Plasticity and conformational equilibria of influenza fusion peptides in model lipid bilayers

TY - JOUR

T1 - Plasticity and conformational equilibria of influenza fusion peptides in model lipid bilayers

AU - Haria, Neil R

AU - Monticelli, Luca

AU - Fraternali, Franca

AU - Lorenz, Christian D

PY - 2014

Y1 - 2014

N2 - Membrane fusion is critical to eukaryotic cellular function and crucial to the entry of enveloped viruses such as influenza and human immunodeficiency virus. Influenza viral entry in the host cell is mediated by a 20-23 amino acid long sequence, called the fusion peptide. In the last years, possible structures for the fusion peptide and their implication in the membrane fusion initiation have been proposed; these ranging from an inverted V shaped α-helical structure to an α-helical hairpin, or to a complete α-helix. Here we develop a coarse grained approach to describe effectively the plasticity of the fusion peptide and the explored conformational states. We describe also a trimeric assembly for the fusion peptide and analyse the explored states in a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine model membrane. For the single fusion peptide systems the kink angle observed experimentally for the V shaped structure shows a strong correlation with the orientation of the fusion peptide within the lipid bilayer. The trimeric fusion peptide model also experiences different conformational states and represents a more realistic model for the anchoring mechanism of one influenza haemagglutinin molecule. "This article is part of a Special Issue entitled: Viral Membrane Proteins - Channels for Cellular Networking".

AB - Membrane fusion is critical to eukaryotic cellular function and crucial to the entry of enveloped viruses such as influenza and human immunodeficiency virus. Influenza viral entry in the host cell is mediated by a 20-23 amino acid long sequence, called the fusion peptide. In the last years, possible structures for the fusion peptide and their implication in the membrane fusion initiation have been proposed; these ranging from an inverted V shaped α-helical structure to an α-helical hairpin, or to a complete α-helix. Here we develop a coarse grained approach to describe effectively the plasticity of the fusion peptide and the explored conformational states. We describe also a trimeric assembly for the fusion peptide and analyse the explored states in a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine model membrane. For the single fusion peptide systems the kink angle observed experimentally for the V shaped structure shows a strong correlation with the orientation of the fusion peptide within the lipid bilayer. The trimeric fusion peptide model also experiences different conformational states and represents a more realistic model for the anchoring mechanism of one influenza haemagglutinin molecule. "This article is part of a Special Issue entitled: Viral Membrane Proteins - Channels for Cellular Networking".

U2 - 10.1016/j.bbamem.2013.12.020

DO - 10.1016/j.bbamem.2013.12.020

M3 - Article

C2 - 24440592

SN - 0006-3002

VL - N/A

SP - N/A

JO - Biochimica et Biophysica Acta

JF - Biochimica et Biophysica Acta

IS - N/A

M1 - N/A

ER -