Chemokines & SARS-CoV-2 Nucleocapsid Protein: Protein Domain Mapping Utilizing Octet^® BLI

Overview

Immunotherapy is a crucial strategy in fighting diseases like cancer, Alzheimer's, inflammatory diseases, and anti-viral responses. Manipulating and modulating the immune-system and its components is thereby a key strategy. Key strategies for drug development and therapy involve targeting immune regulators such as cytokines and chemokines (chemotactic cytokines; CHKs), their receptors (G protein coupled receptors; GPCRs) as well as modulating immune cells such as T-cells (CAR-T cell therapy), employing immune cell engagers (ICE) like bi- and tri-specific antibodies.

Characterization of protein domains participating in biomolecular interactions between antigens and key components of the innate immune system provides crucial insights for drug discovery, vaccine development and antigen cartography. Identifying and mapping these domains of interaction within a given protein can be challenging, laborious and time consuming. It requires the use of techniques such as alanine scanning, generation of escape mutants, and deep mutational scanning. The fluidic-free approach utilizing the Octet^® Bio-Layer Interferometry (BLI) platform  enables the rapid, label-free and high-throughput analysis of the interacting antigen domains and epitope diversity in real-time.

This application note discusses and comprehensively characterizes the interaction between the SARS-CoV-2 Nucleocapsid (N) protein (presented as the first secreted human coronavirus viral chemokine binding protein; vCBP) and human chemokines as a model for protein domain mapping of biomolecular interactions on the Octet^® BLI platform. It also provides guidance and considerations for assay development and optimization.

• Document type: Application Note
• Page count: 12 minutes
• Read time: 20 minutes

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