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Bat Influenza M2 Shows Functions Similar to Those of Classical Influenza A Viruses

Wenyu Yang1,2, Liping Wang1,2, Lei Shi1,2,3

  • 1Department of Veterinary Pathobiology, College of Veterinary Medicine, University of Missouri, Columbia, MO 65211, USA.

Pathogens (Basel, Switzerland)
|June 25, 2025
PubMed

Insights

Bat influenza M2 proteins function as ion channels, similar to classical influenza A viruses (IAVs). Key amino acid differences in bat M2 impact antiviral sensitivity and virus survival, revealing functional similarities despite low sequence identity.

Area of Science:

  • Virology
  • Molecular Biology
  • Drug Discovery

Background:

  • Influenza A viruses (IAVs) possess an M2 protein functioning as an ion channel crucial for viral replication and a target for antivirals.
  • Bat influenza viruses represent a diverse group with distinct features compared to classical IAVs.
  • The functional role of the M2 protein in bat influenza viruses, particularly its ion channel activity and susceptibility to antivirals, remains largely unexplored.

Purpose of the Study:

  • To investigate the ion channel activity of bat influenza M2 proteins.
  • To determine the role of specific amino acid residues in bat M2 function and antiviral susceptibility.
  • To compare the functional characteristics of bat influenza M2 with those of classical IAV M2.

Main Methods:

  • Site-directed mutagenesis of bat influenza M2 protein.
  • Ion channel activity assays.
  • Antiviral susceptibility testing (e.g., amantadine).
  • Virus replication and survival assays.

Main Results:

  • Bat influenza M2 protein exhibits ion channel activity, analogous to classical IAV M2.
  • Specific amino acid substitutions at positions 31 (N/S), 37 (H/G), and 41 (W/A) in bat M2 significantly affect antiviral sensitivity and virus replication.
  • Position 31 is critical for amantadine sensitivity, while positions 37 and 41 are vital for virus replication and survival.

Conclusions:

  • Bat influenza M2 proteins function as ion channels, sharing functional similarities with conventional IAV M2 proteins.
  • Despite low sequence identity, bat M2's critical amino acid residues dictate its ion channel properties and susceptibility to established antivirals.
  • These findings have implications for understanding influenza virus evolution and developing broad-spectrum antiviral strategies.
Keywords:
antiviral resistancebat influenza M2ion channel

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