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Related Concept Videos

Introduction to Virus01:28

Introduction to Virus

Viruses are unique biological entities that blur the boundary between living and non-living systems. Although they lack cellular structure and metabolic processes, they can exhibit characteristics of life when infecting a host. Their defining feature is a nucleic acid core, composed of either DNA or RNA, encapsulated within a protein coat called a capsid. This simple structure allows them to invade host cells and use their machinery for replication efficiently.Viral Structure and...

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Solid-State NMR of Virus Membrane Proteins.

Mei Hong1

  • 1Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.

Accounts of Chemical Research
|February 28, 2025
PubMed
Summary

Solid-state NMR reveals the mechanism of proton transport by influenza M2 and SARS-CoV-2 E viroporins. These studies elucidate drug binding sites and viral budding mechanisms, aiding antiviral drug development.

Area of Science:

  • Structural biology
  • Virology
  • Biophysics

Background:

  • Enveloped viruses utilize viroporins, essential membrane proteins, to permeabilize host cells and facilitate viral budding.
  • Viroporins are challenging to study using traditional structural methods due to their small size and hydrophobic nature.
  • Solid-state NMR (ssNMR) spectroscopy offers a powerful approach to investigate viroporin structure, dynamics, and function in native-like membrane environments.

Purpose of the Study:

  • To elucidate the structure, dynamics, and mechanism of action of influenza M2 and SARS-CoV-2 E proteins using ssNMR.
  • To investigate the proton transport mechanism, drug interactions, and membrane scission roles of influenza M2.
  • To determine the structural basis for the activation and function of SARS-CoV-2 E protein.

Main Methods:

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  • Solid-state NMR (ssNMR) spectroscopy, including 15N and 13C exchange NMR, quantitative 15N NMR, and 13C-2H distance measurements.
  • Development and application of 19F ssNMR techniques for measuring interatomic distances up to 1-2 nm.
  • Investigation of protein behavior across a range of pH conditions and in the presence of specific ligands and lipids.

Main Results:

  • Detailed mechanism of proton shuttling by influenza M2, involving histidine protonation/deprotonation and reorientation, and its inhibition by amantadine.
  • Identification of amantadine binding sites on M2, correlating with drug resistance mutations and revealing a role in cholesterol-dependent membrane scission.
  • Determination of atomic structures for influenza BM2 and SARS-CoV-2 E, revealing pH-dependent structural changes and insights into their activation mechanisms.

Conclusions:

  • Solid-state NMR is highly effective for determining the structure, dynamics, and function of challenging viroporin systems.
  • The findings provide atomic-level insights into viral ion channel function, drug interactions, and viral assembly processes.
  • This work paves the way for the rational design of novel antiviral drugs targeting essential viral membrane proteins.