Linked Life Data

18554741

Source:http://linkedlifedata.com/resource/pubmed/id/18554741

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2008-7-8
pubmed:abstractText
Cell entry of severe acute respiratory syndrome coronavirus (SARS-CoV) is mediated by the viral spike (S) protein. Amino acids 319-510 on the S protein have been mapped as the receptor-binding domain (RBD), which mediates binding to the SARS-CoV receptor angiotensin converting enzyme 2 (ACE2) on SARS-CoV susceptible cells. In this study, we expressed a fusion protein containing the human codon-optimized RBD of the SARS-CoV spike protein linked to the Fc portion of human IgG1 (named RBD-Fc) in HEK293 cells. The RBD-Fc protein was purified by affinity chromatography. The flow cytometry assay showed that the purified RBD-Fc protein could bind to ACE2. We demonstrated that the RBD spike protein alone could be internalized into SARS-CoV susceptible cells together with ACE2. We also showed that the removal of N-glycans from the RBD spike protein did not abolish this phenomenon. Our discoveries may have some implications for the development of the SARS vaccine.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0168-1702
pubmed:author
pubmed:issnType
Print
pubmed:volume
136
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8-15
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Endocytosis of the receptor-binding domain of SARS-CoV spike protein together with virus receptor ACE2.
pubmed:affiliation
National Key Laboratory of Medical Molecular Biology, School of Basic Medicine, Peking Union Medical College, Tsinghua University and Institute of Basic Medical Sciences Chinese Academy of Medical Sciences, Beijing 100005, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't