Evidence map›Paper›PMID 17041212›Full record

ArticleJournal of virology2006

Identifying epitopes responsible for neutralizing antibody and DC-SIGN binding on the spike glycoprotein of the severe acute respiratory syndrome coronavirus.

Yi-Ping Shih, Chia-Yen Chen, Shih-Jen Liu, Kuan-Hsuan Chen, Yuan-Ming Lee, Yu-Chan Chao, Yi-Ming Arthur Chen

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

30 citing papers in PubMed, 50 citations in OpenAlex.

  1. Sepsis - it is all about the platelets.Frontiers in immunology · 2023
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Can SARS-CoV-2 Virus Use Multiple Receptors to Enter Host Cells?International journal of molecular sciences · 2021
    Review
  8. Article
  9. Review
  10. Article
  11. COVID-19: Risk groups, mechanistic insights and challenges.International journal of clinical practice · 2020
    Article
  12. SARS-CoV-2 Spike Protein Interacts with Multiple Innate Immune Receptors.bioRxiv : the preprint server for biology · 2020
    Article
  13. The ocular surface, coronaviruses and COVID-19.Clinical & experimental optometry · 2020
    Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 1 country.

Yi-Ping ShihAIDS Prevention and Research Center, National Yang-Ming University, Taipei 111, Taiwan, Republic of China.
Chia-Yen Chen
Shih-Jen Liu
Kuan-Hsuan Chen
Yuan-Ming Lee
Yu-Chan Chao
Yi-Ming Arthur Chen
National Yang Ming Chiao Tung University · TWInstitute of Molecular Biology, Academia Sinica · TWNational Health Research Institutes · TWTaipei Veterans General Hospital · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The severe acute respiratory syndrome-associated coronavirus (SARS-CoV) uses dendritic cell-specific ICAM-3 grabbing nonintegrin (DC-SIGN) to facilitate cell entry via cellular receptor-angiotensin-converting enzyme 2. For this project, we used recombinant baculoviruses expressing different lengths of SARS-CoV spike (S) protein in a capture assay to deduce the minimal DC-SIGN binding region. Our results identified the region location between amino acid (aa) residues 324 to 386 of the S protein. We then generated nine monoclonal antibodies (MAbs) against the S protein to map the DC-SIGN-binding domain using capture assays with pseudotyped viruses and observed that MAb SIa5 significantly blocked S protein-DC-SIGN interaction. An enhancement assay using the HKU39849 SARS-CoV strain and human immature dendritic cells confirmed our observation. Data from a pepscan analysis and M13 phage peptide display library system mapped the reactive MAb SIa5 epitope to aa residues 363 to 368 of the S protein. Results from a capture assay testing three pseudotyped viruses with mutated N-linked glycosylation sites of the S protein indicate that only two pseudotyped viruses (N330Q and N357Q, both of which lost glycosylation sites near the SIa5 epitope) had diminished DC-SIGN-binding capacity. We also noted that MAb SIb4 exerted a neutralizing effect against HKU39849; its reactive epitope was mapped to aa residues 435 to 439 of the S protein. We offer the data to facilitate the development of therapeutic agents and preventive vaccines against SARS-CoV infection.

Indexed as

Antibodies, MonoclonalAntibodies, ViralAntigens, ViralBaculoviridaeBase SequenceBinding SitesCell Adhesion MoleculesDC-Specific ICAM-3 Grabbing NonintegrinDendritic CellsDNA, ViralEpitope MappingEpitopesGlycosylationHumansIn Vitro TechniquesLectins, C-TypeAntibodies, MonoclonalAntibodies, ViralAntigens, ViralCell Adhesion MoleculesDC-Specific ICAM-3 Grabbing NonintegrinDNA, ViralEpitopesLectins, C-TypeMembrane GlycoproteinsReceptors, Cell SurfaceRecombinant ProteinsSpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVspike protein, mouse hepatitis virusViral Envelope Proteins

Identifiers

PMID17041212
PMCPMC1641789
OpenAlexW2171573919

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.