RAS PhysicsКристаллография Crystallography Reports

  • ISSN (Print) 0023-4761
  • ISSN (Online) 3034-5510

Structural Basis for Interactions between Influenza A Virus M2 Proton Channel and Adamantane-Based Antiviral Drugs

PII
10.31857/S0023476123600374-1
DOI
10.31857/S0023476123600374
Publication type
Status
Published
Authors
Volume/ Edition
Volume 68 / Issue number 6
Pages
845-853
Abstract
Influenza A virus pandemics still remain a threat to global health. One class of antiviral drugs, namely, inhibitors of the specific viral enzyme neuraminidase, is predominantly used in the fight against these pandemics. These antivirals include zanamivir (Relenza™) and oseltamivir (Tamiflu™). The viral resistance to this class of compounds steadily increases. The M2 proton channel of influenza A virus is an alternative clinically proven target for antiviral therapy. However, many circulating virus strains bear amino acid mutations in the M2 protein, causing resistance to drugs of the adamantane series, M2 blockers, such as rimantadine and amantadine. Consequently, inhibitors targeting mutants of the M2 channel are urgently needed for public biosafety and health. This review is devoted to structural-functional interactions used in practice and mediated by the action of experimental drugs on the protein target, the transmembrane domain of the influenza virus M2 proton channel. An analysis of the experimental and model structural data available in open access is presented.
Keywords
Date of publication
15.09.2025
Year of publication
2025
Number of purchasers
0
Views
15

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