ArticleJournal of virological methods2005
A novel cell-based binding assay system reconstituting interaction between SARS-CoV S protein and its cellular receptor.
Article in Journal of virological methods, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 24 citations in OpenAlex.
- ABO blood group as a determinant of COVID-19 and Long COVID: An observational, longitudinal, large study.PloS one · 2023Observational
- Article
- Cell adhesion as a novel approach to determining the cellular binding motif on the severe acute respiratory syndrome coronavirus spike protein.Journal of virological methods · 2014Article
- Immunogenicity of the spike glycoprotein of bat SARS-like coronavirus.Virologica Sinica · 2010Article
- Dual effect of nitric oxide on SARS-CoV replication: viral RNA production and palmitoylation of the S protein are affected.Virology · 2009Article
- Inhibition of the interaction between the SARS-CoV spike protein and its cellular receptor by anti-histo-blood group antibodies.Glycobiology · 2008Article
- Genetic immunization with Hantavirus vaccine combining expression of G2 glycoprotein and fused interleukin-2.Genetic vaccines and therapy · 2008Article
- Determination and application of immunodominant regions of SARS coronavirus spike and nucleocapsid proteins recognized by sera from different animal species.Journal of immunological methods · 2008Article
- Mapping of equine lentivirus receptor 1 residues critical for equine infectious anemia virus envelope binding.Journal of virology · 2008Article
- The use of hepatitis C virus NS3/4A and secreted alkaline phosphatase to quantitate cell-cell membrane fusion mediated by severe acute respiratory syndrome coronavirus S protein and the receptor angiotensin-converting enzyme 2.Analytical biochemistry · 2007Article
- Induction of specific immune responses by severe acute respiratory syndrome coronavirus spike DNA vaccine with or without interleukin-2 immunization using different vaccination routes in mice.Clinical and vaccine immunology : CVI · 2007Article
- Modification of SARS-CoV S1 gene render expression in Pichia pastoris.Virus genes · 2006Article
- Article
- ACE2 orthologues in non-mammalian vertebrates (Danio, Gallus, Fugu, Tetraodon and Xenopus).Gene · 2006Article
- Monoclonal antibodies targeting the HR2 domain and the region immediately upstream of the HR2 of the S protein neutralize in vitro infection of severe acute respiratory syndrome coronavirus.Journal of virology · 2006Article
- The severe acute respiratory syndrome coronavirus 3a is a novel structural protein.Biochemical and biophysical research communications · 2005Article
- SARS-CoV genome polymorphism: a bioinformatics study.Genomics, proteomics & bioinformatics · 2005Article
- Characterization of viral proteins encoded by the SARS-coronavirus genome.Antiviral research · 2005Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Severe acute respiratory syndrome (SARS), a life-threatening disease, is caused by the newly identified virus SARS coronavirus (SARS-CoV). In order to study the spike (S) protein of this highly contagious virus, we established a clonal cell-line, CHO-SG, from the Chinese hamster ovary cells that stably expresses C-terminally EGFP-tagged SARS-CoV S protein (S-EGFP). The ectodomain of the S glycoprotein is localized on the surface of CHO-SG cells with N-acetyl-glucosamine-terminated carbohydrate structure. CHO-SG cells associated tightly with Vero E6 cells, a SARS-CoV receptor (ACE2) expressing cell-line, and the interaction remained stable under highly stringent condition (1M NaCl). This interaction could be blocked by either the serum from a SARS convalescent patient or a goat anti-ACE2 antibody, indicating that the interaction is specific. A binding epitope with lesser degree of glycosylation and native conformation was localized by using rabbit anti-sera raised against five denatured recombinant S protein fragments expressed in Escherichia coli. One of the sera obtained from the fragment encompassing amino acids 48-358 significantly blocked the interaction between CHO-SG and Vero E6 cells. The region is useful for studying neutralizing antibodies in future vaccine development. This paper describes an easy and safe cell-based assay suitable for studying the binding between SARS-CoV S protein and its receptor.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.