Solid-State NMR of Virus Membrane Proteins
Name
nihms-2083901.pdf
Description
Accepted version
Size
2.22 MB
Format
Adobe PDF
Checksum (MD5)
e5c38daf59754d553a5ca2da2143956d
Author(s)
Hong, Mei
Date Issued
February 18, 2025
Journal
Accounts of Chemical Research
Publisher
American Chemical Society
Citation
Solid-State NMR of Virus Membrane Proteins. Mei Hong. Accounts of Chemical Research 2025 58 (6), 847-860.
Version
Author's final manuscript
Abstract
This review provides a personal account of my laboratory’s virus membrane protein research. The focus is on viroporins, multifunctional proteins that conduct ions and mediate virus budding to sustain the virus lifecycle and cause pathogenicity to cells. Using solid-state NMR spectroscopy, we have investigated in detail the structure, dynamics, mechanism of action of influenza M2 proton channels. Since 2020, we have determined the atomic structures of the SARS-CoV-2 E protein, from which we are obtaining mechanistic knowledge about this coronavirus ion channel. Using solid-state NMR experiments that measure protein-ligand contacts, we discovered how M2 complexes with cholesterol to cause membrane curvature. These studies of viroporins are enriched by our investigation of other membrane proteins in infectious diseases, including antimicrobial peptides, viral fusion proteins, and bacterial transporters. In reviewing our major findings, I will describe the interesting unanticipated events that led to some of the successful experiments. Discoveries often cannot be planned but come by serendipity. By sharing these experiences, I hope to encourage students to follow their curiosity and embrace the exploration of uncharted scientific territory.
Terms of Use
Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1021/acs.accounts.4c00800
