Interactions of LSECtin and DC-SIGN/DC-SIGNR with viral ligands: Differential pH dependence, internalization and virion binding
Gramberg T, Soilleux E, Fisch T, Lalor PF, Hofmann H, Wheeldon S, Cotterill A, Wegele A, Winkler T, Adams DH, Poehlmann S (2008)
Publication Status: Published
Publication Type: Journal article, Original article
Publication year: 2008
Journal
Publisher: ACADEMIC PRESS INC ELSEVIER SCIENCE
Book Volume: 373
Pages Range: 189-201
Journal Issue: 1
DOI: 10.1016/j.virol.2007.11.001
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-associatedGP. 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. (C) 2007 Elsevier Inc. All rights reserved.
Authors with CRIS profile
Thomas Gramberg
Juniorprofessur für Antivirale Native Immunität
Thomas Winkler
Professur für Genetik
Involved external institutions
John Radcliffe Hospital
United Kingdom (GB)
University of Birmingham
United Kingdom (GB)
Christian-Albrechts-Universität zu Kiel
Germany (DE)
Medizinische Hochschule Hannover (MHH) / Hannover Medical School
Germany (DE)
United Kingdom (GB)
University of Birmingham
United Kingdom (GB)
Christian-Albrechts-Universität zu Kiel
Germany (DE)
Medizinische Hochschule Hannover (MHH) / Hannover Medical School
Germany (DE)
How to cite
APA:
Gramberg, T., Soilleux, E., Fisch, T., Lalor, P.F., Hofmann, H., Wheeldon, S.,... Poehlmann, S. (2008). Interactions of LSECtin and DC-SIGN/DC-SIGNR with viral ligands: Differential pH dependence, internalization and virion binding. Virology, 373(1), 189-201. https://dx.doi.org/10.1016/j.virol.2007.11.001
MLA:
Gramberg, Thomas, et al. "Interactions of LSECtin and DC-SIGN/DC-SIGNR with viral ligands: Differential pH dependence, internalization and virion binding." Virology 373.1 (2008): 189-201.
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