About: Interactions of LSECtin and DC-SIGN/DC-SIGNR with viral ligands: Differential pH dependence, internalization and virion binding

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About: Interactions of LSECtin and DC-SIGN/DC-SIGNR with viral ligands: Differential pH dependence, internalization and virion binding Goto Sponge NotDistinct Permalink

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

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Interactions of LSECtin and DC-SIGN/DC-SIGNR with viral ligands: Differential pH dependence, internalization and virion binding
Creator	Pöhlmann, Stefan Hofmann, Heike Gramberg, Thomas Fisch, Tanja Wegele, Anja Winkler, Thomas Cotterill, Andrew Soilleux, Elizabeth Wheeldon, Sophie Adams, David Lalor, Patricia
Source	Elsevier; Medline; PMC
abstract	Abstract The calcium-dependent lectins DC-SIGN and DC-SIGNR (collectively termed DC-SIGN/R) bind to high-mannose carbohydrates on a variety of viruses. In contrast, the related lectin LSECtin does not recognize mannose-rich glycans and interacts with a more restricted spectrum of viruses. Here, we analyzed whether these lectins differ in their mode of ligand engagement. LSECtin and DC-SIGNR, which we found to be co-expressed by liver, lymph node and bone marrow sinusoidal endothelial cells, bound to soluble Ebola virus glycoprotein (EBOV-GP) with comparable affinities. Similarly, LSECtin, DC-SIGN and the Langerhans cell-specific lectin Langerin readily bound to soluble human immunodeficiency virus type-1 (HIV-1) GP. However, only DC-SIGN captured HIV-1 particles, indicating that binding to soluble GP is not necessarily predictive of binding to virion-associated GP. Capture of EBOV-GP by LSECtin triggered ligand internalization, suggesting that LSECtin like DC-SIGN might function as an antigen uptake receptor. However, the intracellular fate of lectin–ligand complexes might differ. Thus, exposure to low-pH medium, which mimics the acidic luminal environment in endosomes/lysosomes, released ligand bound to DC-SIGN/R but had no effect on LSECtin interactions with ligand. Our results reveal important differences between pathogen capture by DC-SIGN/R and LSECtin and hint towards different biological functions of these lectins.
has issue date	2008-03-30(xsd:dateTime)
bibo:doi	10.1016/j.virol.2007.11.001
bibo:pmid	18083206
has license	els-covid
sha1sum (hex)	45e64c5963b9f16e654cb31ff11561e1a9a420c3
schema:url	https://doi.org/10.1016/j.virol.2007.11.001
resource representing a document's title	Interactions of LSECtin and DC-SIGN/DC-SIGNR with viral ligands: Differential pH dependence, internalization and virion binding
has PubMed Central identifier	PMC7103327
has PubMed identifier	18083206
schema:publication	Virology
resource representing a document's body	covid:45e64c5963b9f16e654cb31ff11561e1a9a420c3#body_text
is schema:about of	named entity 'captured' named entity 'collectively' named entity 'lysosomes' named entity 'HIV-1' named entity 'particles' named entity 'internalization' covid:arg/45e64c5963b9f16e654cb31ff11561e1a9a420c3 named entity 'mimics' named entity 'soluble' named entity 'carbohydrates' named entity 'bone marrow' named entity 'penicillin' named entity 'Invitrogen' named entity '37°C' named entity 'recombinant proteins' named entity 'lectin' named entity 'ligand' named entity 'formalin' named entity 'infectivity' named entity 'lysosomes' named entity 'mannose receptor' named entity 'placenta' named entity 'bone marrow' named entity 'Cy5' named entity 'transfection' named entity 'Gp120' named entity 'lectin' named entity 'ligand binding' named entity 'fusion protein' named entity 'mannan' named entity 'DC-SIGN' named entity 'MHC' named entity 'liver' named entity 'negative control' named entity 'lectin' named entity 'flow cytometry' named entity 'Germany' named entity 'HIV-1' named entity 'antibody' named entity 'lectins' named entity 'electroporation' named entity 'liver' named entity 'antibodies' named entity 'streptomycin' named entity 'envelope protein' named entity 'cloned' named entity 'Dulbecco's modified Eagle's medium' named entity 'sexually transmitted' named entity 'Research Ethics Committee' named entity 'DC-SIGN' named entity 'HIV-1' named entity 'Langerin' named entity 'glycoprotein' named entity 'internalization' named entity 'medium' named entity 'lectins' named entity 'lectin' named entity 'infection' named entity 'macrophages' named entity 'viruses' named entity '293 cells' named entity 'MAb' named entity 'blood stream' named entity 'present in the blood' named entity 'Invitrogen' named entity 'membrane fusion' named entity 'Gramberg' named entity 'cell lysates' named entity 'DCs' named entity 'clinically relevant' named entity 'lectin'

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