CX/HY Glycan-Binding Lectin for Broad-Spectrum Influenza Neutralization

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Solution Overview

Problem

Current influenza antiviral agents are limited in their effectiveness against rapidly mutating strains, and there is a need for broad-spectrum antiviral therapies that can combat multiple influenza virus strains, particularly those with high pathogenicity like H1N1, H5N1, and H7N9, and address the unpredictability in viral evolution.

Innovation Solution

A CX/HY-type binding lectin, such as Lablab purpureus Flt3 receptor interacting lectin (FRIL), is administered to target CX-type and HY-type glycans on influenza viruses, neutralizing multiple strains by binding to specific glycan structures on the virus envelope.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Adaptability or versatility

If current influenza antiviral agents (neuraminidase inhibitors and M2 ion channel protein inhibitors) are used, then treatment of specific influenza strains is effective, but broad-spectrum activity against multiple rapidly mutating strains is limited

Engineering Contradiction:
Improvebroad-spectrum antiviral activityVSAvoideffectiveness against rapidly mutating strains
Core Design Contradiction:
Adaptability or versatilityVSReliability

Solution Approach 1:

The lectin is designed to bind to a universal glycan structure (complex-type or hybrid-type N-glycans with trimannosyl core) that is conserved across multiple influenza virus strains including H1N1, H5N1, H3N2, and H7N9. This universal binding target allows a single agent to neutralize diverse viral strains that would otherwise require different specific antivirals, achieving broad-spectrum activity while maintaining reliability through targeting of conserved viral glycoproteins

Inventive Principle:
Principle #6Universality (Multi-functionality)

Solution Approach 2:

The invention changes the target parameter from strain-specific viral proteins (neuraminidase, M2 ion channel) to a conserved glycan structure (complex-type or hybrid-type N-glycans) on viral envelope proteins. This parameter change enables the lectin to recognize and bind to multiple influenza strains regardless of their protein sequence variations, thereby achieving broad-spectrum activity against rapidly mutating strains

Inventive Principle:
Principle #35Parameter changes

2Reliability

If vaccines targeting specific seasonal viral strains are used, then protection against those specific strains is achieved, but protection against unpredictably evolving strains is insufficient

Engineering Contradiction:
Improveprotection against specific seasonal strainsVSAvoidprotection against unpredictably evolving strains
Core Design Contradiction:
ReliabilityVSAdaptability or versatility

Solution Approach 1:

The lectin provides preliminary neutralization of influenza viruses by binding to conserved glycan structures on viral envelope proteins before the virus can infect cells. This preliminary action occurs regardless of the specific viral strain, providing immediate broad-spectrum protection that does not depend on prior exposure to specific seasonal strains or their evolution

Inventive Principle:
Principle #10Preliminary action

Solution Approach 2:

By targeting the universal complex-type or hybrid-type N-glycan structure present on multiple influenza virus strains, the lectin functions as a universal antiviral agent that can protect against both known seasonal strains and unpredictably evolving strains, overcoming the limitations of strain-specific vaccines

Inventive Principle:
Principle #6Universality (Multi-functionality)

3Ease of operation

If high mannose-type binding lectins are used, then binding to mannose residues occurs, but specific binding to CX-type and HY-type glycans with trimannosyl core is not achieved

Engineering Contradiction:
Improvebinding to mannose residuesVSAvoidspecificity to CX-type and HY-type glycans
Core Design Contradiction:
Ease of operationVSMeasurement precision

Solution Approach 1:

The lectin is engineered with specific binding sites that recognize the local structural features of complex-type or hybrid-type N-glycans, particularly the trimannosyl core structure with specific antenna configurations. This local quality matching between the lectin binding site and the specific glycan structure enables high-specificity binding to CX-type and HY-type glycans while excluding high mannose-type glycans, achieving both ease of binding and measurement precision

Inventive Principle:
Principle #3Local quality

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 CX/HY-type lectin demonstrates broad-spectrum antiviral activity, effectively neutralizing various influenza virus strains, including H1N1, H5N1, and H7N9, and can be administered via multiple routes to prevent or treat influenza infections.

Implementation Method 1

a CX/HY-type binding lectin as described herein is capable of specifically binds to a CX-type glycan and/or a HY-type glycan on influenza virus

Methodology Applied
Scientific EffectLectin-glycan binding: Adsorption

Data Source

PatentUS12576134B2Antiviral lectin and uses thereof
Publication Date: 2026.03.17 ACAD SINICA
  • US12576134B2 patent drawing
  • US12576134B2 patent drawing
  • US12576134B2 patent drawing

AI summary

The present invention relates to antiviral lectin and uses thereof. Particularly, the present invention relates to a complex-type (CX-type) and/or hybrid-type (HY-type) glycan binding lectin for use in treating or preventing influenza virus infection. The present invention also provides a method for treating or preventing influenza virus infection by administrating to a subject in need said lectin or a composition comprising the same.