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Crucial steps in the structure determination of a coronavirus spike glycoprotein using cryo‐electron microscopy
Author(s) -
Walls Alexandra,
Tortorici M. Alejandra,
Bosch BerendJan,
Frenz Brandon,
Rottier Peter J. M.,
DiMaio Frank,
Rey Felix A.,
Veesler David
Publication year - 2017
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3048
Subject(s) - trimer , coronavirus , glycoprotein , cryo electron microscopy , lipid bilayer fusion , viral entry , biophysics , transmembrane protein , computational biology , biology , microbiology and biotechnology , virology , chemistry , covid-19 , receptor , virus , biochemistry , medicine , viral replication , infectious disease (medical specialty) , dimer , disease , organic chemistry , pathology
The tremendous pandemic potential of coronaviruses was demonstrated twice in the last 15 years by two global outbreaks of deadly pneumonia. Entry of coronaviruses into cells is mediated by the transmembrane spike glycoprotein S, which forms a trimer carrying receptor‐binding and membrane fusion functions. Despite their biomedical importance, coronavirus S glycoproteins have proven difficult targets for structural characterization, precluding high‐resolution studies of the biologically relevant trimer. Recent technological developments in single particle cryo‐electron microscopy allowed us to determine the first structure of a coronavirus S glycoprotein trimer which provided a framework to understand the mechanisms of viral entry and suggested potential inhibition strategies for this family of viruses. Here, we describe the key factors that enabled this breakthrough.