Nanobody targeting SARS-CoV-2 S1 subunit for cost-effective neutralization
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Solution Overview
Problem
Current technologies lack effective solutions for targeting and neutralizing the SARS-CoV-2 virus, particularly in blocking its S protein S1 subunit, which is crucial for viral entry into host cells.
Innovation Solution
Development of a nanobody targeting the SARS-CoV-2 S protein S1 subunit, comprising a single domain antibody protein with a specific amino acid sequence, expressed using a prokaryotic expression vector, and purified to achieve high affinity and neutralization capabilities.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If traditional antibodies are used to target SARS-CoV-2, then neutralization capability is achieved, but production cost is high and immune response is easily triggered
Solution Approach 1:
The patent segments the antibody structure into a single-domain nanobody format, retaining only the essential antigen-binding variable domain (VH) while removing constant regions. This segmentation enables simplified production in prokaryotic systems, reducing manufacturing costs while maintaining neutralization capability against SARS-CoV-2
Solution Approach 2:
The nanobody is designed as a simplified, disposable therapeutic agent that can be produced cheaply in bacterial expression systems. The single-domain structure allows rapid production and regeneration, replacing expensive traditional antibodies with cost-effective nanobodies for SARS-CoV-2 treatment
2Reliability
If complex antibody structures are used, then binding affinity is high, but production complexity increases
Solution Approach 1:
The patent extracts the essential antigen-binding function from the complex full-length antibody structure, isolating only the variable domain (VH) as a standalone nanobody. This extraction maintains high binding affinity for SARS-CoV-2 while dramatically simplifying production to a single-domain protein that can be expressed in simple prokaryotic systems
Solution Approach 2:
The nanobody creates a simplified copy of the antibody's essential function using only the variable domain sequence. This copied structure retains the binding capability while eliminating the complex constant regions, enabling straightforward production and genetic engineering
3Reliability
If traditional vaccination approaches are used, then immune response is stimulated, but development time is extended
Solution Approach 1:
The patent uses the identified nanobody structure as a preliminary action platform for rapid vaccine and therapeutic development. The known single-domain sequence allows immediate cloning, expression, and testing, eliminating lengthy traditional antibody development timelines while maintaining effective SARS-CoV-2 neutralization
Applied Scientific Principles
This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.
Function Achieved in This Case
The nanobody effectively binds to the SARS-CoV-2 S protein S1 and S2 subunits, demonstrating strong binding signals and neutralizing activity, thereby inhibiting viral infection, with a purity of over 90% and proven ability to block SARS-CoV-2 from infecting cells.
Implementation Method 1
The nanobody effectively binds to the SARS-CoV-2 S protein S1 and S2 subunits, demonstrating strong binding signals and neutralizing activity
Data Source
AI summary
A nanobody and its application based on SARS-CoV-2 S protein S1 subunit are provided, and the present disclosure relates to biomedical technology. The present disclosure chooses the Spike RBD of SARS-CoV-2 as a target, and screens the nanobody targeting SARS-CoV-2 by using a nanobody library. After an ELISA test, the Spike RBD target of SARS-CoV-2 can be specifically identification while a SPIKE S1+S2 ECD target is identification, and a binding signal is relatively strong. The corresponding nanobody sequence is constructed into a prokaryotic expression vector for expression and purification to express the target nanobody successfully. After purification, the purity is greater than 90%. The ELISA test of VHH nanobody showed that the purified nanobody has higher affinity to the two targets.