pH-induced conformational change of the influenza M2 protein C-terminal domain

Phuong A. Nguyen; Cinque S. Soto; Alexei Polishchuk; Gregory A. Caputo; Chad D. Tatko; Chunlong Ma; Yuki Ohigashi; Lawrence H. Pinto; William F. Degrado; Kathleen P. Howard

doi:10.1021/bi801315m

pH-induced conformational change of the influenza M2 protein C-terminal domain

Phuong A. Nguyen, Cinque S. Soto, Alexei Polishchuk, Gregory A. Caputo, Chad D. Tatko, Chunlong Ma, Yuki Ohigashi, Lawrence H. Pinto, William F. Degrado, Kathleen P. Howard

Research output: Contribution to journal › Article › peer-review

60 Scopus citations

Abstract

The M2 protein from influenza A is a pH-activated proton channel that plays an essential role in the viral life cycle and serves as a drug target. Using spin labeling EPR spectroscopy, we studied a 38-residue M2 peptide spanning the transmembrane region and its C-terminal extension. We obtained residue-specific environmental parameters under both high- and low-pH conditions for nine consecutive C-terminal sites. The region forms a membrane surface helix at both high and low pH, although the arrangement of the monomers within the tetramer changes with pH. Both electrophysiology and EPR data point to a critical role for residue Lys 49.

Original language	English (US)
Pages (from-to)	9934-9936
Number of pages	3
Journal	Biochemistry
Volume	47
Issue number	38
DOIs	https://doi.org/10.1021/bi801315m
State	Published - Sep 23 2008
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry

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10.1021/bi801315m

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title = "pH-induced conformational change of the influenza M2 protein C-terminal domain",

abstract = "The M2 protein from influenza A is a pH-activated proton channel that plays an essential role in the viral life cycle and serves as a drug target. Using spin labeling EPR spectroscopy, we studied a 38-residue M2 peptide spanning the transmembrane region and its C-terminal extension. We obtained residue-specific environmental parameters under both high- and low-pH conditions for nine consecutive C-terminal sites. The region forms a membrane surface helix at both high and low pH, although the arrangement of the monomers within the tetramer changes with pH. Both electrophysiology and EPR data point to a critical role for residue Lys 49.",

author = "Nguyen, {Phuong A.} and Soto, {Cinque S.} and Alexei Polishchuk and Caputo, {Gregory A.} and Tatko, {Chad D.} and Chunlong Ma and Yuki Ohigashi and Pinto, {Lawrence H.} and Degrado, {William F.} and Howard, {Kathleen P.}",

year = "2008",

month = sep,

day = "23",

doi = "10.1021/bi801315m",

language = "English (US)",

volume = "47",

pages = "9934--9936",

journal = "Biochemistry",

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TY - JOUR

T1 - pH-induced conformational change of the influenza M2 protein C-terminal domain

AU - Nguyen, Phuong A.

AU - Soto, Cinque S.

AU - Polishchuk, Alexei

AU - Caputo, Gregory A.

AU - Tatko, Chad D.

AU - Ma, Chunlong

AU - Ohigashi, Yuki

AU - Pinto, Lawrence H.

AU - Degrado, William F.

AU - Howard, Kathleen P.

PY - 2008/9/23

Y1 - 2008/9/23

N2 - The M2 protein from influenza A is a pH-activated proton channel that plays an essential role in the viral life cycle and serves as a drug target. Using spin labeling EPR spectroscopy, we studied a 38-residue M2 peptide spanning the transmembrane region and its C-terminal extension. We obtained residue-specific environmental parameters under both high- and low-pH conditions for nine consecutive C-terminal sites. The region forms a membrane surface helix at both high and low pH, although the arrangement of the monomers within the tetramer changes with pH. Both electrophysiology and EPR data point to a critical role for residue Lys 49.

AB - The M2 protein from influenza A is a pH-activated proton channel that plays an essential role in the viral life cycle and serves as a drug target. Using spin labeling EPR spectroscopy, we studied a 38-residue M2 peptide spanning the transmembrane region and its C-terminal extension. We obtained residue-specific environmental parameters under both high- and low-pH conditions for nine consecutive C-terminal sites. The region forms a membrane surface helix at both high and low pH, although the arrangement of the monomers within the tetramer changes with pH. Both electrophysiology and EPR data point to a critical role for residue Lys 49.

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DO - 10.1021/bi801315m

M3 - Article

C2 - 18754675

AN - SCOPUS:52249123874

SN - 0006-2960

VL - 47

SP - 9934

EP - 9936

JO - Biochemistry

JF - Biochemistry

IS - 38

ER -

pH-induced conformational change of the influenza M2 protein C-terminal domain

Abstract

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