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

68 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.

UR - https://www.scopus.com/pages/publications/52249123874

UR - https://www.scopus.com/pages/publications/52249123874#tab=citedBy

U2 - 10.1021/bi801315m

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

All Science Journal Classification (ASJC) codes

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