PropertyValue
?:abstract
  • The recent outbreak of pneumonia-causing COVID-19 in China is an urgent global public health issue with an increase in mortality and morbidity. Here we report our modelled homo-trimer structure of COVID-19 spike glycoprotein in both closed (ligand-free) and open (ligand-bound) conformation, which is involved in host cell adhesion. We also predict the unique N- and O-linked glycosylation sites of spike glycoprotein that distinguish it from the SARS and underlines shielding and camouflage of COVID-19 from the host the defence system. Furthermore, our study also highlights the key finding that the S1 domain of COVID-19 spike glycoprotein potentially interacts with the human CD26, a key immunoregulatory factor for hijacking and virulence. These findings accentuate the unique features of COVID-19 and assist in the development of new therapeutics.
?:creator
?:doi
?:doi
  • 10.1080/22221751.2020.1739565
?:journal
  • Emerg_Microbes_Infect
?:license
  • cc-by
?:pdf_json_files
  • document_parses/pdf_json/3aa241293d8448d3b6dac7fec4f2565114b746ce.json
?:pmcid
?:pmid
?:pmid
  • 32178593.0
?:publication_isRelatedTo_Disease
?:sha_id
?:source
  • Medline; PMC
?:title
  • Emerging WuHan (COVID-19) coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26
?:type
?:year
  • 2020-03-17

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