Ancient species offers contemporary therapeutics: an update on shark V<sub>NAR</sub> single domain antibody sequences, phage libraries and potential clinical applications. [PDF]
ABSTRACTThe antigen binding variable domain (VNAR) of the shark immunoglobulin new antigen receptor (IgNAR) evolved approximately 500 million years ago and it is one of the smallest antibody fragments in the animal kingdom with sizes of 12–15 kDa.
English H, Hong J, Ho M.
europepmc +4 more sources
Conventional monoclonal antibodies (mAbs) have been widely used in research and diagnostic applications due to their high affinity and specificity. However, multiple limitations, such as large size, complex structure and sensitivity to extreme ambient temperature potentially weaken the performance of mAbs in certain applications.
Cheong, Wei Shien +3 more
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A novel shark single-domain antibody targeting OGT as a tool for detection and intracellular localization [PDF]
IntroductionO-GlcNAcylation is a type of reversible post-translational modification on Ser/Thr residues of intracellular proteins in eukaryotic cells, which is generated by the sole O-GlcNAc transferase (OGT) and removed by O-GlcNAcase (OGA).
Xiaozhi Xi +21 more
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Organized B cell sites in cartilaginous fishes reveal the evolutionary foundation of germinal centers. [PDF]
The absence of germinal centers (GCs) in cartilaginous fishes lies at odds with data showing that nurse sharks can produce robust antigen-specific responses and affinity mature their B cell repertoires.
Matz H +8 more
europepmc +5 more sources
Improving the pharmacokinetic properties of biologics by fusion to an anti-HSA shark VNAR domain. [PDF]
Advances in recombinant antibody technology and protein engineering have provided the opportunity to reduce antibodies to their smallest binding domain components and have concomitantly driven the requirement for devising strategies to increase serum half-life to optimise drug exposure, thereby increasing therapeutic efficacy. In this study, we adopted
Müller MR +15 more
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Intraocular Penetration of a vNAR: In Vivo and In Vitro VEGF165 Neutralization
Variable new antigen receptor domain (vNAR) antibodies are novel, naturally occurring antibodies that can be isolated from naïve, immune or synthetic shark libraries. These molecules are very interesting to the biotechnology and pharmaceutical industries
Tanya A. Camacho-Villegas +6 more
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Shark IgNAR: The Next Broad Application Antibody in Clinical Diagnoses and Tumor Therapies? [PDF]
Antibodies represent a relatively mature detection means and serve as therapeutic drug carriers in the clinical diagnosis and treatment of cancer—among which monoclonal antibodies (mAbs) currently occupy a dominant position.
Xiaofeng Jiang +5 more
doaj +2 more sources
PLAbDab-nano: a database of camelid and shark nanobodies from patents and literature. [PDF]
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 ...
Gordon GL +7 more
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MOESM2 of Isolation and characterization of malaria PfHRP2 specific VNAR antibody fragments from immunized shark phage display library [PDF]
Additional file 2. Deduced amino acid sequences in hypervariable regions of VNAR clones targeting to three malaria biomarkers. The non-canonical cysteine residue is highlighted in red colour. This table also indicates the length of CDR3, number of cysteine residue, and type of IgNAR family for each clone.
Chiuan Leow +4 more
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The shark strikes twice: Generation of Mono- and Bispecific High-Affinity vNAR Antibody Domains via Step-Wise Affinity Maturation [PDF]
The aim of the work presented herein was the generation of high-affinity shark vNAR domains targeting different disease related antigens. For this, the natural IgNAR V domain repertoire of the bamboo shark (Chiloscyllium plagiosum) was analyzed and in analogy to these findings, a semi-synthetic complementarity determining region 3 (CDR3)-randomized ...
Zielonka, Stefan
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