A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein.
The agent responsible for the recent severe acute respiratory syndrome (SARS) outbreak is a previously unidentified coronavirus. While there is a wealth of epidemiological studies, little if any molecular characterization of SARS coronavirus (SCoV) proteins has been carried out. Here we describe the molecular characterization of SCoV E protein, a critical component of the virus responsible for virion envelope morphogenesis. We conclusively show that SCoV E protein contains an unusually short, palindromic transmembrane helical hairpin around a previously unidentified pseudo-center of symmetry, a structural feature which seems to be unique to SCoV. The hairpin deforms lipid bilayers by way of increasing their curvature, providing for the first time a molecular explanation of E protein's pivotal role in viral budding. The molecular understanding of this critical component of SCoV may represent the beginning of a concerted effort aimed at inhibiting its function, and consequently, viral infectivity.
Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, The Hebrew University, Givat-Ram, Jerusalem 91904, Israel.
Eyal
E
Arbely
Ziad
Z
Khattari
Guillaume
G
Brotons
Mutaz
M
Akkawi
Tim
T
Salditt
Isaiah T
IT
Arkin
D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000378:metabolism; D017934:Coronavirus / Q000378:metabolism*; D008051:Lipid Bilayers / Q000737:chemistry; D008854:Microscopy, Electron; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D045473:Severe acute respiratory syndrome-related coronavirus; D012542:Scattering, Radiation; D017386:Sequence Homology, Amino Acid; D017550:Spectroscopy, Fourier Transform Infrared; D013816:Thermodynamics; D014759:Viral Envelope Proteins / Q000737:chemistry*; D014965:X-Rays
D008051:Lipid Bilayers; D014759:Viral Envelope Proteins