scholarly journals Proton Transport Behavior through the Influenza A M2 Channel: Insights from Molecular Simulation

2007 ◽  
Vol 93 (10) ◽  
pp. 3470-3479 ◽  
Author(s):  
Hanning Chen ◽  
Yujie Wu ◽  
Gregory A. Voth
Keyword(s):  
Molecular Simulation ◽  
Proton Transport ◽  
Influenza A ◽  
Transport Behavior

scholarly journals Acid-Activation, Proton Transport Rate Saturation, and pH-Dependence of Amantadine Block for Influenza a M2 Protein Truncate (22-62)

2010 ◽  
Vol 98 (3) ◽  
pp. 503a ◽  
Author(s):  
Emily Peterson ◽  
Myunggi Yi ◽  
Huan-Xiang Zhou ◽  
Mukesh Sharma ◽  
Timothy A. Cross ◽  
...  
Keyword(s):  
Proton Transport ◽  
Influenza A ◽  
Ph Dependence ◽  
Transport Rate ◽  
Acid Activation ◽  
M2 Protein

scholarly journals Determining the Functional Core for Proton Transport, Ion Selectivity and Amantadine Sensitivity of the A/M2 Protein from Influenza A Virus

2009 ◽  
Vol 96 (3) ◽  
pp. 668a
Author(s):  
Chunlong Ma ◽  
Alexei Polishchuk ◽  
Yuki Ohigashi ◽  
William F. DeGrado ◽  
Robert A. Lamb ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Proton Transport ◽  
Influenza A ◽  
Ion Selectivity ◽  
M2 Protein

Two different types of channels exhibiting distinct proton transport behavior in an open-framework aluminophosphate

2018 ◽  
Vol 258 ◽  
pp. 695-701 ◽  
Author(s):  
Chen Xue ◽  
Yang Zou ◽  
Shao-Xian Liu ◽  
Xiao-Ming Ren ◽  
Zheng-Fang Tian
Keyword(s):  
Proton Transport ◽  
Open Framework ◽  
Transport Behavior ◽  
Different Types

scholarly journals Acid activation mechanism of the influenza A M2 proton channel

2016 ◽  
Vol 113 (45) ◽  
pp. E6955-E6964 ◽  
Author(s):  
Ruibin Liang ◽  
Jessica M. J. Swanson ◽  
Jesper J. Madsen ◽  
Mei Hong ◽  
William F. DeGrado ◽  
...  
Keyword(s):  
Free Energy ◽  
Proton Transport ◽  
Influenza A ◽  
Conduction Mechanism ◽  
Transmembrane Domain ◽  
Proton Conduction ◽  
Proton Flux ◽  
Activation Mechanism ◽  
Proton Channel ◽  
Acid Activation

The homotetrameric influenza A M2 channel (AM2) is an acid-activated proton channel responsible for the acidification of the influenza virus interior, an important step in the viral lifecycle. Four histidine residues (His37) in the center of the channel act as a pH sensor and proton selectivity filter. Despite intense study, the pH-dependent activation mechanism of the AM2 channel has to date not been completely understood at a molecular level. Herein we have used multiscale computer simulations to characterize (with explicit proton transport free energy profiles and their associated calculated conductances) the activation mechanism of AM2. All proton transfer steps involved in proton diffusion through the channel, including the protonation/deprotonation of His37, are explicitly considered using classical, quantum, and reactive molecular dynamics methods. The asymmetry of the proton transport free energy profile under high-pH conditions qualitatively explains the rectification behavior of AM2 (i.e., why the inward proton flux is allowed when the pH is low in viral exterior and high in viral interior, but outward proton flux is prohibited when the pH gradient is reversed). Also, in agreement with electrophysiological results, our simulations indicate that the C-terminal amphipathic helix does not significantly change the proton conduction mechanism in the AM2 transmembrane domain; the four transmembrane helices flanking the channel lumen alone seem to determine the proton conduction mechanism.

Proton Transport through the Influenza A M2 Channel: Three-Dimensional Reference Interaction Site Model Study

2010 ◽  
Vol 132 (28) ◽  
pp. 9782-9788 ◽  
Author(s):  
Saree Phongphanphanee ◽  
Thanyada Rungrotmongkol ◽  
Norio Yoshida ◽  
Supot Hannongbua ◽  
Fumio Hirata
Keyword(s):  
Proton Transport ◽  
Influenza A ◽  
Three Dimensional ◽  
Interaction Site ◽  
Site Model ◽  
Model Study ◽  
Reference Interaction Site
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