Assembly of the m2 tetramer is strongly modulated by lipid chain length.
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 Förster 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-glycero-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.
Schick
Sandra
S
Department of Materials Science and Engineering, The Johns Hopkins University, Baltimore, Maryland, USA.
Chen
Lirong
L
Li
Edwin
E
Lin
Janice
J
Köper
Ingo
I
Hristova
Kalina
K
D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000378:metabolism; D031541:Fluorescence Resonance Energy Transfer; D009980:Influenza A virus; D008051:Lipid Bilayers / Q000737:chemistry* / Q000378:metabolism*; D008969:Molecular Sequence Data; D010713:Phosphatidylcholines / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D055503:Protein Multimerization; D014763:Viral Matrix Proteins / Q000737:chemistry* / Q000378:metabolism*; D000086082:Viroporin Proteins
D008051:Lipid Bilayers; D010713:Phosphatidylcholines; D014763:Viral Matrix Proteins; C488937:M2 protein, Influenza A virus; D000086082:Viroporin Proteins; C002448:1,2-linoleoylphosphatidylcholine; C028694:1-palmitoyl-2-oleoylphosphatidylcholine