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Updated: May 10, 2026

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay

Published on: October 20, 2018

In vitro O-antigen ligase assay.

Xiang Ruan¹, Miguel A Valvano

¹Department of Microbiology and Immunology, Centre for Human Immunology, University of Western Ontario, London, ON, Canada.

Methods in Molecular Biology (Clifton, N.J.)

|June 15, 2013

Summary

We developed an in vitro assay for WaaL, a key enzyme in lipopolysaccharide synthesis. This assay enables the study of the crucial glycosidic bonding reaction using native substrates.

Area of Science:

Biochemistry
Molecular Biology
Enzymology

Background:

Lipopolysaccharide (LPS) synthesis is essential for bacterial outer membrane integrity.
The WaaL enzyme plays a critical role in LPS biosynthesis by catalyzing a key ligation step.
Understanding LPS synthesis is vital for developing novel antibacterial strategies.

Purpose of the Study:

To develop and validate an in vitro assay for the WaaL enzyme.
To facilitate the study of the WaaL-catalyzed glycosidic bond formation.
To enable biochemical characterization of LPS ligation.

Main Methods:

Utilized native substrates for the WaaL ligation reaction.
Established an in vitro assay system for enzymatic activity measurement.

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Characterized the glycosidic bond formation catalyzed by WaaL.

Main Results:

Successfully reconstituted the WaaL-catalyzed ligation reaction in vitro.
Demonstrated the enzyme's ability to form glycosidic bonds between O-antigen and lipid A-core oligosaccharide.
Validated the use of native substrates for assay development.

Conclusions:

The developed in vitro assay provides a robust tool for studying WaaL function.
This assay will aid in understanding the mechanisms of LPS synthesis.
Further research can utilize this system to investigate WaaL inhibitors or variants.