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Recent Advances in Lysozyme
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Recent Advances in Lysozyme

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Medicinal Chemistry".

Deadline for manuscript submissions: 30 June 2024 | Viewed by 7113

Special Issue Editors

Prof. Dr. Patrizia Ferraboschi

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Guest Editor
Department of Medical Biotechnology and Translational Medicine, Università degli Studi di Milano, Via Saldini 50, 20133 Milano, Italy
Interests: organic synthesis; biocatalysis; asymmetric synthesis; biologically active compounds
Special Issues, Collections and Topics in MDPI journals
Dr. Paride Grisenti

E-Mail Website
Guest Editor
Bioseutica BV, Corso Elvezia 4, 6900 Lugano, Switzerland
Interests: lysozyme; organic synthesis; nuclear magnetic resonance
Samuele Ciceri

E-Mail Website
Guest Editor Assistant
Department of Pharmaceutical Sciences, University of Milan, Via L. Mangiagalli 25, 20133 Milano, Italy
Interests: organic synthesis; biocatalysis; asymmetric synthesis; biologically active compounds; NMR spectroscopy; HPLC
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Lysozyme, an approximately 14 kDa protein, present in many mucosal secretions (tears, saliva, mucus) and tissues of animals and plants, is endowed with a well-known antibiotic activity mainly against Gram-positive bacteria, whereas its action against viruses and fungi is less explored.

The antimicrobial action of lysozyme is explained through the enzymatic hydrolysis of the 1β,4-glycosidic bonds between N-acetylmuramic acid (NAM) and N-acetylglucosamide (NAG) in the polysaccharide backbone of the peptidoglycans present in the Gram-positive bacterial cell wall.  

Since its discovery by A. Fleming, exactly one hundred years ago, in 1922, lysozyme has been considered an endogenous antibiotic, and both different lysozyme sources (eggs, milk, saliva, tears, etc.) and applications (medical, food preservatives, animal feed, etc.) have been widely studied.

Interest in this protein never has been abandoned, and currently, studies are focused on the identification of modified (chemically or physically) lysozymes, endowed with wider antibacterial activities, also encouraged by the antibiotic resistance problem. Moreover, the availability of modified lysozymes or of lysozyme peptides and oligomers, either alone or in combination with other antibiotics or antivirals, offers the chance to explore possible applications to treat viral infections such as coronavirus disease (COVID-19).  

Prof. Dr. Patrizia Ferraboschi
Dr. Paride Grisenti
Guest Editors

Samuele Ciceri
Guest Editor Assistant

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • lysozyme
  • recombinant lysozyme
  • antibiotic activity
  • antibiotic resistance
  • antiviral activity
  • pyroelectric and piezoelectric properties
  • immunological properties

Published Papers (5 papers)

