About: The 3.1-Angstrom Cryo-electron Microscopy Structure of the Porcine Epidemic Diarrhea Virus Spike Protein in the Prefusion Conformation

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About: The 3.1-Angstrom Cryo-electron Microscopy Structure of the Porcine Epidemic Diarrhea Virus Spike Protein in the Prefusion Conformation Goto Sponge NotDistinct Permalink

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Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The 3.1-Angstrom Cryo-electron Microscopy Structure of the Porcine Epidemic Diarrhea Virus Spike Protein in the Prefusion Conformation
Creator	Wrapp, Daniel Mclellan, Jason
Source	Medline; PMC
abstract	Porcine epidemic diarrhea virus (PEDV) is an alphacoronavirus that has a significant agricultural and economic impact due to the high mortality rate associated with infection of neonatal piglets. Like other coronaviruses, PEDV makes use of a large, trimeric spike (S) glycoprotein to mediate membrane fusion and gain entry into host cells. Despite the importance of the spike protein in viral entry and host immune responses, high-resolution structural information concerning this large macromolecular machine has been difficult to obtain. Here, we report the cryo-electron microscopy structure of the PEDV S protein in the prefusion conformation at a resolution of 3.1 Å. Our studies revealed that the sialic acid-binding domain at the N terminus of the S1 subunit has an orientation that is substantially different from that observed in the previously determined spike structure from human alphacoronavirus NL63. We also observed dissociated S1 subunit trimers wherein the putative receptor-binding domains exist in a conformation differing from that observed in the intact spike proteins, suggesting that the PEDV receptor-binding domain undergoes conformational rearrangements akin to those that have been described in the related betacoronaviruses. Collectively, these data provide new insights into the biological processes that mediate alphacoronavirus attachment, receptor engagement, and fusion triggering while also identifying a source of conformational heterogeneity that could be manipulated to improve PEDV vaccine antigens. IMPORTANCE 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.
has issue date	2019-11-13(xsd:dateTime)
bibo:doi	10.1128/jvi.00923-19
bibo:pmid	31534041
has license	cc-by
sha1sum (hex)	2b2903114784318062dabce86e330fbbe9309aa8
schema:url	https://doi.org/10.1128/jvi.00923-19
resource representing a document's title	The 3.1-Angstrom Cryo-electron Microscopy Structure of the Porcine Epidemic Diarrhea Virus Spike Protein in the Prefusion Conformation
has PubMed Central identifier	PMC6854500
has PubMed identifier	31534041
schema:publication	J Virol
resource representing a document's body	covid:2b2903114784318062dabce86e330fbbe9309aa8#body_text
is schema:about of	named entity 'HIGH' named entity 'ASSOCIATED WITH' named entity 'ANTIGENS' named entity 'STAGES' named entity 'DATA' named entity 'DISPLAYED' named entity 'HOST' named entity 'DISSOCIATED' named entity 'BIOLOGICAL PROCESSES' named entity 'NL63' named entity 'STUDIES' named entity 'PROTEINS' named entity 'MACHINES' named entity 'ENGAGEMENT' named entity 'INFECTION' named entity 'OBTAIN' named entity 'INSIGHTS' named entity 'ECONOMIC IMPACT' named entity 'DENSELY' named entity 'AGRICULTURAL' named entity 'HETEROGENEITY' named entity 'OBSERVED' named entity 'HIGH-RESOLUTION' named entity 'HOST CELLS' named entity 'POSITION' named entity 'GAIN' named entity 'DESIGN' named entity 'MEMBRANE FUSION' named entity 'STRUCTURAL' named entity 'SPIKE PROTEIN' named entity 'SIALIC ACID' named entity 'REVEALED' named entity 'CAPPING' named entity 'ENTRY INTO HOST' named entity 'STRUCTURE' named entity 'CONFORMATION' named entity 'BETACORONAVIRUSES' named entity 'HUMAN' named entity 'HAVE' named entity 'DUE TO' named entity 'DOMAIN' named entity 'SUBUNIT' named entity 'LIKE' named entity 'INFORMATION' named entity 'REARRANGEMENTS' named entity 'IDENTIFYING' named entity 'IMMUNE RESPONSES' named entity 'COULD BE' named entity 'GLYCOPROTEIN' named entity '3.1' named entity 'GLYCOSYLATED' named entity 'NOVEL' named entity 'ORIENTATION' named entity 'CRYO-ELECTRON MICROSCOPY' named entity 'BINDING' named entity 'HERE' named entity 'REPORT' named entity 'ALPHACORONAVIRUS' named entity 'SUPPRESSIVE' named entity 'TRIGGERING' named entity 'NEONATAL' named entity 'OUR' named entity 'SOURCE' named entity 'CONFORMATION' named entity 'CRYO-ELECTRON MICROSCOPY' named entity 'PORCINE EPIDEMIC DIARRHEA VIRUS' named entity '3.1' named entity 'ANGSTROM' named entity 'DIFFERENT' named entity 'TERMINUS' named entity 'AGRICULTURAL DAMAGE' named entity 'VIRAL ENTRY' named entity 'MOLECULAR' named entity 'RESOLUTION' named entity 'ACCESSIBLE' named entity 'RECEPTOR BINDING' named entity 'DESCRIBED' named entity 'BASIS' named entity 'INTACT' named entity 'S PROTEIN'

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