Amantadine blocks channel activity of the transmembrane segment of the NB protein from influenza B

Citation
Wb. Fischer et al., Amantadine blocks channel activity of the transmembrane segment of the NB protein from influenza B, EUR BIOPHYS, 30(6), 2001, pp. 416-420
Citations number
28
Categorie Soggetti
Biochemistry & Biophysics
Journal title
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
ISSN journal
01757571 → ACNP
Volume
30
Issue
6
Year of publication
2001
Pages
416 - 420
Database
ISI
SICI code
0175-7571(200110)30:6<416:ABCAOT>2.0.ZU;2-L
Abstract
NB is short auxiliary protein with ca. 100 amino acids, encoded in the vira l genome of influenza B. It is believed to be similar to M2 from influenza A and Vpu from HIV-1 in that it demonstrates ion channel activity. Channels formed by the protein can be blocked by amantadine. We have synthesized th e putative transmembrane segment of NB (IRG S-20 IIITICVSL I-30 VILIVFGCI A (40) KIFI (NB, Lee)). Reconstituted in a lipid bilayer the peptide shows ch annel activity. The addition of amantadine leads to dose-dependent loss of channel activity. Channel blocking is reversible. Channel behaviour of the peptide in the presence of amantadine is in accordance with findings, for t he intact channel. Thus, the synthetic transmembrane peptide captures the i on channel activity of the intact NB protein.