Multivalent Particle Compositions for High-Avidity Viral Neutralization
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Solution Overview
Problem
Existing technologies face challenges in achieving tight binding and effective neutralization of viral spike proteins, particularly those from viruses like SARS-CoV-1, SARS-CoV-2, and MERS-CoV, due to the limitations of soluble virus-capturing polypeptides.
Innovation Solution
Development of multivalent particles with virus-capturing polypeptides expressed at high valency and in oligomerized formats, forming multivalent interactions that provide tighter binding through avidity to viral spike proteins, utilizing fusion proteins with transmembrane and oligomerization domains.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If soluble virus-capturing polypeptides are used, then the binding to viral spike proteins is weak, but the neutralization effectiveness is insufficient
Solution Approach 1:
The invention divides the virus-capturing function into multiple discrete polypeptide units displayed on the particle surface, each capable of binding to viral spike proteins. This segmentation allows the system to achieve high avidity through multiple independent binding sites, resolving the contradiction between weak individual binding and insufficient neutralization effectiveness.
Solution Approach 2:
The invention merges multiple virus-capturing polypeptides onto a single particle surface, creating a multivalent display. This combination of multiple binding units on one particle enables simultaneous interaction with multiple viral spike proteins, transforming weak monovalent binding into strong multivalent neutralization.
2Reliability
If high valency display of virus-capturing polypeptides is achieved, then binding avidity increases, but particle complexity increases
Solution Approach 1:
The particle platform is designed to universally display multiple copies of the same virus-capturing polypeptide sequence, achieving high valency without requiring complex heterologous structures. This universal display mechanism simplifies particle construction while maintaining high binding avidity through repeated units.
Solution Approach 2:
The invention controls the valency parameter (number of displayed polypeptide copies) to optimize binding avidity. By adjusting the copy number parameter rather than changing fundamental particle structure, the system achieves high avidity with minimal increase in overall complexity.
3Productivity
If multiple copies of virus-capturing polypeptide are displayed on particle surface, then neutralization potency increases, but manufacturing precision requirements increase
Solution Approach 1:
The invention uses identical copies of the virus-capturing polypeptide sequence displayed multiple times on the particle surface. This copying strategy ensures that each unit has the same binding characteristics, simplifying manufacturing precision requirements compared to displaying diverse protein sequences with different functional requirements.
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 multivalent particles achieve enhanced binding and neutralization of viral spike proteins, effectively neutralizing viruses such as SARS-CoV-1, SARS-CoV-2, and MERS-CoV, with increased potency correlated to the copy number of displayed polypeptides on the particle surface.
Implementation Method 1
the displayed virus-capturing polypeptide forms multivalent interactions with a viral spike protein which provide tighter binding through avidity
Data Source
AI summary
Provided herein are multivalent particles and compositions of multivalent particles for blocking viral infection.