Nonclassical antagonism between human lysozyme and AMPs against <i>Pseudomonas aeruginosa</i>

Blumenthal, Ian; Davis, Lydia R.; Berman, Chet Michael.; Griswold, Karl E.

doi:10.1002/2211-5463.13094

Cited by 6 publications

(5 citation statements)

References 38 publications

(47 reference statements)

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“…The human lysozyme was reported by Hancock to show a good synergy with the AMP protegrin against Enterococcus faecalis : indeed the MICs of protegrin and lysozyme were lowered from 16 and 6 μg/mL, when used alone, to 4 and 0.39 μg/mL, respectively, in combination [ 230 ]. The combination of human lysozyme with six different AMPs against P. aeruginosa was recently examined and the authors discovered that some AMPs manifest antagonistic interactions with hLys, in contrast to prior reports [ 231 ]. These results, according to the authors, must be considered for the future development of lysozyme and AMP combination therapies.…”

Section: Synergistic Activity Of Lysozymementioning

confidence: 96%

Applications of Lysozyme, an Innate Immune Defense Factor, as an Alternative Antibiotic

Ferraboschi

Ciceri

Grisenti³

2021

Antibiotics

174

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Lysozyme is a ~14 kDa protein present in many mucosal secretions (tears, saliva, and mucus) and tissues of animals and plants, and plays an important role in the innate immunity, providing protection against bacteria, viruses, and fungi. Three main different types of lysozymes are known: the c-type (chicken or conventional type), the g-type (goose type), and the i-type (invertebrate type). It has long been the subject of several applications due to its antimicrobial properties. The problem of antibiotic resistance has stimulated the search for new molecules or new applications of known compounds. The use of lysozyme as an alternative antibiotic is the subject of this review, which covers the results published over the past two decades. This review is focused on the applications of lysozyme in medicine, (the treatment of infectious diseases, wound healing, and anti-biofilm), veterinary, feed, food preservation, and crop protection. It is available from a wide range of sources, in addition to the well-known chicken egg white, and its synergism with other compounds, endowed with antimicrobial activity, are also summarized. An overview of the modified lysozyme applications is provided in the form of tables.

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Section: Synergistic Activity Of Lysozymementioning

confidence: 96%

Applications of Lysozyme, an Innate Immune Defense Factor, as an Alternative Antibiotic

Ferraboschi

Ciceri

Grisenti³

2021

Antibiotics

174

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“…It catalyzes the breaking of β -1,4-glycosidic bonds of peptidoglycan in bacterial cell walls [ 1 , 2 ] and exerts broad-spectrum antibacterial activities against Gram-negative bacteria (GNB) and Gram-positive bacteria (GPB) in vitro [ 2 ]. LYS is present not only in human [ 3 ] but also in the egg whites of most avians [ 4 ]. Additionally, LYS also has many other biological properties, such as antimicrobial [ 2 ], anti-inflammatory [ 5 ], antitumor [ 6 , 7 ], and antiviral [ 1 ] activities.…”

Section: Introductionmentioning

confidence: 99%

The In Vitro Antimicrobial and Antibiofilm Activities of Lysozyme against Gram-Positive Bacteria

