Next Article in Journal
Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective
Next Article in Special Issue
Rearrangement of the Cellulose-Enriched Cell Wall in Flax Phloem Fibers over the Course of the Gravitropic Reaction
Previous Article in Journal
ORAI2 Down-Regulation Potentiates SOCE and Decreases Aβ42 Accumulation in Human Neuroglioma Cells
Previous Article in Special Issue
Abberant Immunoglobulin G Glycosylation in Rheumatoid Arthritis by LTQ-ESI-MS

TETRALEC, Artificial Tetrameric Lectins: A Tool to Screen Ligand and Pathogen Interactions

Institut de Biologie Structurale, CEA, CNRS, University of Grenoble Alpes, F-38000 Grenoble, France
Immunology Unit & Research Center for Emerging Infections and Zoonoses (RIZ), University of Veterinary Medicine Hannover, 30559 Hannover, Germany
Glycotechnology Laboratory, Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), CIBER-BBN, Paseo Miramón 182, 20014 San Sebastian, Spain
Author to whom correspondence should be addressed.
Present address: Département de Chimie Moléculaire, UMR CNRS 5250, Université Grenoble-Alpes, BP 53, 38041 Grenoble, France.
Present address: Department of Pediatric Pneumology, Allergology and Neonatology and Cluster of Excellence RESIST (EXC 2155), Hannover Medical School, 30625 Hannover, Germany.
Int. J. Mol. Sci. 2020, 21(15), 5290;
Received: 3 July 2020 / Revised: 23 July 2020 / Accepted: 23 July 2020 / Published: 25 July 2020
C-type lectin receptor (CLR)/carbohydrate recognition occurs through low affinity interactions. Nature compensates that weakness by multivalent display of the lectin carbohydrate recognition domain (CRD) at the cell surface. Mimicking these low affinity interactions in vitro is essential to better understand CLR/glycan interactions. Here, we present a strategy to create a generic construct with a tetrameric presentation of the CRD for any CLR, termed TETRALEC. We applied our strategy to a naturally occurring tetrameric CRD, DC-SIGNR, and compared the TETRALEC ligand binding capacity by synthetic N- and O-glycans microarray using three different DC-SIGNR constructs i) its natural tetrameric counterpart, ii) the monomeric CRD and iii) a dimeric Fc-CRD fusion. DC-SIGNR TETRALEC construct showed a similar binding profile to that of its natural tetrameric counterpart. However, differences observed in recognition of low affinity ligands underlined the importance of the CRD spatial arrangement. Moreover, we further extended the applications of DC-SIGNR TETRALEC to evaluate CLR/pathogens interactions. This construct was able to recognize heat-killed Candida albicans by flow cytometry and confocal microscopy, a so far unreported specificity of DC-SIGNR. In summary, the newly developed DC-SIGNR TETRALEC tool proved to be useful to unravel novel CLR/glycan interactions, an approach which could be applied to other CLRs. View Full-Text
Keywords: C-type lectin; DC-SIGNR; glycan array; multivalency; pathogen recognition C-type lectin; DC-SIGNR; glycan array; multivalency; pathogen recognition
Show Figures

Figure 1

MDPI and ACS Style

Achilli, S.; Monteiro, J.T.; Serna, S.; Mayer-Lambertz, S.; Thépaut, M.; Le Roy, A.; Ebel, C.; Reichardt, N.-C.; Lepenies, B.; Fieschi, F.; Vivès, C. TETRALEC, Artificial Tetrameric Lectins: A Tool to Screen Ligand and Pathogen Interactions. Int. J. Mol. Sci. 2020, 21, 5290.

AMA Style

Achilli S, Monteiro JT, Serna S, Mayer-Lambertz S, Thépaut M, Le Roy A, Ebel C, Reichardt N-C, Lepenies B, Fieschi F, Vivès C. TETRALEC, Artificial Tetrameric Lectins: A Tool to Screen Ligand and Pathogen Interactions. International Journal of Molecular Sciences. 2020; 21(15):5290.

Chicago/Turabian Style

Achilli, Silvia, João T. Monteiro, Sonia Serna, Sabine Mayer-Lambertz, Michel Thépaut, Aline Le Roy, Christine Ebel, Niels-Christian Reichardt, Bernd Lepenies, Franck Fieschi, and Corinne Vivès. 2020. "TETRALEC, Artificial Tetrameric Lectins: A Tool to Screen Ligand and Pathogen Interactions" International Journal of Molecular Sciences 21, no. 15: 5290.

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

Back to TopTop