VLPT Protein Characterization for Ehrlichia Vaccine Development

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Solution Overview

Problem

Current methods lack effective characterization of the major immunoreactive protein VLPT in Ehrlichia chaffeensis, which is crucial for understanding host immune responses and developing protective immunity against human monocytotropic ehrlichiosis (HME).

Innovation Solution

Identification and characterization of the native 32-kDa VLPT protein, including localization of major antibody epitopes and determination of its molecular basis, using synthetic and recombinant polypeptides to define immunodeterminants and create immunogenic compositions for vaccine development.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Measurement precision

If current methods are used to study immunoreactive proteins, then research progress is limited, but characterization of VLPT protein remains incomplete

Engineering Contradiction:
Improvecharacterization precisionVSAvoidinformation completeness
Core Design Contradiction:
Measurement precisionVSLoss of information

Solution Approach 1:

The patent segments the VLPT protein into distinct functional domains (tandem repeats, ankyrin domains, signal sequences) and characterizes each separately using domain-specific methods, enabling comprehensive understanding of the protein's immunogenicity and molecular properties that cannot be achieved with conventional whole-protein analysis alone

Inventive Principle:
Principle #1Segmentation

Solution Approach 2:

The patent introduces recombinant protein fragments and domain-specific antibodies as intermediary tools to mediate between the complex VLPT protein and detection/characterization methods, allowing precise mapping of epitopes and functional regions without requiring complete structural elucidation of the entire protein

Inventive Principle:
Principle #24Intermediary (Mediator)

2Reliability

If comprehensive characterization of VLPT is pursued, then understanding of immune response improves, but research time and complexity increase

Engineering Contradiction:
Improveimmune response understandingVSAvoidresearch time
Core Design Contradiction:
ReliabilityVSLoss of time

Solution Approach 1:

The patent performs preliminary characterization of VLPT protein domains, epitopes, and immunogenic regions in advance through recombinant expression and domain mapping, creating a detailed molecular blueprint that accelerates subsequent vaccine development and immune response studies without requiring de novo analysis

Inventive Principle:
Principle #10Preliminary action

Solution Approach 2:

The patent focuses characterization efforts on specific immunologically relevant regions of VLPT (tandem repeats, ankyrin domains, signal sequences) rather than attempting uniform analysis of the entire protein, thereby obtaining critical immune response information more efficiently by concentrating resources on functionally important locales

Inventive Principle:
Principle #3Local quality

Data Source

PatentUS10131705B2Vaccines and diagnostics for the ehrlichioses
Publication Date: 2018.11.20 RES DEVMENT FOUND
  • US10131705B2 patent drawing
  • US10131705B2 patent drawing
  • US10131705B2 patent drawing

AI summary

The present invention concerns VLPT immunoreactive compositions for E. chaffeensis and compositions related thereto, including vaccines, antibodies, polypeptides, peptides, and polynucleotides. In particular, epitopes for E. chaffeensis VLPT are disclosed.