Assembly of the M2 Tetramer Is Strongly Modulated by Lipid Chain Length

Sandra Schick, Lirong Chen, Edwin Li, Janice Lin, Ingo Köper, Kalina A Hristova

Research output: Contribution to journalArticle

Abstract

The influenza virus matrix protein 2 (M2) assembles into a tetramer in the host membrane during viral uncoating and maturation. It has been used as a model system to understand the relative contributions of protein-lipid and protein-protein interactions to membrane protein structure and association. Here we investigate the effect of lipid chain length on the association of the M2 transmembrane domain into tetramers using Forster resonance energy transfer. We observe that the interactions between the M2 helices are much stronger in 1,2-dilauroyl-sn-glycero-3-phosphocholine than in 1-palmitoyl-2-oleoyl-sn-glyc- ero-3-phosphocholine bilayers. Thus, lipid chain length and bilayer thickness not only modulate peptide interactions, but could also be a major determinant of the association of transmembrane helices into functional membrane protein oligomers.

Original languageEnglish (US)
Pages (from-to)1810-1817
Number of pages8
JournalBiophysical Journal
Volume99
Issue number6
DOIs
StatePublished - 2010

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Lipids
Proteins
Membrane Proteins
Virus Uncoating
Fluorescence Resonance Energy Transfer
Orthomyxoviridae
Peptides
Membranes

ASJC Scopus subject areas

  • Biophysics

Cite this

Assembly of the M2 Tetramer Is Strongly Modulated by Lipid Chain Length. / Schick, Sandra; Chen, Lirong; Li, Edwin; Lin, Janice; Köper, Ingo; Hristova, Kalina A.

In: Biophysical Journal, Vol. 99, No. 6, 2010, p. 1810-1817.

Research output: Contribution to journalArticle

Schick, Sandra ; Chen, Lirong ; Li, Edwin ; Lin, Janice ; Köper, Ingo ; Hristova, Kalina A. / Assembly of the M2 Tetramer Is Strongly Modulated by Lipid Chain Length. In: Biophysical Journal. 2010 ; Vol. 99, No. 6. pp. 1810-1817.
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