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

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          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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          Most cited references27

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          MOLMOL: A program for display and analysis of macromolecular structures

          Reto Koradi, Martin Billeter, Kurt Wüthrich (1996)
          Article 0 comments Cited 378 times – based on 0 reviews     Review now
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            The program XEASY for computer-supported NMR spectral analysis of biological macromolecules.

            C. Bartels, T Xia, M Billeter … (1995)
            A new program package, XEASY, was written for interactive computer support of the analysis of NMR spectra for three-dimensional structure determination of biological macromolecules. XEASY was developed for work with 2D, 3D and 4D NMR data sets. It includes all the functions performed by the precursor program EASY, which was designed for the analysis of 2D NMR spectra, i.e., peak picking and support of sequence-specific resonance assignments, cross-peak assignments, cross-peak integration and rate constant determination for dynamic processes. Since the program utilizes the X-window system and the Motif widget set, it is portable on a wide range of UNIX workstations. The design objective was to provide maximal computer support for the analysis of spectra, while providing the user with complete control over the final resonance assignments. Technically important features of XEASY are the use and flexible visual display of 'strips', i.e., two-dimensional spectral regions that contain the relevant parts of 3D or 4D NMR spectra, automated sorting routines to narrow down the selection of strips that need to be interactively considered in a particular assignment step, a protocol of resonance assignments that can be used for reliable bookkeeping, independent of the assignment strategy used, and capabilities for proper treatment of spectral folding and efficient transfer of resonance assignments between spectra of different types and different dimensionality, including projected, reduced-dimensionality triple-resonance experiments.
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              Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria.

              Barbara Masschalck, Chris W Michiels (2003)
              The purpose of this review is to describe the antibacterial properties and mode of action of lysozyme against gram-positive and gram-negative bacteria, and to provide insight in the underlying causes of bacterial resistance or sensitivity to lysozyme. Such insight improves our understanding of the role of this ubiquitous enzyme in antibacterial defense strategies in nature and provides a basis for the development and improvement of applications of this enzyme as an antibacterial agent. The bactericidal properties of lysozyme are primarily ascribed to its N-acetylmuramoylhydrolase enzymic activity, resulting in peptidoglycan hydrolysis and cell lysis. However, an increasing body of evidence supports the existence of a nonenzymic and/or nonlytic mode of action. Because gram-negative bacteria, including some major foodborne pathogens, are normally insensitive to lysozyme by virtue of their outer membrane that acts as a physical barrier preventing access of the enzyme, several strategies have been developed to extend the working spectrum of lysozyme to gram-negative bacteria. These include denaturation of lysozyme, modification of lysozyme by covalent attachment of polysaccharides, fatty acids and other compounds, attachment of C-terminal hydrophobic peptides to lysozyme by genetic modification, and the use of outer membrane permeabilizing agents such as EDTA or polycations or permeabilizing treatments such as high hydrostatic pressure treatment.
              Article 0 comments Cited 84 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (iso-abbrev): Q. Rev. Biophys.
                Title: Quarterly reviews of biophysics
                Publisher: Cambridge University Press (CUP)
                ISSN (Electronic): 1469-8994
                ISSN (Print): 0033-5835
                Publication date (Electronic): January 2017
                Volume: 50
                Affiliations
                [1 ] RI-B-NT Research Institute of Bioinformatics and Nanotechnology,Franziusallee 177, 24148 Kiel,Germany.
                [2 ] Department of Chemical and Biological Engineering,Chalmers University of Technology,41296 Gothenburg,Sweden.
                [3 ] Clinic of Obstetrics, Gynecology and Andrology for Small and Large Animals,Justus-Liebig-University, Justus-Liebig-University Giessen,Frankfurter Str. 106, 35392 Giessen,Germany.
                [4 ] Institute for Veterinary Physiology and Biochemistry, Justus-Liebig-University,Frankfurter Str.100, 35392 Giessen,Germany.
                [5 ] Laboratory of Glycoconjugate Chemistry,N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences,Leninsky prospect 47, 119991 Moscow,Russian Federation.
                [6 ] Department of Biophysics,Bose Institute,P-1/12 CIT Scheme VII (M), Kolkata 700054,India.
                [7 ] Pneumology, Heart-Thorax-Center Fulda,Pacelliallee 4 - 36043 Fulda,Germany.
                [8 ] Medical Clinic II, Justus-Liebig-University,Klinikstraße 33, 35392 Giessen,Germany; Member of the German Center for Lung Research (DZL).
                [9 ] Institute of Biochemistry, Christian-Albrechts-University,Olshausenstrasse 40, 24098 Kiel,Germany.
                [10 ] Infectious Diseases Division, Department of Medicine,King Fahad Medical City, PO Box 59046, Riyadh 11525,Kingdom of Saudi Arabia.
                [11 ] Department of Chemistry and Molecular Biology,University of Gothenburg,40530 Gothenburg,Sweden.
                [12 ] Department of Structural Biology,Institute of Zoology, Christian-Albrechts-University,Am Botanischen Garten 1-9, 24118 Kiel,Germany.
                Article
                Publisher Item ID: S0033583517000075
                DOI: 10.1017/S0033583517000075
                PubMed ID: 29233221
                SO-VID: af456004-3172-47a1-83ae-02e23b8c64ee
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