Clearing of Suspensions of<i>Micrococcus lysodeikticus</i>Catalysed by Lysozymes from Hen, Goose, and Turkey Egg Whites, Human Milk, and Phage T4. Assessment of Potential as Signal Generators for Homogeneous Enzyme Immunoassays for Urinary Steroids

Cooke, Delwyn G.; Blackwell, Leonard F.

doi:10.1080/15321810701209704

Cited by 3 publications

(1 citation statement)

References 32 publications

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“…LYSO breaks bacterial cell walls made of peptidoglycan via hydrolysis of the β (1–4) glucosidic bond between N-acetylmuramic acid and N-acetylglucosamine [28, 29]. M. lysoleikticus possesses a peptidoglycan wall [30]. Our results showed that baicalin enhanced the activity of LYSO in a dose-dependent manner.…”

Section: Discussionmentioning

confidence: 88%

Baicalin promotes the bacteriostatic activity of lysozyme on S. aureus in mammary glands and neutrophilic granulocytes in mice

et al. 2017

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Staphylococcus aureus causes mastitis as a result of community-acquired or nosocomial infections. Lysozyme (LYSO) is an enzyme that is upregulated in many organisms during the innate immune response against infection by bacterial pathogens. Baicalin is a bioactive flavonoid that can bind to enzymes, often to potentiate their effect. Here we tested the effects of baicalin on the activity of LYSO using the S. aureus mastitis mouse model and neutrophilic granulocyte model of S. aureus infection. In our experiments, S. aureus counts decreased with increasing baicalin concentration. Furthermore, qPCR and western blot analyses showed that LYSO expression was unaffected by baicalin, while fluorescence quenching and UV fluorescence spectral analyses showed that baicalin binds to LYSO. To test whether this binding increased LYSO activity, we assessed LYSO-induced bacteriostasis in the presence of baicalin. Our results showed that LYSO-induced S. aureus bacteriostasis increased with increasing concentrations of baicalin, and that baicalin binding to LYSO synergistically increased the antibacterial activity of LYSO. These results demonstrate that baicalin enhances LYSO-induced bacteriostasis during the innate immune response to S. aureus. They suggest baicalin is a potentially useful therapeutic agent for the treatment of bacterial infections.

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Section: Discussionmentioning

confidence: 88%

Baicalin promotes the bacteriostatic activity of lysozyme on S. aureus in mammary glands and neutrophilic granulocytes in mice

et al. 2017

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Inhibition of Human Immunodeficiency Type 1 Virus (HIV-1) Life Cycle by Different Egg White Lysozymes

Behbahani

Nosrati

Mohabatkar

2018

Appl Biochem Biotechnol

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Lysozyme is a relatively small enzyme with different biological activities, which is found in tears, saliva, egg white, and human milk. In the study, the anti-HIV-1 activity of lysozymes purified from quail, Meleagris, and hen egg white has been determined. For this end, a time-of-drug-addition assay was performed to identify the target of anti-HIV-1 agents and for determination of probable anti HIV-1 mechanism of the studied lysozyme, the binding affinity of the lysozymes to the human CD4 receptor was studied by molecular docking method. To define structural differences between studied lysozymes, structural motifs of them were predicted by MEME tool. Quail, hen, and Meleagris lysozymes showed potent anti-HIV-1 activity with EC of 7.5, 10, and 55 nM, respectively. The time-of-drug-addition study demonstrated that the inhibitory effect of all purified lysozymes is before HIV-1 infection. The frequency and intensity of CD4 expression in PBMCs decreased in the presence of all mentioned lysozymes. Also, the expression level of C-C chemokine receptor type 5 (CCR5) and chemokine receptor type 4 (CXCR4) on CD4+ T cells was not changed in cells treated with these lysozymes. The results of in silico study confirmed that the binding energy of quail lysozyme with CD4 was more than that of other studied lysozymes. The results revealed that these lysozymes restrict HIV-1 attachment to host cell CD4.

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Conjugation of Estrone Glucuronide with Human Lysozyme

Cooke

Blackwell

2015

Journal of Immunoassay and Immunochemistry

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Human milk lysozyme was conjugated with estrone glucuronide to give a monoacylated conjugate, two disubstituted isoforms, and one trisubstituted isoform in 99.4% yield. The conjugates were pure and highly inhibited (>98%) by the anti-estrone glucuronide antibody. The clearing curves were biphasic for all four conjugates but a 3 min initial rate assay was established and used to measure a normal menstrual cycle profile of estrone glucuronide excretion rates. The marked differences between the hen egg white and human milk lysozyme conjugates show that near identical tertiary structures do not necessarily imply similar physical, chemical, biochemical, and kinetic behavior.

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Clearing of Suspensions ofMicrococcus lysodeikticusCatalysed by Lysozymes from Hen, Goose, and Turkey Egg Whites, Human Milk, and Phage T4. Assessment of Potential as Signal Generators for Homogeneous Enzyme Immunoassays for Urinary Steroids

Cited by 3 publications

References 32 publications

Baicalin promotes the bacteriostatic activity of lysozyme on S. aureus in mammary glands and neutrophilic granulocytes in mice

Baicalin promotes the bacteriostatic activity of lysozyme on S. aureus in mammary glands and neutrophilic granulocytes in mice

Inhibition of Human Immunodeficiency Type 1 Virus (HIV-1) Life Cycle by Different Egg White Lysozymes

Conjugation of Estrone Glucuronide with Human Lysozyme

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