A FUNCTIONALLY DEFINED MODEL FOR THE M-2 PROTON CHANNEL OF INFLUENZA-A VIRUS SUGGESTS A MECHANISM FOR ITS ION SELECTIVITY

Authors
PINTO LH DIECKMANN GR GANDHI CS PAPWORTH CG BRAMAN J SHAUGHNESSY MA LEAR JD LAMB RA DEGRADO WF
Citation
Lh. Pinto et al., A FUNCTIONALLY DEFINED MODEL FOR THE M-2 PROTON CHANNEL OF INFLUENZA-A VIRUS SUGGESTS A MECHANISM FOR ITS ION SELECTIVITY, Proceedings of the National Academy of Sciences of the United Statesof America, 94(21), 1997, pp. 11301-11306
Citations number
40
Categorie Soggetti
Multidisciplinary Sciences
Journal title
Proceedings of the National Academy of Sciences of the United Statesof America → ACNP
ISSN journal
00278424
Volume
94
Issue
21
Year of publication
1997
Pages
11301 - 11306
Database
ISI
SICI code
0027-8424(1997)94:21<11301:AFDMFT>2.0.ZU;2-X
Abstract
The Mt protein from influenza A virus forms proton-selective channels that are essential to viral function and are the target of the drug am antadine. Cys scanning was used to generate a series of mutants with s uccessive substitutions in the transmembrane segment of the protein, a nd the mutants were expressed in Xenopus laevis oocytes. The effect of the mutations on reversal potential, ion currents, and amantadine res istance were measured. Fourier analysis revealed a periodicity consist ent with a four-stranded coiled coil or helical bundle. A three-dimens ional model of this structure suggests a possible mechanism for the pr oton selectivity of the Mt channel of influenza virus.