads to the discovery and isolation of antigen-specific VNARs with diagnostic and therapeutic potential towards infectious diseases. This review provides an overview of the shark VNAR antibody, the types of phage display technology with comparison to the other types of display system, as well as the application and case studies of phage-displayed shark VNAR antibodies against infectious diseases.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.fsi.2023.108986 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Characteristics and Genomic Localization of Nurse Shark () IgNAR.
Int J Mol Sci
November 2024
School of Life Sciences, Central South University, Changsha 410031, China.
The variable domain of IgNAR shows great potential in biological medicine and therapy. IgNAR has been discovered in sharks and rays, with the nurse shark () IgNARs being the most extensively studied among sharks. Despite being identified in nurse sharks over 30 years ago, the characteristics and genomic localization of IgNAR remain poorly defined, with significant gaps even in the latest released genome data.
View Article and Find Full Text PDFA novel shark VNAR antibody-based immunotoxin targeting TROP-2 for cancer therapy.
Acta Pharm Sin B
November 2024
College of Marine Science and Biological Engineering, Qingdao University of Science and Technology, Qingdao 266042, China.
Article Synopsis
- - TROP-2, a protein linked to various types of cancer, is a potential target for new cancer treatments, specifically antibody-drug conjugates (ADCs), but their effectiveness against solid tumors is limited due to issues like poor penetration.
- - Researchers developed a small, stable immunotoxin using a shark-derived antibody known as VNAR, which has better tissue penetration properties than traditional antibodies.
- - The study identified a specific VNAR, called VNAR-5G8, which binds effectively to TROP-2 and created a recombinant immunotoxin (5G8-PE38) that showed strong anti-tumor activity, suggesting its potential as a cancer therapy option.
PLAbDab-nano: a database of camelid and shark nanobodies from patents and literature.
Nucleic Acids Res
January 2025
Department of Statistics, University of Oxford, 24-29 St Giles', Oxford, OX1 3LB, UK.
Nanobodies are essential proteins of the adaptive immune systems of camelid and shark species, complementing conventional antibodies. Properties such as their relatively small size, solubility and high thermostability make VHH (variable heavy domain of the heavy chain) and VNAR (variable new antigen receptor) modalities a promising therapeutic format and a valuable resource for a wide range of biological applications. The volume of academic literature and patents related to nanobodies has risen significantly over the past decade.
View Article and Find Full Text PDFH, C and N resonance assignments of a shark variable new antigen receptor against hyaluronan synthase.
Biomol NMR Assign
December 2024
CAS and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Center for Ocean Mega-Science, Chinese Academy of Sciences, Qingdao, China.
Single domain antibody (sdAb) is only composed of a variable domain of the heavy-chain-only antibody, which is devoid of light chain and naturally occurring in camelids and cartilaginous fishes. Variable New Antigen Receptor (VNAR), a type of single domain antibody present in cartilaginous fishes such as sharks, is the smallest functional antigen-binding fragment found in nature. The unique features, including flexible paratope, high solubility and outstanding stability make VNAR a promising prospect in antibody drug development and structural biology research.
View Article and Find Full Text PDFShark anti-idiotypic variable new antigen receptor specific for an alpaca nanobody: Exploration of a nontoxic substitute to ochratoxin A in immunoassay.
J Hazard Mater
September 2024
School of Food Science and Engineering, Hainan University, Haikou 570228, China. Electronic address:
Nontoxic substitutes to mycotoxins can facilitate the development of eco-friendly immunoassays. To explore a novel nontoxic substitute to ochratoxin A (OTA), this study screened shark anti-idiotypic variable new antigen receptors (VNARs) against the alpaca anti-OTA nanobody Nb28 through phage display. After four rounds of biopanning of a naïve VNAR phage display library derived from six adult Chiloscyllium plagiosum sharks, one positive clone, namely, P-3, was validated through a phage enzyme-linked immunosorbent assay (phage ELISA).
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!