Lysozyme Association with Nucleic Acids

Steinrauf, L. K.; Shiuan, David; Yang, Wen-Jen; Chiang, Michael Y.

doi:10.1006/bbrc.1999.1804

Cited by 41 publications

(43 citation statements)

References 10 publications

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“…16,35 The results obtained in this study suggest that glucosamine covalently attached to lysozyme and casein might sterically prevent the aggregation of heat-induced unfolding of these proteins, thereby stabilising them in solution. 52 Taken together, the results of the present study show that efficient and rapid glycosylation of casein and lysozyme resulting in improved functional properties can be achieved by covalent attachment of glucosamine using a WSC. The latter reagent is fairly unstable and is essentially removed from the reaction mixture in the dialysis step.…”

Section: Discussionsupporting

confidence: 64%

Effect of conjugation with glucosamine on the functional properties of lysozyme and casein

2008

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BACKGROUND: Modification with carbohydrates usually changes the functional properties of proteins. Such modification might make non-conventional food proteins (such as plant and microbial proteins) more applicable for human consumption. The purpose of this research was to conjugate glucosamine to lysozyme and casein using a water-soluble carbodiimide and to investigate the effect of conjugation on the functional properties of these proteins.

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Section: Discussionsupporting

confidence: 64%

Effect of conjugation with glucosamine on the functional properties of lysozyme and casein

2008

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“…Lysozyme is another protein that has been shown to precipitate DNA (17). However, the precipitation of DNA by beta toxin is markedly different from that of lysozyme.…”

Section: Discussionmentioning

confidence: 99%

Beta toxin catalyzes formation of nucleoprotein matrix in staphylococcal biofilms

Huseby

Kruse

Digre

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

180

213

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Biofilms are surface-associated communities of microbes encompassed by an extracellular matrix. It is estimated that 80% of all bacterial infections involve biofilm formation, but the structure and regulation of biofilms are incompletely understood. Extracellular DNA (eDNA) is a major structural component in many biofilms of the pathogenic bacterium Staphylococcus aureus, but its role is enigmatic. Here, we demonstrate that beta toxin, a neutral sphingomyelinase and a virulence factor of S. aureus, forms covalent cross-links to itself in the presence of DNA (we refer to this as biofilm ligase activity, independent of sphingomyelinase activity) producing an insoluble nucleoprotein matrix in vitro. Furthermore, we show that beta toxin strongly stimulates biofilm formation in vivo as demonstrated by a role in causation of infectious endocarditis in a rabbit model. Together, these results suggest that beta toxin cross-linking in the presence of eDNA assists in forming the skeletal framework upon which staphylococcal biofilms are established.Staphyloccus aureus | virulence | exotoxins

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“…Lysozyme is well known for its muramidase activity which hydrolyzes the bond between Nacetylglucosoamine and N-acetyl muramic acid leading to degradation of peptidylglycan in the cell wall of Gram-positive bacteria. In addition, lysozyme has also been reported to have functions including the induction of fusion of phospholipid vesicles [2], DNAmembrane association [3], antitumor activities [4], inhibition of HIV replication [5], and association with nucleic acids [6].…”

Section: Introductionmentioning

confidence: 99%

Characterization of the Interactions of Lysozyme with DNA by Surface Plasmon Resonance and Circular Dichroism Spectroscopy

Lin¹,

Wey

Kan

et al. 2008

Appl Biochem Biotechnol

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Association with nucleic acid has been recognized as a unique role of lysozyme and may explain why lysozyme was called a killer protein against HIV infection. In the present study, we characterized the interactions of lysozyme and its derived peptides with a biotin-labeled pUC19 plasmid DNA. Real-time detection of the macromolecular interaction was performed using the SPR (surface plasmon resonance) spectroscopy. The SPR sensorgrams were analyzed and the association and dissociation rate constants as well as the dissociation equilibrium constant KD were, thus, estimated. The results reveal that other than the electrostatic interactions between the basic protein and the nucleotide sequences carrying negative charges, the specific DNA-binding motifs at the N- and C-termini of lysozyme were also involved in the interactions. The nonapeptide RAWVAWRNR (aa 107-115 of lysozyme) reported previously to block HIV-1 viral entrance and replication was also able to bind DNA with its KD value comparable to that of histones. The possibilities of ligand-binding-induced conformational changes were investigated using the circular dichroism spectroscopy. The CD spectra (200-320 nm) reveal that the conformational changes indeed occur as the spectra of lysozyme-DNA interactions are much less at the major trough region than the sum of individual spectra. The interaction of lysozyme with DNA molecules may interfere with DNA replication, modulate gene expression, and block bacterial and viral infections. These all suggest that human lysozyme may represent part of the innate immune system with a very broad protective spectrum.

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Lysozyme Association with Nucleic Acids

Cited by 41 publications

References 10 publications

Effect of conjugation with glucosamine on the functional properties of lysozyme and casein

Effect of conjugation with glucosamine on the functional properties of lysozyme and casein

Beta toxin catalyzes formation of nucleoprotein matrix in staphylococcal biofilms

Characterization of the Interactions of Lysozyme with DNA by Surface Plasmon Resonance and Circular Dichroism Spectroscopy

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