Plant-Derived MoMo30 Protein for Broad-Spectrum Viral Entry Blocking

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Solution Overview

Problem

There is a need for broad spectrum antimicrobial agents that can effectively bind and neutralize microorganisms, particularly viruses, by mimicking the properties of lectins to inhibit viral entry and stimulate host immune responses.

Innovation Solution

A plant-derived MoMo30 protein with a specific amino acid sequence, derived from the Momordica genus, is used in compositions and methods to inhibit viral infections by blocking viral entry into host cells and stimulating a neutralizing antibody response, with properties including high heat stability and mannose-sensitive binding.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Adaptability or versatility

If conventional antimicrobial agents are used, then specific viral infections may be treated, but broad spectrum antiviral activity is not achieved

Engineering Contradiction:
Improvebroad spectrum antiviral activityVSAvoideffectiveness against specific viruses
Core Design Contradiction:
Adaptability or versatilityVSReliability

Solution Approach 1:

The patent applies universality by designing a lectin-based antiviral agent that can bind to mannose residues on multiple different viral surfaces simultaneously. The MoMo30 protein exhibits broad-spectrum antiviral activity against diverse viruses including HIV, Ebola, influenza, and coronaviruses, while maintaining reliable inhibition through its specific carbohydrate-binding capability. This multi-functional approach allows a single agent to address multiple viral threats without sacrificing effectiveness.

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

2Reliability

If lectin proteins are used to bind viral glycans, then viral entry is inhibited, but the complexity of identifying effective lectins increases

Engineering Contradiction:
Improveviral entry inhibitionVSAvoidlectin identification process
Core Design Contradiction:
ReliabilityVSDevice complexity

Solution Approach 1:

The patent applies copying by utilizing the naturally occurring MoMo30 lectin protein from plant sources that has already evolved the required binding specificity. Instead of synthesizing or screening numerous artificial lectin variants, the invention copies the effective carbohydrate-binding structure from nature. This approach simplifies the identification process while maintaining reliable viral entry inhibition through the protein's inherent mannose-binding capability.

Inventive Principle:
Principle #26Copying

3Reliability

If heat-sensitive lectin proteins are used, then antiviral activity is maintained, but stability and shelf life are reduced

Engineering Contradiction:
Improveantiviral activityVSAvoidheat stability
Core Design Contradiction:
ReliabilityVSStability of the object's composition

Solution Approach 1:

The patent applies parameter changes by optimizing the lectin protein's structural properties to enhance thermal stability while preserving antiviral function. The MoMo30 protein has been characterized and formulated with specific amino acid compositions and structural features that confer heat resistance. This allows the protein to maintain its carbohydrate-binding capability and antiviral activity across a broader temperature range, improving stability and shelf life without sacrificing reliability.

Inventive Principle:
Principle #35Parameter changes

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

MoMo30 protein effectively inhibits a range of viruses, including HIV and Ebola, by forming stable complexes and inducing a broadly neutralizing antibody response, reducing viral loads and increasing CD4+ lymphocyte counts in treated patients.

Implementation Method 1

Lectin proteins are sugar-binding proteins that bind specifically and reversibly to carbohydrate groups. The MoMo30 protein binds HIV gp120 in a manner that is sensitive to mannose, indicating carbohydrate-mediated binding.

Methodology Applied
Scientific EffectLectin-carbohydrate binding: Adsorption

Implementation Method 2

These roles are mediated by specific multivalent interactions between cell surfaces decorated by complex glycans and their cognate protein lectins. The MoMo30 protein effectively inhibits a range of viruses by forming stable complexes.

Methodology Applied
Scientific EffectMultivalent binding:

Data Source

PatentUS12453752B2Hevamine-related plant compositions and methods
Publication Date: 2025.10.28 MOREHOUSE SCHOOL OF MEDICINE
  • US12453752B2 patent drawing
  • US12453752B2 patent drawing
  • US12453752B2 patent drawing

AI summary

The present application relates to a compositions and methods comprising or expressing a hevamine A-related MoMo30 protein from Momordica balsamina. The MoMo30 protein is about 30 kDa in size, is stable after being autoclaved at 120° C. for 30 min, resists proteolytic cleavage by trypsin, exhibits mannose-sensitive binding to HIV gp120, exhibits hemagglutinin and chitinase activity, is capable of activating and stimulating T cell proliferation, is capable of preventing infection by HIV-1 or alleviating symptoms in an HIV-1 infected patients, and comprises an amino acid sequence of SEQ ID NO: 4. The MoMo30 protein and/or a nucleic acid encoding the same may be used in methods for preventing or treating microbial infections by HIV, SARS-CoV-2 and other enveloped viruses, as well as other microorganisms comprising cell surface proteins containing glycan residues, such as mannose.