Related Experiment Video

Updated: Jun 26, 2026

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
08:09

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

9.5K

Development of an ostrich-derived single-chain variable fragment (scFv) against PTPRN extracellular domain

Hamed Dabiri1, Majid Sadeghizadeh2, Vahab Ziaei3

  • 1Department of Genetics, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.

Scientific Reports
|February 14, 2024
PubMed

Insights

Researchers developed a novel ostrich-derived single-chain variable fragment (scFv) targeting Protein tyrosine phosphatase receptor N (PTPRN). This scFv shows promise for type 1 diabetes immunotherapy and diagnostics.

Area of Science:

  • Immunology
  • Biotechnology
  • Molecular Biology

Background:

  • Type 1 diabetes involves autoimmune destruction of pancreatic beta cells.
  • Targeted immunotherapy using monoclonal antibodies offers a potential treatment strategy.
  • Protein tyrosine phosphatase receptor N (PTPRN) is a key surface antigen candidate for beta cell targeting.

Purpose of the Study:

  • To develop a novel single-chain variable fragment (scFv) targeting the PTPRN extracellular domain.
  • To utilize an ostrich-derived phage display library for antibody development due to phylogenetic distance from mammals.
  • To create a potential tool for type 1 diabetes detection and therapy.

Main Methods:

  • Construction of an ostrich-derived scFv phage display library.
  • Biopanning techniques for enrichment and screening of anti-PTPRN binders.
  • Characterization of the selected scFv using ELISA, western blotting, and flow cytometry.

Main Results:

  • Successful isolation of an ostrich-derived scFv with high affinity and specificity for the PTPRN extracellular domain.
  • Demonstration of the scFv's binding capabilities through various biochemical assays.
  • Establishment of a novel antibody fragment for potential therapeutic and diagnostic applications.

Conclusions:

  • The developed anti-PTPRN scFv is a promising tool for antibody-based targeting systems.
  • This scFv can contribute to advancements in the detection and therapy of type 1 diabetes.
  • The use of phylogenetically distant hosts like ostriches can overcome challenges in antibody development for conserved targets.

More Related Videos

Production of Monoclonal Antibodies Targeting Aminopeptidase N in the Porcine Intestinal Mucosal Epithelium09:45

Production of Monoclonal Antibodies Targeting Aminopeptidase N in the Porcine Intestinal Mucosal Epithelium

Published on: May 18, 2021

2.0K
A "Plug-And-Display" Nanoparticle Vaccine Platform Based on Outer Membrane Vesicles Displaying SARS-CoV-2 Receptor-Binding Domain08:07

A "Plug-And-Display" Nanoparticle Vaccine Platform Based on Outer Membrane Vesicles Displaying SARS-CoV-2 Receptor-Binding Domain

Published on: July 25, 2022

2.6K

Related Concept Videos

Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Rab Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...