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Author Spotlight: Advancements in DNA Nanosensors – Addressing Sensitivity and Selectivity Challenges in Molecular Detection

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Targeting NETs using dual-active DNase1 variants.

Hanna Englert¹, Josephine Göbel¹, Danika Khong¹

¹Institute of Clinical Chemistry and Laboratory Medicine, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.

Frontiers in Immunology

|June 8, 2023

Summary

This summary is machine-generated.

Engineered a dual-acting DNase enzyme combining DNase1 and DNase1L3 activities to effectively degrade Neutrophil Extracellular Traps (NETs). This dual-active DNase shows promise for treating thromboinflammatory diseases by neutralizing DNA and NETs.

Keywords:

DNase1 DNase1-like 3 NET degradation NETosis neutrophil extracellular traps (NETs)protein engineering recombinant proteins thromboinflammation

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Area of Science:

Biochemistry
Molecular Biology
Immunology

Background:

Neutrophil Extracellular Traps (NETs) are implicated in various diseases due to impaired clearance.
Efficient NET degradation relies on DNase1 and DNase1-like 3 (DNase1L3) enzymes.

Purpose of the Study:

To engineer a dual-active DNase with combined DNase1 and DNase1L3 functions.
To evaluate the NET-degrading potential of the engineered enzyme.

Main Methods:

Engineered a dual-active DNase by substituting DNase1 amino acid stretches with DNase1L3 sequences.
Produced transgenic mice expressing the dual-active DNase.
Assessed enzyme activity in mouse body fluids.

Main Results:

Identified key DNase1L3 regions for chromatin degradation.
Created a dual-active DNase1 mutant superior to native enzymes in degrading dsDNA and chromatin.
Demonstrated stability and circulation of the mutant enzyme in vivo.

Conclusions:

The dual-active DNase1 mutant effectively degrades dsDNA and chromatin.
This engineered enzyme is a potential therapeutic agent for thromboinflammatory diseases.