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About:
DC/L-SIGN recognition of spike glycoprotein promotes SARS-CoV-2 trans-infection and can be inhibited by a glycomimetic antagonist
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schema:ScholarlyArticle
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covidontheweb.inria.fr
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Type:
Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
has title
DC/L-SIGN recognition of spike glycoprotein promotes SARS-CoV-2 trans-infection and can be inhibited by a glycomimetic antagonist
Creator
Delgado, Rafael
Lasala, Fátima
Schoehn, Guy
Bernardi, Anna
Fieschi, Franck
Thépaut, Michel
Vivès, Corinne
Sattin, Sara
Bally, Isabelle
Fenel, Daphna
Grimoire, Yasmina
Labiod, Nuria
Luczkowiak, Joanna
Thielens, Nicole
Source
BioRxiv
abstract
The efficient spread of SARS-CoV-2 resulted in a pandemic that is unique in modern history. Despite early identification of ACE2 as the receptor for viral spike protein, much remains to be understood about the molecular events behind viral dissemination. We evaluated the contribution of C-type lectin receptors (CLRS) of antigen-presenting cells, widely present in air mucosa and lung tissue. DC-SIGN, L-SIGN, Langerin and MGL bind to diverse glycans of the spike using multiple interaction areas. Using pseudovirus and cells derived from monocytes or T-lymphocytes, we demonstrate that while virus capture by the CLRs examined does not allow direct cell infection, DC/L-SIGN, among these receptors, promote virus transfer to permissive ACE2+ cells. A glycomimetic compound designed against DC-SIGN, enable inhibition of this process. Thus, we described a mechanism potentiating viral capture and spreading of infection. Early involvement of APCs opens new avenues for understanding and treating the imbalanced innate immune response observed in COVID-19 pathogenesis
has issue date
2020-08-10
(
xsd:dateTime
)
bibo:doi
10.1101/2020.08.09.242917
has license
biorxiv
sha1sum (hex)
464401f08ee6872f2e50d046b479ed55cfce3194
schema:url
https://doi.org/10.1101/2020.08.09.242917
resource representing a document's title
DC/L-SIGN recognition of spike glycoprotein promotes SARS-CoV-2 trans-infection and can be inhibited by a glycomimetic antagonist
schema:publication
bioRxiv
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covid:464401f08ee6872f2e50d046b479ed55cfce3194#body_text
is
schema:about
of
named entity 'infection'
named entity 'glycoprotein'
named entity 'tissue'
named entity 'capture'
named entity 'efficient'
named entity 'T-lymphocytes'
named entity 'virus'
named entity 'receptor'
named entity 'virus'
named entity 'Langerin'
named entity 'infection'
named entity 'IC50'
named entity 'furin'
named entity 'Quality control'
named entity 'DC-SIGN'
named entity 'Jurkat'
named entity 'SARS-CoV-2'
named entity 'SARS-CoV-2 virus'
named entity 'CLRs'
named entity 'host cell'
named entity 'proinflammatory cytokines'
named entity 'SARS-CoV-2'
named entity 'incubation'
named entity 'virulence'
named entity 'mannose'
named entity 'viruses'
named entity 'fucose'
named entity 'lectins'
named entity 'fetal bovine serum'
named entity 'innate immune cells'
named entity 'cytokine storm'
named entity 'Wrapp'
named entity 'uranyl acetate'
named entity 'Coronaviruses'
named entity 'spike protein'
named entity 'RBD'
named entity 'alveolar macrophages'
named entity 'Jurkat'
named entity 'SARS-CoV-2'
named entity 'DC-SIGN'
named entity 'ligands'
named entity 'HIV infection'
named entity 'tissue damage'
named entity 'evolutionary pressure'
named entity 'DC-SIGN'
named entity 'infection'
named entity 'Superose'
named entity 'extracellular'
named entity 'glycan'
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named entity 'infection'
named entity 'Ebola'
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named entity 'carbohydrate'
named entity 'protein'
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named entity 'receptor'
named entity 'antibody'
named entity 'glycan'
named entity 'Negative stain'
named entity 'L-SIGN'
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named entity 'avidity'
named entity 'molecular weight'
named entity 'SARS-CoV-1'
named entity 'Photoshop'
named entity 'DCs'
named entity 'ACE2'
named entity 'Promega'
named entity 'glycolipids'
named entity 'DC-SIGN'
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