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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About: DC/L-SIGN recognition of spike glycoprotein promotes SARS-CoV-2 trans-infection and can be inhibited by a glycomimetic antagonist Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
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
resource representing a document's body	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' named entity 'DC-SIGN' named entity 'infection' named entity 'Ebola' named entity 'DC-SIGN' named entity 'carbohydrate' named entity 'protein' named entity 'receptor' named entity 'receptor' named entity 'antibody' named entity 'glycan' named entity 'Negative stain' named entity 'L-SIGN' named entity 'DC-SIGN' 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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