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S.L. TOKAR, I. WOJCIK, Y.P. LIN, A.J. HAY (2020) 'INHIBITION OF PROTON CONDUCTANCE OF THE INFLUENZA A M2 CHANNEL BY AMINOADAMANTANES' in O.A. Krishtal, E.A. Lukyanetz (Eds.), ESSAYS ON NEUROPHYSIOLOGY BY PLATON KOSTYUK AND HIS STUDENTS, AKADEMPERIODYKA, pp. 279-284

INHIBITION OF PROTON CONDUCTANCE OF THE INFLUENZA A M2 CHANNEL BY AMINOADAMANTANES

S.L. TOKAR1,2, I. WOJCIK1, Y.P. LIN1, A.J. HAY1

  1. National Institute for Medical Research, London, UK
  2. Bogomoletz Institute of physiology NAS of Ukraine, Kyiv, Ukraine;
DOI: https://doi.org/10.15407/biph.books.EssNeur.279


Abstract

The M2 protein of in］ uenza A virus is the smallest known protein which exhibits the basic properties of an ion channel. It is characterized by high proton selectivity and a proton regulated gating mechanism (Chizhmakov et al., 1996a). The proton conductivity of the M2 protein plays important roles in two stages of virus replication. As virus particles enter cells by endocytosis, the M2 channel transfers protons from the acidic endosomal environment to the virus interior, triggering dissociation of the viral matrix protein from the viral ribonucleoprotein (RNP) and release of free viral RNP. the M2 channel reduces the acidity within trans Golgi vesicles, to preserve the structural integrity of the haemagglutinin and infectivity of progeny virus particles.

Keywords: Influenza A, M2 ion channel, proton conductance, rimantadine, amantadine, antiviral resistance, patch-clamp, extracellular pH, drug inhibition, His37 protonation, Val27 gate, viral replication.

Full text: (PDF, in English)

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