Abstract
Coronavirus spike proteins are large, densely glycosylated macromolecular machines that mediate receptor binding and membrane fusion to facilitate entry into host cells. This report describes the atomic-resolution structure of the spike protein from porcine epidemic diarrhea virus, a pathogenic alphacoronavirus that causes severe agricultural damage. The structure reveals a novel position for the sialic acid-binding attachment domain in the intact spike. We also observed shed fusion-suppressive capping subunits that displayed the putative receptor-binding domain in an accessible conformation. These observations provide a basis for understanding the molecular mechanisms that drive the earliest stages of alphacoronavirus infection and will inform future efforts to rationally design vaccines.
Keywords
BiologyAngstromCryo-electron microscopyPorcine epidemic diarrhea virusSpike (software development)Electron microscopeVirologyCoronavirusVirusProtein structureBiophysicsCoronavirus disease 2019 (COVID-19)CrystallographyBiochemistryPhysicsInfectious disease (medical specialty)Chemistry
Affiliated Institutions
Related Publications
Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2
The trimeric SARS coronavirus (SARS-CoV) surface spike (S) glycoprotein consisting of three S1-S2 heterodimers binds the cellular receptor angiotensin-converting enzyme 2 (ACE2)...
Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
The outbreak of a novel coronavirus (2019-nCoV) represents a pandemic threat that has been declared a public health emergency of international concern. The CoV spike (S) glycopr...
Structure, Function, and Evolution of Coronavirus Spike Proteins
The coronavirus spike protein is a multifunctional molecular machine that mediates coronavirus entry into host cells. It first binds to a receptor on the host cell surface throu...
Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen
Significance Coronaviruses such as Middle East respiratory syndrome coronavirus (MERS-CoV) cause severe respiratory distress with high fatality rates. The spike (S) glycoprotein...
The Coronavirus Spike Protein Is a Class I Virus Fusion Protein: Structural and Functional Characterization of the Fusion Core Complex
ABSTRACT Coronavirus entry is mediated by the viral spike (S) glycoprotein. The 180-kDa oligomeric S protein of the murine coronavirus mouse hepatitis virus strain A59 is posttr...
Publication Info
- Year
- 2019
- Type
- article
- Volume
- 93
- Issue
- 23
- Citations
- 100
- Access
- Closed
External Links
Social Impact
Altmetric
PlumX Metrics
Social media, news, blog, policy document mentions
Citation Metrics
100
OpenAlex
Cite This
Daniel Wrapp,
Jason S. McLellan
(2019).
The 3.1-Angstrom Cryo-electron Microscopy Structure of the Porcine Epidemic Diarrhea Virus Spike Protein in the Prefusion Conformation.
Journal of Virology
, 93
(23)
.
https://doi.org/10.1128/jvi.00923-19
Identifiers
- DOI
- 10.1128/jvi.00923-19