Document Type
Article
Publication Date
2-1-2025
Published In
Membranes
Abstract
The N-terminal ectodomain of the influenza A M2 protein is a target for universal influenza vaccine development and novel antiviral strategies. Despite the significance of this domain, it is poorly understood and most structural studies of the M2 protein have disregarded the N-terminal ectodomain in their analyses. Here, we report conformational properties and describe insights into the membrane topology of sites along the N-terminal ectodomain. Full-length M2 protein is embedded in lipid bilayer nanodiscs and studied using site-directed spin labeling electron paramagnetic resonance spectroscopy. Results are consistent with a turn in the middle of the ectodomain that changes in proximity to the membrane surface upon the addition of cholesterol or the antiviral drug rimantadine. Similarly to other domains of M2 protein, lineshape analysis suggests that the N-terminal ectodomain can adopt multiple conformations.
Keywords
influenza, M2 protein, ectodomain, spin labels, EPR, universal vaccine
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
Recommended Citation
Kyra C. Roeke and Kathleen P. Howard.
(2025).
"Conformation And Membrane Topology Of The N-Terminal Ectodomain Of Influenza A M2 Protein".
Membranes.
Volume 15,
Issue 2.
DOI: 10.3390/membranes15020040
https://works.swarthmore.edu/fac-chemistry/300
Comments
This work is freely available under a Creative Commons license.