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Lysozyme's lectin-like characteristics facilitates its immune defense function

  • Ruiyan Zhang (a1) (a2), Lisha Wu (a3), Thomas Eckert (a4) (a5), Monika Burg-Roderfeld (a5), Miguel A. Rojas-Macias (a5), Thomas Lütteke (a5), Vadim B. Krylov (a6), Dmitry A. Argunov (a6), Aritreyee Datta (a7), Philipp Markart (a8) (a9), Andreas Guenther (a10), Bengt Norden (a3), Roland Schauer (a9), Anirban Bhunia (a7), Mushira Abdelaziz Enani (a11), Martin Billeter (a12), Axel J. Scheidig (a2), Nikolay E. Nifantiev (a6) and Hans-Christian Siebert (a1)...
Abstract
Abstract

Abstract

Interactions between human lysozyme (HL) and the lipopolysaccharide (LPS) of Klebsiella pneumoniae O1, a causative agent of lung infection, were identified by surface plasmon resonance. To characterize the molecular mechanism of this interaction, HL binding to synthetic disaccharides and tetrasaccharides representing one and two repeating units, respectively, of the O-chain of this LPS were studied. pH-dependent structural rearrangements of HL after interaction with the disaccharide were observed through nuclear magnetic resonance. The crystal structure of the HL-tetrasaccharide complex revealed carbohydrate chain packing into the A, B, C, and D binding sites of HL, which primarily occurred through residue-specific, direct or water-mediated hydrogen bonds and hydrophobic contacts. Overall, these results support a crucial role of the Glu35/Asp53/Trp63/Asp102 residues in HL binding to the tetrasaccharide. These observations suggest an unknown glycan-guided mechanism that underlies recognition of the bacterial cell wall by lysozyme and may complement the HL immune defense function.

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Copyright
This is an Open Access article, distributed under the terms of the Creative Commons Attribution licence (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted re-use, distribution, and reproduction in any medium, provided the original work is properly cited.
Corresponding author
*Authors for correspondence: M. Billeter, Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, 40530 Gothenburg, Sweden. Tel: +46 31 7863925; Fax: +46 31 7862599; Email: martin.billeter@chem.gu.se
A. J. Scheidig, Department of Structural Biology, Institute of Zoology, Christian-Albrechts-University, Am Botanischen Garten 1-9, 24118 Kiel, Germany. Tel: +49 431 8804286; Fax: +49 431 8804929; Email: axel.scheidig@strubio.uni-kiel.de.
N. E. Nifantiev, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky prospect 47, 119991 Moscow, Russian Federation. Tel: +7 499 1358784; Fax: +7 499 1358784; Email: nen@ioc.ac.ru
H-C. Siebert, RI-B-NT Research Institute of Bioinformatics and Nanotechnology, Franziusallee 177, 24148 Kiel, Germany. Tel.: +49 431 66878443; Fax: +49 431 56 06 295; Email: hcsiebert@aol.com
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