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NMR structure of the SARS Coronavirus E protein pentameric ion channel
Structural highlights
FunctionVEMP_SARS Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis (By similarity). Activates the host NLRP3 inflammasome, leading to IL-1beta overproduction.[HAMAP-Rule:MF_04204][1] [2] Publication Abstract from PubMedCoronaviruses (CoV) cause common colds in humans, but are also responsible for the recent Severe Acute, and Middle East, respiratory syndromes (SARS and MERS, respectively). A promising approach for prevention are live attenuated vaccines (LAVs), some of which target the envelope (E) protein, which is a small membrane protein that forms ion channels. Unfortunately, detailed structural information is still limited for SARS-CoV E, and non-existent for other CoV E proteins. Herein, we report a structural model of a SARS-CoV E construct in LMPG micelles with, for the first time, unequivocal intermolecular NOEs. The model corresponding to the detergent-embedded region is consistent with previously obtained orientational restraints obtained in lipid bilayers and in vivo escape mutants. The C-terminal domain is mostly alpha-helical, and extramembrane intermolecular NOEs suggest interactions that may affect the TM channel conformation. Structural model of the SARS coronavirus E channel in LMPG micelles.,Surya W, Li Y, Torres J Biochim Biophys Acta. 2018 Jun;1860(6):1309-1317. doi:, 10.1016/j.bbamem.2018.02.017. Epub 2018 Feb 21. PMID:29474890[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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