HERV-W Envelope Peptide Domain Identification for ASCT Binding

Resolve Bottlenecks,
Find Innovative SolutionsGenerate Solutions

Solution Overview

Problem

The mechanisms of binding between the HERV-W envelope protein and ASCT receptors remain unclear, hindering the development of inhibitors to prevent retroviral entry, tumor propagation, and related diseases, as no specific domain for binding has been identified.

Innovation Solution

A peptide domain responsible for interactions between the HERV-W envelope protein and hASCT receptors is identified, defined by specific amino acid motifs, allowing for the recognition and inhibition of these interactions.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Measurement precision

If the mechanisms of binding between HERV-W envelope protein and ASCT receptors are studied using conventional methods, then general understanding of viral interaction is obtained, but specific binding domain identification remains unclear

Engineering Contradiction:

Improvebinding domain identificationVSAvoidbinding mechanism clarity

Core Design Contradiction:

Measurement precisionVSDifficulty of detecting and measuring

Solution Approach 1:

The envelope protein is divided into three distinct domains (N-terminal, central, and C-terminal) through systematic deletion and mutation analysis. This segmentation allows identification of the central domain as the specific binding region responsible for ASCT receptor interaction, resolving the ambiguity in binding mechanism

Inventive Principle:

Principle #1Segmentation

Solution Approach 2:

The invention identifies that specific local regions within the envelope protein (particularly the central domain with conserved amino acid sequences) possess unique binding properties. This local quality approach reveals that not the entire envelope protein but specific localized domains are responsible for high-affinity binding to ASCT receptors

Inventive Principle:

Principle #3Local quality

2Ease of manufacture

If no specific binding domain is identified, then development of inhibitors is hindered, but identifying the domain enables targeted therapeutic strategies

Engineering Contradiction:

Improveinhibitor developmentVSAvoidtherapeutic efficacy

Core Design Contradiction:

Ease of manufactureVSReliability

Solution Approach 1:

The central binding domain is extracted and isolated as a distinct functional unit from the complete envelope protein. This extracted domain can be used independently as a target for inhibitor design or as a diagnostic tool, facilitating drug development while maintaining therapeutic reliability through validated binding specificity

Inventive Principle:

Principle #2Taking out (Extraction)

Solution Approach 2:

The identified central domain serves as an intermediary structure that mediates between the envelope protein and ASCT receptors. By targeting this intermediary binding domain, inhibitors can effectively block viral entry without needing to interact with the entire envelope protein, simplifying drug design while ensuring reliable therapeutic effect

Inventive Principle:

Principle #24Intermediary (Mediator)

Data Source

PatentUS10040829B2Methods for producing peptides including HERV-W envelope motifs and for producing antibodies specific for the peptides

Publication Date: 2018.08.07 BIOMERIEUX SA

AI summary

A peptide domain necessary for an interaction between an envelope of a virus belonging to an HERV-W interference group and an hASCT receptor comprises (i) an N-terminus motif having an amino acid sequence selected from the group consisting of: SEQ ID No. 1 to SEQ ID No. 29, (ii) a C-terminus motif having an amino acid sequence selected from the group consisting of: SEQ ID No. 30 to SEQ ID No. 40, and (iii) at least one motif between the N-terminus and the C-terminus, and having an amino acid sequence selected from the group consisting of: SEQ ID No. 41, SEQ ID No. 42 and SEQ ID No. 73.