Details

Autor(en) / Beteiligte

• Achilli, Silvia
• Monteiro, João T
• Serna, Sonia
• Mayer-Lambertz, Sabine
• Thépaut, Michel
• Le Roy, Aline
• Ebel, Christine
• Reichardt, Niels-Christian
• Lepenies, Bernd
• Fieschi, Franck
• Vivès, Corinne

Titel

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

Ist Teil von

• International journal of molecular sciences, 2020-07, Vol.21 (15), p.5290

Ort / Verlag

Switzerland: MDPI AG

Erscheinungsjahr

2020

Quelle

MEDLINE

Beschreibungen/Notizen

• 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 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.