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Research

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12 pages, 1958 KiB  
Article
Lysozyme Inhibitors as Tools for Lysozyme Profiling: Identification and Antibacterial Function of Lysozymes in the Hemolymph of the Blue Mussel
by Lise Vanderkelen, Joris M. Van Herreweghe and Chris W. Michiels
Molecules 2023, 28(20), 7071; https://doi.org/10.3390/molecules28207071 - 13 Oct 2023
Cited by 1 | Viewed by 861
Abstract
Lysozymes are universal components of the innate immune system of animals that kill bacteria by hydrolyzing their main cell wall polymer, peptidoglycan. Three main families of lysozyme have been identified, designated as chicken (c)-, goose (g)- and invertebrate (i)-type. In response, bacteria have [...] Read more.
Lysozymes are universal components of the innate immune system of animals that kill bacteria by hydrolyzing their main cell wall polymer, peptidoglycan. Three main families of lysozyme have been identified, designated as chicken (c)-, goose (g)- and invertebrate (i)-type. In response, bacteria have evolved specific protein inhibitors against each of the three lysozyme families. In this study, we developed a serial array of three affinity matrices functionalized with a c-, g-, and i-type inhibitors for lysozyme typing, i.e., to detect and differentiate lysozymes in fluids or extracts from animals. The tool was validated on the blue mussel (Mytilus edulis), whose genome carries multiple putative i-, g-, and c-type lysozyme genes. Hemolymph plasma of the animals was found to contain both i- and g-type, but not c-type lysozyme. Furthermore, hemolymph survival of Aeromonas hydrophila and E. coli strains lacking or overproducing the i- type or g-type lysozyme inhibitor, respectively, was analyzed to study the role of the two lysozymes in innate immunity. The results demonstrated an active role for the g-type lysozyme in the innate immunity of the blue mussel, but failed to show a contribution by the i-type lysozyme. Lysozyme profiling using inhibitor-based affinity chromatography will be a useful novel tool for studying animal innate immunity. Full article
(This article belongs to the Special Issue Recent Advances in Lysozyme)
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9 pages, 1129 KiB  
Article
Lysozyme Modification Using Proteolytic Enzymes
by Łukasz Tomczyk, Grzegorz Leśnierowski and Renata Cegielska-Radziejewska
Molecules 2023, 28(17), 6260; https://doi.org/10.3390/molecules28176260 - 26 Aug 2023
Viewed by 886
Abstract
The lysozyme in the chicken egg white consists of various bioactive amino acids. However, these compounds are inactive when they are in the sequence of parent proteins. They become active only when isolated from these proteins. The aim of this study was to [...] Read more.
The lysozyme in the chicken egg white consists of various bioactive amino acids. However, these compounds are inactive when they are in the sequence of parent proteins. They become active only when isolated from these proteins. The aim of this study was to modify lysozyme with proteolytic enzymes under specific conditions of the reaction environment so as to obtain active biopeptides. The physicochemical properties of the resulting preparations were also assessed. Our study showed that the modification of lysozyme with hydrolytic enzymes (pepsin and trypsin) under strictly specified conditions resulted in obtaining biopeptide preparations with new and valuable properties, as compared with native lysozyme. After the enzymatic modification of lysozyme, two structural fractions were distinguished in the composition of the resulting preparations—the monomeric fraction and the peptide fraction. The modified lysozyme exhibited high surface hydrophobicity and high total antibacterial activity despite the decrease in the hydrolytic activity. Modification of lysozyme with hydrolytic enzymes, especially pepsin, resulted in preparations with very good antioxidative properties. Full article
(This article belongs to the Special Issue Recent Advances in Lysozyme)
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12 pages, 5485 KiB  
Article
Heat-Treated Lysozyme Hydrochloride: A Study on Its Structural Modifications and Anti-SARS-CoV-2 Activity
by Serena Delbue, Elena Pariani, Silvia Parapini, Cristina Galli, Nicoletta Basilico, Sarah D’Alessandro, Sara Pellegrino, Elena Pini, Samuele Ciceri, Patrizia Ferraboschi and Paride Grisenti
Molecules 2023, 28(6), 2848; https://doi.org/10.3390/molecules28062848 - 21 Mar 2023
Cited by 1 | Viewed by 1508
Abstract
Lysozyme (E.C. 3.2.1.17), an about 14 kDa protein and pI 11, widely spread in nature, is present in humans mainly in milk, saliva, and intestinal mucus as a part of innate defense mechanisms. It is endowed with antimicrobial activity due to its action [...] Read more.
Lysozyme (E.C. 3.2.1.17), an about 14 kDa protein and pI 11, widely spread in nature, is present in humans mainly in milk, saliva, and intestinal mucus as a part of innate defense mechanisms. It is endowed with antimicrobial activity due to its action as an N-acetylmuramidase, cleaving the 1-4β glycosidic linkage in the peptidoglycan layer of Gram-positive bacteria. This antimicrobial activity is exerted only against a limited number of Gram-negative bacteria. Different action mechanisms are proposed to explain its activity against Gram-negative bacteria, viruses, and fungi. The antiviral activity prompted the study of a possible application of lysozyme in the treatment of SARS-CoV-2 infections. Among the different sources of lysozyme, the chicken egg albumen was chosen, being the richest source of this protein (c-type lysozyme, 129 amino acids). Interestingly, the activity of lysozyme hydrochloride against SARS-CoV-2 was related to the heating (to about 100 °C) of this molecule. A chemical–physical characterization was required to investigate the possible modifications of native lysozyme hydrochloride by heat treatment. The FTIR analysis of the two preparations of lysozyme hydrochloride showed appreciable differences in the secondary structure of the two protein chains. HPLC and NMR analyses, as well as the enzymatic activity determination, did not show significant modifications. Full article
(This article belongs to the Special Issue Recent Advances in Lysozyme)
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Review