Liu¹,

Wang

Huang

et al. 2022

Computational and Mathematical Methods in Medicine

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Objective. To analyze the in vitro antibacterial and antibiofilm activities of lysozyme (LYS) and its combination with various drugs against Gram-positive bacteria (GPB, n = 9 ), thus to provide an exploration direction for drug development. Methods. The minimum inhibitory concentrations (MICs) of linezolid (LZD), amikacin (AMK), ceftriaxone/sulbactam (CRO/SBT), cefotaxime/sulbactam (CTX/SBT), piperacillin/sulbactam (PIP/SBT), doxycycline (DOX), levofloxacin (LVX), amoxicillin/clavulanate potassium (7 : 1, AK71), imipenem (IPM), azithromycin (AZM), and their combinations with LYS were determined with tuber twice dilution. The antimicrobial and antibiofilm activities of LYS, AZM, LVX, and their combinations with others were evaluated through MTT and crystal violet assay. Results. High-dose LYS (30 μg/mL) combined with PIP/SBT and AK71, respectively, showed synergistic antibacterial activities against methicillin-resistant Staphylococcus aureus (MRSA), while it showed no synergistic activities when combined with other drugs. LYS and AZM inhibited the biofilm formation of one MRSA strain, but they and LVX had no similar activities against methicillin-resistant Staphylococcus epidermidis (MRSE) or vancomycin-resistant Enterococcus faecium (VREF). Particularly, LYS increased the permeability of biofilms of MRSA 33 and exhibited antibiofilm activities against MRSA 31 ( inhibition rate = 38.1 % ) and MRSE 61 ( inhibition rate = 46.6 % ). The combinations of PIP/SBT+LYS, AMK+LYS, and LZD+LYS showed stronger antibiofilm activities against MRSA 62, MRSE 62, MRSE 63, and VREF 11. Conclusion. The antimicrobial and antibiofilm activities of LYS against MRSA were better than AZM, while that of LYS against MRSE and VREF, respectively, was similar with AZM and LVX.

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“…Since it has recently been demonstrated that bacteria can develop resistance to AMPs and that their combined use allows to delay the evolution of pathogen resistance [ 8 , 9 ], the use of combined forms of lactoferrin-derived AMPs seems to be the most appropriate way to avoid the development of resistance. Such combinations can be based not only on AMPs or antibiotics [ 43 , 44 ], but also on enzymes that are active against different G(+) and G(−) bacteria [ 45 , 46 , 47 ]. In vitro studies of the combined use of various AMPs derived from human and bovine lactoferrin with traditional antibiotics revealed the presence of a synergistic effect between polypeptides and antibiotics; however, the obtained results were insufficient to produce therapeutic effects in vivo [ 48 ].…”

Section: Discussionmentioning

confidence: 99%

Synergistic Antimicrobial Action of Lactoferrin-Derived Peptides and Quorum Quenching Enzymes

Aslanli

Domnin

Stepanov

et al. 2023

IJMS

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Combined use of various antimicrobial peptides (AMPs) with enzymes that hydrolyze the signaling molecules of the resistance mechanism of various microorganisms, quorum sensing (QS), to obtain effective antimicrobials is one of the leading approaches in solving the antimicrobial resistance problem. Our study investigates the lactoferrin-derived AMPs, lactoferricin (Lfcin), lactoferampin and Lf(1-11), as potential partners for combination with enzymes hydrolyzing lactone-containing QS molecules, the hexahistidine-containing organophosphorus hydrolase (His6-OPH) and penicillin acylase, to obtain effective antimicrobial agents with a scope of practical application. The possibility of the effective combination of selected AMPs and enzymes was first investigated in silico using molecular docking method. Based on the computationally obtained results, His6-OPH/Lfcin combination was selected as the most suitable for further research. The study of physical–chemical characteristics of His6-OPH/Lfcin combination revealed the stabilization of enzymatic activity. A notable increase in the catalytic efficiency of action of His6-OPH in combination with Lfcin in the hydrolysis of paraoxon, N-(3-oxo-dodecanoyl)-homoserine lactone and zearalenone used as substrates was established. Antimicrobial efficiency of His6-OPH/Lfcin combination was determined against various microorganisms (bacteria and yeasts) and its improvement was observed as compared to AMP without enzyme. Thus, our findings demonstrate that His6-OPH/Lfcin combination is a promising antimicrobial agent for practical application.

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Nonclassical antagonism between human lysozyme and AMPs against Pseudomonas aeruginosa

Cited by 6 publications

References 38 publications

Applications of Lysozyme, an Innate Immune Defense Factor, as an Alternative Antibiotic

Applications of Lysozyme, an Innate Immune Defense Factor, as an Alternative Antibiotic

The In Vitro Antimicrobial and Antibiofilm Activities of Lysozyme against Gram-Positive Bacteria

Synergistic Antimicrobial Action of Lactoferrin-Derived Peptides and Quorum Quenching Enzymes

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