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Related Experiment Video

Updated: May 14, 2026

TransFLP — A Method to Genetically Modify Vibrio cholerae Based on Natural Transformation and FLP-recombination

TransFLP — A Method to Genetically Modify Vibrio cholerae Based on Natural Transformation and FLP-recombination

Published on: October 8, 2012

Engineered Coiled-Coils Convert Cholera Toxin B-Pentamers into Programmable Membrane Fusogens.

Wenyue Dai^1,2, Erik Kempmann^3,4, Francesca Rosato^3,4

¹School of Chemistry, University of Leeds, Leeds LS2 9JT, U.K.

|May 13, 2026

Summary

This summary is machine-generated.

Researchers engineered cholera toxin B-subunit (CTB) into a programmable membrane fusogen. Linker length, not coiled-coil orientation, determined fusion efficiency, offering a new strategy for bioengineering membrane fusion.

Keywords:

coiled-coil protein engineering lectin−glycolipid interactions membrane fusion nanobiotechnology programmable biointerfaces synthetic fusogens

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TransFLP — A Method to Genetically Modify Vibrio cholerae Based on Natural Transformation and FLP-recombination

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Engineering Cell-permeable Protein

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Published on: December 28, 2009

Area of Science:

Biochemistry
Bioengineering
Molecular Biology

Background:

Membrane fusion is crucial for biological processes and bioengineering applications.
Limited design principles exist for programming protein-driven membrane fusion at specific interfaces.

Purpose of the Study:

To re-engineer the cholera toxin B-subunit (CTB) into a programmable membrane fusogen.
To investigate the role of linker architecture and length in CTB-mediated membrane fusion.

Main Methods:

CTB was engineered into dimers using coiled-coil linkers with defined parallel and antiparallel architectures.
Fusion of giant unilamellar vesicles (GUVs) was assessed using FRET-based lipid mixing assays.
Mechanistic insights were gained through flow cytometry, confocal microscopy, and QCM-D.

Main Results:

Both parallel and antiparallel CTB dimers induced membrane cross-linking and full fusion.
Fusogenic efficiency was primarily dictated by the length of the CTA2 linker, not the coiled-coil orientation.
A generalizable strategy for engineering tunable lectin-based fusogens was established.

Conclusions:

Linker geometry is a key design parameter for engineering fusogenic proteins.
This work advances programmable membrane fusion platforms for applications like drug delivery and synthetic cells.