PropertyValue
?:abstract
  • SARS-CoV-2 variants with spike (S)-protein D614G mutations now predominate globally. We therefore compare the properties of the mutated S protein (S(G614)) with the original (S(D614)). We report here pseudoviruses carrying S(G614) enter ACE2-expressing cells more efficiently than those with S(D614). This increased entry correlates with less S1-domain shedding and higher S-protein incorporation into the virion. Similar results are obtained with virus-like particles produced with SARS-CoV-2 M, N, E, and S proteins. However, D614G does not alter S-protein binding to ACE2 or neutralization sensitivity of pseudoviruses. Thus, D614G may increase infectivity by assembling more functional S protein into the virion.
is ?:annotates of
?:creator
?:doi
  • 10.1038/s41467-020-19808-4
?:doi
?:journal
  • Nat_Commun
?:license
  • cc-by
?:pdf_json_files
  • document_parses/pdf_json/2ed1623ace0d563ab95b806f90994ac608271e10.json
?:pmc_json_files
  • document_parses/pmc_json/PMC7693302.xml.json
?:pmcid
?:pmid
?:pmid
  • 33243994.0
?:publication_isRelatedTo_Disease
?:sha_id
?:source
  • Medline; PMC
?:title
  • SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity
?:type
?:year
  • 2020-11-26

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