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Article

BC2L-C N-Terminal Lectin Domain Complexed with Histo Blood Group Oligosaccharides Provides New Structural Information

1
Univ. Grenoble Alpes, CNRS, CERMAV, 38000 Grenoble, France
2
Università degli Studi di Milano, Dip. Chimica, via Golgi 19, 20133 Milano, Italy
*
Author to whom correspondence should be addressed.
Academic Editor: Derek J. McPhee
Molecules 2020, 25(2), 248; https://doi.org/10.3390/molecules25020248
Received: 7 December 2019 / Revised: 27 December 2019 / Accepted: 29 December 2019 / Published: 7 January 2020
Lectins mediate adhesion of pathogens to host tissues, filling in a key role in the first steps of infection. Belonging to the opportunistic pathogen Burkholderia cenocepacia, BC2L-C is a superlectin with dual carbohydrate specificity, believed to mediate cross-linking between bacteria and host cells. Its C-terminal domain binds to bacterial mannosides while its N-terminal domain (BCL2-CN) recognizes fucosylated human epitopes. BC2L-CN presents a tumor necrosis factor alpha (TNF-α) fold previously unseen in lectins with a novel fucose binding mode. We report, here, the production of a novel recombinant form of BC2L-CN (rBC2L-CN2), which allowed better protein stability and unprecedented co-crystallization with oligosaccharides. Isothermal calorimetry measurements showed no detrimental effect on ligand binding and data were obtained on the binding of Globo H hexasaccharide and l-galactose. Crystal structures of rBC2L-CN2 were solved in complex with two blood group antigens: H-type 1 and H-type 3 (Globo H) by X-ray crystallography. They provide new structural information on the binding site, of importance for the structural-based design of glycodrugs as new antimicrobials with antiadhesive properties. View Full-Text
Keywords: TNF-like lectin; fucosides; blood group antigen; crystallography TNF-like lectin; fucosides; blood group antigen; crystallography
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MDPI and ACS Style

Bermeo, R.; Bernardi, A.; Varrot, A. BC2L-C N-Terminal Lectin Domain Complexed with Histo Blood Group Oligosaccharides Provides New Structural Information. Molecules 2020, 25, 248. https://doi.org/10.3390/molecules25020248

AMA Style

Bermeo R, Bernardi A, Varrot A. BC2L-C N-Terminal Lectin Domain Complexed with Histo Blood Group Oligosaccharides Provides New Structural Information. Molecules. 2020; 25(2):248. https://doi.org/10.3390/molecules25020248

Chicago/Turabian Style

Bermeo, Rafael, Anna Bernardi, and Annabelle Varrot. 2020. "BC2L-C N-Terminal Lectin Domain Complexed with Histo Blood Group Oligosaccharides Provides New Structural Information" Molecules 25, no. 2: 248. https://doi.org/10.3390/molecules25020248

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