Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-22286
J Virol 1993 Sep 01;679:5585-94. doi: 10.1128/JVI.67.9.5585-5594.1993.
Show Gene links Show Anatomy links

Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block.

Wang C , Takeuchi K , Pinto LH , Lamb RA .


???displayArticle.abstract???
The influenza A virus M2 integral membrane protein has ion channel activity which can be blocked by the antiviral drug amantadine. The M2 protein transmembrane domain is highly conserved in amino acid sequence for all the human, swine, equine, and avian strains of influenza A virus, and thus, known amino acid differences could lead to altered properties of the M2 ion channel. We have expressed in oocytes of Xenopus laevis the M2 protein of human influenza virus A/Udorn/72 and the avian virus A/chicken/Germany/34 (fowl plague virus, Rostock) and derivatives of the Rostock ion channel altered in the presumed pore region. The pH of activation of the M2 ion channels and amantadine block of the M2 ion channels were investigated. The channels were found to be activated by pH in a similar manner but differed in their apparent Kis for amantadine block.

???displayArticle.pubmedLink??? 7688826
???displayArticle.pmcLink??? PMC237962
???displayArticle.link??? J Virol
???displayArticle.grants??? [+]

Species referenced: Xenopus laevis

References [+] :
ARMSTRONG, ANOMALOUS RECTIFICATION IN THE SQUID GIANT AXON INJECTED WITH TETRAETHYLAMMONIUM CHLORIDE. 1965, Pubmed