The core of the respiratory syncytial virus fusion protein is a trimeric coiled coil. Matthews, J., Young, T., Tucker, S., & Mackay, J. Journal of Virology, 74(13):5911-5920, 2000. cited By 67
The core of the respiratory syncytial virus fusion protein is a trimeric coiled coil [link]Paper  doi  abstract   bibtex   
Entry into the host cell by enveloped viruses is mediated by fusion (F) or transmembrane glycoproteins. Many of these proteins share a fold comprising a trimer of antiparallel coiled-coil heterodimers, where the heterodimers are formed by two discontinuous heptad repeat motifs within the proteolytically processed chain. The F protein of human respiratory syncytial virus (RSV; the major cause of lower respiratory tract infections in infants) contains two corresponding regions that are predicted to form coiled coils (HR1 and HR2), together with a third predicted heptad repeat (HR3) located in a nonhomologous position. In order to probe the structures of these three domains and ascertain the nature of the interactions between them, we have studied the isolated HR1, HR2, and HR3 domains of RSV F by using a range of biophysical techniques, including circular dichroism, nuclear magnetic resonance spectroscopy, and sedimentation equilibrium. HR1 forms a symmetrical, trimeric coiled coil in solution (K3 ≃ 2.2 x 1011 M-2) which interacts with HR2 to form a 3:3 hexamer. The HR1-HR2 interaction domains have been mapped using limited proteolysis, reversed-phase high- performance liquid chromatography, and electrospray-mass spectrometry. HR2 in isolation exists as a largely unstructured monomer, although it exhibits a tendency to form aggregates with β-sheet-like characteristics. Only a small increase in α-helical content was observed upon the formation of the hexamer. This suggests that the RSV F glycoprotein contains a domain that closely resembles the core structure of the simian parainfluenza virus 5 fusion protein (K. A. Baker, R. E. Dutch, R. A. Lamb, and T. S. Jardetzky, Mol. Cell 3:309-319, 1999). Finally, HR3 forms weak α-helical homodimers that do not appear to interact with HR1, HR2, or the HR1-HR2 complex. The results of these studies support the idea that viral fusion proteins have a common core architecture.
@ARTICLE{Matthews20005911,
author={Matthews, J.M. and Young, T.F. and Tucker, S.P. and Mackay, J.P.},
title={The core of the respiratory syncytial virus fusion protein is a trimeric coiled coil},
journal={Journal of Virology},
year={2000},
volume={74},
number={13},
pages={5911-5920},
doi={10.1128/JVI.74.13.5911-5920.2000},
note={cited By 67},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034086980&doi=10.1128%2fJVI.74.13.5911-5920.2000&partnerID=40&md5=897c11d2c0d174b1683c68fa1686cb46},
affiliation={Biota Holdings Ltd., Melbourne, Vic. 3004, Australia; Department of Biochemistry, University of Sydney, Sydney, NSW 2006, Australia},
abstract={Entry into the host cell by enveloped viruses is mediated by fusion (F) or transmembrane glycoproteins. Many of these proteins share a fold comprising a trimer of antiparallel coiled-coil heterodimers, where the heterodimers are formed by two discontinuous heptad repeat motifs within the proteolytically processed chain. The F protein of human respiratory syncytial virus (RSV; the major cause of lower respiratory tract infections in infants) contains two corresponding regions that are predicted to form coiled coils (HR1 and HR2), together with a third predicted heptad repeat (HR3) located in a nonhomologous position. In order to probe the structures of these three domains and ascertain the nature of the interactions between them, we have studied the isolated HR1, HR2, and HR3 domains of RSV F by using a range of biophysical techniques, including circular dichroism, nuclear magnetic resonance spectroscopy, and sedimentation equilibrium. HR1 forms a symmetrical, trimeric coiled coil in solution (K3 ≃ 2.2 x 1011 M-2) which interacts with HR2 to form a 3:3 hexamer. The HR1-HR2 interaction domains have been mapped using limited proteolysis, reversed-phase high- performance liquid chromatography, and electrospray-mass spectrometry. HR2 in isolation exists as a largely unstructured monomer, although it exhibits a tendency to form aggregates with β-sheet-like characteristics. Only a small increase in α-helical content was observed upon the formation of the hexamer. This suggests that the RSV F glycoprotein contains a domain that closely resembles the core structure of the simian parainfluenza virus 5 fusion protein (K. A. Baker, R. E. Dutch, R. A. Lamb, and T. S. Jardetzky, Mol. Cell 3:309-319, 1999). Finally, HR3 forms weak α-helical homodimers that do not appear to interact with HR1, HR2, or the HR1-HR2 complex. The results of these studies support the idea that viral fusion proteins have a common core architecture.},
keywords={hybrid protein;  membrane protein, amino acid sequence;  article;  circular dichroism;  host cell;  lower respiratory tract infection;  mass spectrometry;  nonhuman;  nuclear magnetic resonance spectroscopy;  priority journal;  protein degradation;  protein domain;  protein interaction;  protein structure;  Respiratory syncytial pneumovirus;  reversed phase high performance liquid chromatography;  virus envelope, Amino Acid Sequence;  Circular Dichroism;  HN Protein;  Humans;  Molecular Sequence Data;  Nuclear Magnetic Resonance, Biomolecular;  Oligopeptides;  Peptide Biosynthesis;  Protein Structure, Secondary;  Protein Structure, Tertiary;  Respiratory Syncytial Virus, Human;  Viral Envelope Proteins;  Viral Proteins},
correspondence_address1={Matthews, J.M.; Department of Biochemistry, , Sydney, NSW 2006, Australia; email: j.matthews@biochem.usyd.edu.au},
issn={0022538X},
coden={JOVIA},
pubmed_id={10846072},
language={English},
abbrev_source_title={J. Virol.},
document_type={Article},
source={Scopus},
}
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