Human Intelectin Binding Microbial Glycans for Selective Detection
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Solution Overview
Problem
Current human lectins are unable to selectively recognize microbial glycans, as they interact with human glycans, making it difficult to distinguish between host and microbe, and there is a need for a method to identify and inhibit microbes effectively.
Innovation Solution
The use of human intelectin molecules, which can bind to specific microbial glycan molecules, such as those containing vicinal 1,2-diols, to detect and inhibit microorganisms like Streptococcus pneumonia and Cryptococcus neoformans, by conjugating them with antimicrobial agents or immune beacons, and creating fusion proteins with complement-activating peptides.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Measurement precision
If human lectins are used to recognize glycans, then glycan recognition capability is achieved, but selectivity between host and microbe is lost due to interaction with human glycans
Solution Approach 1:
The patent applies local quality by engineering lectins with modified binding properties that specifically recognize microbial glycan structures (such as beta-galactofuranose and KDO) while maintaining non-reactivity toward human glycans. This selective local binding capability allows the lectin to distinguish between host and microbial cells, resolving the contradiction between achieving glycan recognition and avoiding false positive binding to human glycans.
2Measurement precision
If lectins are designed to bind microbial glycans specifically, then detection accuracy improves, but the complexity of identifying suitable lectin targets increases
Solution Approach 1:
The patent employs parameter changes by modifying lectin molecular structures to alter their binding specificity toward microbial glycans. By changing parameters such as carbohydrate recognition domain structure and binding affinity, the invention achieves high detection accuracy for microbes while systematically identifying suitable lectin targets through rational design rather than complex screening processes.
3Adaptability or versatility
If human lectins interact with human glycans, then host cell recognition is achieved, but microbial detection capability is compromised
Solution Approach 1:
The patent applies segmentation by separating the functions of host cell recognition and microbial detection into distinct molecular entities. Human lectins are engineered or selected to specifically bind microbial glycans without interacting with human glycans, while host cell recognition functions are handled by other components of the immune system. This functional segmentation resolves the contradiction between maintaining host cell recognition capability and achieving accurate microbial detection.
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
This approach allows for specific detection and inhibition of microorganisms, avoiding false positives with human glycans and providing a targeted method to combat bacterial and fungal infections.
Implementation Method 1
intelectins are a newly discovered class of animal lectins not similar to known C-type lectins (Drickamer, 1993), but nevertheless in many cases having been shown to bind carbohydrates in a calcium-dependent manner
Implementation Method 2
The human intelectin may bind to a β-linked D-galactofuranose residue, a glycan containing a heptose, D-glycero-D-talo-oct-2-ulosonic acid (KO) and/or 3-deoxy-D-manno-oct-2-ulosonic acid (KDO) residue
Data Source
AI summary
The present disclosure provides for methods of diagnosing and treating bacterial infections. Human Intelectin 1 (hIntL-1) has been shown to bind selectively to glycan components on bacteria including Streptococcus pneumonia, Proteus mirabilis, Proteus vulgaris, Klebsiella pneumonia and Yersinia pestis. This interaction can be targeted to identify, purify and therapeutically target such organisms.