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16 pages, 3639 KiB  
Review
Lysozyme: A Natural Product with Multiple and Useful Antiviral Properties
by Alberta Bergamo and Gianni Sava
Molecules 2024, 29(3), 652; https://doi.org/10.3390/molecules29030652 - 30 Jan 2024
Cited by 2 | Viewed by 1329
Abstract
Lysozyme, especially the one obtained from hen’s egg white, continues to show new pharmacological properties. The fact that only a few of these properties can be translated into therapeutic applications is due to the lack of suitable clinical studies. However, this lack cannot [...] Read more.
Lysozyme, especially the one obtained from hen’s egg white, continues to show new pharmacological properties. The fact that only a few of these properties can be translated into therapeutic applications is due to the lack of suitable clinical studies. However, this lack cannot hide the evidence that is emerging from scientific research. This review for the first time examines, from a pharmacological point of view, all the relevant studies on the antiviral properties of lysozyme, analyzing its possible mechanism of action and its ability to block viral infections and, in some cases, inhibit viral replication. Lysozyme can interact with nucleic acids and alter their function, but this effect is uncoupled from the catalytic activity that determines its antibacterial activity; it is present in intact lysozyme but is equally potent in a heat-degraded lysozyme or in a nonapeptide isolated by proteolytic digestion. An analysis of the literature shows that lysozyme can be used both as a disinfectant for raw and processed foods and as a drug to combat viral infections in animals and humans. To summarize, it can be said that lysozyme has important antiviral properties, as already suspected in the initial studies conducted over 50 years ago, and it should be explored in suitable clinical studies on humans. Full article
(This article belongs to the Special Issue Recent Advances in Lysozyme)
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13 pages, 1597 KiB  
Review
Pharmacological Modulation of Host Immunity with Hen Egg White Lysozyme (HEWL)—A Review
by Alberta Bergamo and Gianni Sava
Molecules 2023, 28(13), 5027; https://doi.org/10.3390/molecules28135027 - 27 Jun 2023
Cited by 4 | Viewed by 1907
Abstract
In the 100 years since its discovery, lysozyme has become an important molecule, both as model for studies in different fields and as a candidate for the therapy of various pathological conditions. Of the dozens of known lysozymes, in this review we focus [...] Read more.
In the 100 years since its discovery, lysozyme has become an important molecule, both as model for studies in different fields and as a candidate for the therapy of various pathological conditions. Of the dozens of known lysozymes, in this review we focus on one in particular, lysozyme extracted from hen egg white (HEWL), and its interaction with the immune system when it is administered orally. Experimental data show that there is an axis that directs immune system activation from GALT (gut-associated lymphoid tissue) and the intestinal lymphocyte clusters. Although a contribution of peptidoglycans from digestion of the bacterial cell wall in the intestinal lumen cannot be excluded, immune stimulation is not dependent on the enzymatic activity of HEWL. The immune responses suggest that HEWL is able to recover from immunodepression caused by tumor growth or immunosuppressants, and that it also improves the success of chemotherapy. The positive results obtained in a small Phase 2 study in patients, the ease of oral administration of this protein, and the absence of adverse effects suggest that HEWL may play an important role in all diseases where the immune system is weakened or where its enhancement plays a critical role in the resolution of the pathology. Full article
(This article belongs to the Special Issue Recent Advances in Lysozyme)
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