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Membrane Fusion and Infection of the Influenza Hemagglutinin

Chapter

Abstract

The influenza virus is a major health concern associated with an estimated 5000 to 30,000 deaths every year (Reed et al. 2015) and a significant economic impact with the development of treatments, vaccinations and research (Molinari et al. 2007). The entirety of the influenza genome is comprised of only eleven coding genes. An enormous degree of variation in non-conserved regions leads to significant challenges in the development of inclusive inhibitors for treatment. The fusion peptide domain of the influenza A hemagglutinin (HA) is a promising candidate for treatment since it is one of the most highly conserved sequences in the influenza genome (Heiny et al. 2007), and it is vital to the viral life cycle. Hemagglutinin is a class I viral fusion protein that catalyzes the membrane fusion process during cellular entry and infection. Impediment of the hemagglutinin’s function, either through incomplete post-translational processing (Klenk et al. 1975; Lazarowitz and Choppin 1975) or through mutations (Cross et al. 2001), leads to non-infective virus particles. This review will investigate current research on the role of hemagglutinin in the virus life cycle, its structural biology and mechanism as well as the central role of the hemagglutinin fusion peptide (HAfp) to influenza membrane fusion and infection.

Keywords

Fusion peptide NMR Membrane curvature Membrane protein structure 

Abbreviations

BICS

Bicelle Induced Curvature and Sorting

CD

Circular Dichroism spectroscopy

DPC

Dodecylphosphocholine

DOPC

1,2-dioleoyl-sn-glycero-3-phosphocholine

DOPE

1,2-dioleoyl-sn-glycero-3-phosphoethanolamine

DPoPE

dipalmitoleoylphosphatidylethanolamine

DSC

Differential Scanning Calorimetry

EM

Electron Microscopy

EPR

Electron Paramagnetic Resonance

FP

Fusion Peptide

FRET

Fluorescence Resonance Energy Transfer

FTIR

Fourier Transform Infrared spectroscopy

HA

Hemagglutinin

HA0

Hemagglutinin pre-cleavage precursor

HA1

Hemagglutinin subunit 1

HA2

Hemagglutinin subunit 2

HAfp

Hemagglutinin fusion peptide domain (full-length, 23-residue form)

HAfp20

Hemagglutinin fusion peptide domain (truncated, 20-residue form)

HA-TMD

Hemagglutinin transmembrane domain

HII

type II Hexagonal inverted state

MD

Molecular Dynamics simulations

NMR

Nuclear Magnetic Resonance spectroscopy

NA

Neuraminidase

NGC

Negative Gaussian Curvature

NOE

Nuclear Overhauser Effect

PI

Phosphatidylinositol

PRE

Paramagnetic Relaxation Enhancement

POPC

1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine

POPE

1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine

POPS

1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoserine

PS

Phosphatidylserine

RDC

Residual Dipolar Coupling

SM

Sphingomyelin

vRNPs

viral ribonucleoprotein complexes

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Copyright information

© Springer Internation Publishing Switzerland 2016

Authors and Affiliations

  1. 1.Department of ChemistryUniversity of Illinois at ChicagoChicagoUSA

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