Antifungal and antibacterial functions of medicinal leech recombinant destabilase-lysozyme and its heated-up derivative

Yudina, T.G.; Guo, Deyin; Piskunkova, N. F.; Павлова, И.Б.; Zavalova, L. L.; Baskova, I. P.

doi:10.1007/s11705-012-1277-2

Cited by 10 publications

(8 citation statements)

References 13 publications

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“…lys25 is up-regulated in the intestinal cells of C. elegans on pathogen infection (Mallo et al, 2002). Dest-lys is up-regulated on bacterial infection in C. elegans (Irazoqui et al, 2010), and is also known for its antifungal properties (Yudina et al, 2012;Zavalova et al, 2006). In addition, several lectins are involved in the innate immune system against bacteria.…”

Section: Discussionmentioning

confidence: 99%

Analysis of the transcriptome of Hirschmanniella oryzae to explore potential survival strategies and host–nematode interactions

Bauters

Haegeman

Kyndt

et al. 2013

Molecular Plant Pathology

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The rice root nematode Hirschmanniella oryzae is the most abundant plant-parasitic nematode in flooded rice fields and is distributed world-wide. Although it is economically less important than sedentary nematodes, it can cause severe yield reductions and economic losses in specific environmental conditions. No transcriptome data for this genus were available until now. We have performed 454 sequencing on a mixed life stages population to gain an insight into nematode-plant interactions and nematode survival strategies. The results of two assembly strategies were combined to reduce the redundancy of the data, generating a final dataset of 21 360 contigs. The data were screened for putative plant cell wall-modifying proteins, which facilitate nematode migration through host roots. A β-mannanase, previously not reported in nematodes, was detected in the dataset. The data were screened for putative effector proteins that may alter the host defence mechanism. Two enzymes, chorismate mutase and isochorismatase, thought to be involved in the salicyclic acid pathway, were identified. Experimental treatments of H. oryzae with artificial seawater showed that late embryogenesis abundant (LEA) proteins and SXP/RAL-2 are induced, suggesting that these proteins are involved in the process of anhydrobiosis. The newly generated data can highlight potential differences between sedentary and migratory nematodes, and will be useful in the further study of host-nematode interactions and the developmental biology of this nematode.

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Section: Discussionmentioning

confidence: 99%

Analysis of the transcriptome of Hirschmanniella oryzae to explore potential survival strategies and host–nematode interactions

Bauters

Haegeman

Kyndt

et al. 2013

Molecular Plant Pathology

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“…It attracts interest because it also shows thrombolytic activity through the lysis of the bonds ε-(γ-Glu)-Lys present in fibrin. For these reasons, its recombinant isoforms [ 53 ] and antifungal activity [ 54 ] have been studied.…”

Section: Sourcesmentioning

confidence: 99%

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

Ferraboschi

Ciceri

Grisenti³

2021

Antibiotics

207

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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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“…These values were similar for all mlDL isoforms: for lytic activity—pH 4.5–10 and I = 0–0.4 M, for isopeptidase activity—pH 4.5–7.5 and I = 0–0.1 M. For muramidase activity mlDL had two ranges: pH 2.5–3 and I = 0–0.25 M, pH 4.5–12 and I = 0–0.05 M. This information allows us to suggest the similarity of their enzymatic properties. Previous studies have demonstrated the antimicrobial activity of heat-inactivated mlDL [ 19 ]. This antimicrobial effect was also observed with synthetic amphipathic fragments of mlDL [ 18 ].…”

Section: Discussionmentioning

confidence: 99%

“…The muramidase activity of destabilase was demonstrated by the cell wall disruption of Мicrococcus lysodeikticus [ 16 ]. At the same time, this enzyme with heat-inactivated muramidase activity still exhibited high antimicrobial activity against not only bacteria but also yeasts, fungi, and archaea [ 13 , 18 , 19 ]. It has also been shown that synthetic amphipathic fragments of the destabilase possess antimicrobial activity [ 18 ].…”

Section: Introductionmentioning

confidence: 99%

A comparison of the enzymatic properties of three recombinant isoforms of thrombolytic and antibacterial protein—Destabilase-Lysozyme from medicinal leech

et al. 2015

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BackgroundDestabilase-Lysozyme (mlDL) is a multifunctional i-type enzyme that has been found in the secretions from the salivary glands of medicinal leeches. mlDL has been shown to exhibit isopeptidase, muramidase and antibacterial activity. This enzyme attracts interest because it expresses thrombolytic activity through isopeptidolysis of the ε-(γ-Glu)-Lys bonds that cross-link polypeptide chains in stabilised fibrin. To date, three isoforms of mlDL have been identified.The enzymatic properties of pure mlDL isoforms have not yet been described because only destabilase complexes containing other proteins could be isolated from the salivary gland secretion and because low product yield from the generation of recombinant proteins has made comprehensive testing difficult.ResultsIn the present study, we optimised the procedures related to the expression, isolation and purification of active mlDL isoforms (mlDL-Ds1, mlDL-Ds2, mlDL-Ds3) using an Escherichia coli expression system, and we detected and compared their muramidase, lytic, isopeptidase and antimicrobial activities. After optimisation, the product yield was 30 mg per litre of culture. The data obtained in our study led to the suggestion that the recombinant mlDL isoforms isolated from inclusion bodies form stable oligomeric complexes. Analyses of the tested activities revealed that all isoforms exhibited almost identical patterns of pH and ionic strength effects on the activities. We determined that mlDL-Ds1, 2, 3 possessed non-enzymatic antibacterial activity independent of their muramidase activity. For the first time, we demonstrated the fibrinolytic activity of the recombinant mlDL and showed that only intact proteins possessed this activity, suggesting their enzymatic nature.ConclusionsThe recombinant Destabilase-Lysozyme isoforms obtained in our study may be considered potential thrombolytic agents that act through a mechanism different from that of common thrombolytics.Electronic supplementary materialThe online version of this article (doi:10.1186/s12858-015-0056-3) contains supplementary material, which is available to authorized users.

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Antifungal and antibacterial functions of medicinal leech recombinant destabilase-lysozyme and its heated-up derivative

Cited by 10 publications

References 13 publications

Analysis of the transcriptome of Hirschmanniella oryzae to explore potential survival strategies and host–nematode interactions

Analysis of the transcriptome of Hirschmanniella oryzae to explore potential survival strategies and host–nematode interactions

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

A comparison of the enzymatic properties of three recombinant isoforms of thrombolytic and antibacterial protein—Destabilase-Lysozyme from medicinal leech

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