Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Conserved Binding Sites

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...

Antibody Structure

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Antibody-lectin chimeras for glyco-immune checkpoint blockade.

Nature biotechnology·2025

Same author

Pulsed stimuli enable p53 phase resetting to synchronize single cells and modulate cell fate.

Molecular systems biology·2025

Same author

Inertial effect of cell state velocity on the quiescence-proliferation fate decision.

NPJ systems biology and applications·2024

Same author

Designing Multivalent and Multispecific Biologics.

Annual review of chemical and biomolecular engineering·2023

Same author

Pulsed stimuli entrain p53 to synchronize single cells and modulate cell-fate determination.

bioRxiv : the preprint server for biology·2023

Same author

Facile Display of Homomultivalent Proteins for <i>In Vitro</i> Selections.

ACS synthetic biology·2023

Search research articles

Related Experiment Video

Updated: Oct 11, 2025

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

Engineering a Minimal Leucine-rich Repeat IgG-binding Module.

George C Markou¹, Ayako Ohoka², Casim A Sarkar³

¹Department of Chemical Engineering and Materials Science, University of Minnesota, Minneapolis, MN, 55455, USA.

Applied Biochemistry and Biotechnology

|November 27, 2021

Summary

This summary is machine-generated.

Sea lamprey immunization discovered a novel leucine-rich repeat (LRR) protein binder. This binder specifically targets immunoglobulin G Fc domains, offering a new tool for biotechnology.

Keywords:

Immunization Leucine-rich repeat protein Ribosome display Sea lamprey

More Related Videos

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood

Published on: February 6, 2018

Protein Engineering by Yeast Surface Display

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

Related Experiment Videos

Last Updated: Oct 11, 2025

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood

Published on: February 6, 2018

Protein Engineering by Yeast Surface Display

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

Area of Science:

Biochemistry
Immunology
Protein Engineering

Background:

Sea lamprey immunization can generate leucine-rich repeat (LRR) protein binders, analogous to mammalian antibodies.
A novel minimal LRR protein was discovered using immunization with the human immunoglobulin G Fc domain (IgG Fc).

Purpose of the Study:

To characterize a novel LRR protein binder discovered through sea lamprey immunization.
To engineer a soluble and functional variant of the LRR protein for biotechnological applications.

Main Methods:

Sea lamprey immunization with human IgG Fc domain to discover novel LRR binders.
Cell-free ribosome display for analyzing the expression and binding properties of the LRR protein (VLRB.IgGFc).
Protein engineering to create a chimeric protein (Repe-VLRB.IgGFc) by combining a soluble LRR repebody with VLRB.IgGFc.

Main Results:

The novel LRR protein, VLRB.IgGFc, was found to specifically bind to the IgG Fc domain with minimal cross-reactivity to IgA or IgM using ribosome display.
Initial attempts to express VLRB.IgGFc in Escherichia coli were challenging, indicating solubility issues.
A soluble chimeric protein, Repe-VLRB.IgGFc, was successfully produced by combining VLRB.IgGFc with a known soluble LRR repebody.

Conclusions:

The minimal LRR protein VLRB.IgGFc is a specific binder of IgG Fc domains.
The modular architecture of LRR proteins allows for functional augmentation.
The engineered Repe-VLRB.IgGFc and its variants represent valuable tools for detecting, purifying, or targeting IgGs in biotechnology.