Relevant bibliographies by topics / Endolysins

Academic literature on the topic 'Endolysins'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Endolysins"

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Gontijo, Marco Túlio Pardini, Genesy Perez Jorge, and Marcelo Brocchi. "Current Status of Endolysin-Based Treatments against Gram-Negative Bacteria." Antibiotics 10, no. 10 (September 22, 2021): 1143. http://dx.doi.org/10.3390/antibiotics10101143.

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The prevalence of multidrug-resistant Gram-negative bacteria is a public health concern. Bacteriophages and bacteriophage-derived lytic enzymes have been studied in response to the emergence of multidrug-resistant bacteria. The availability of tRNAs and endolysin toxicity during recombinant protein expression is circumvented by codon optimization and lower expression levels using inducible pET-type plasmids and controlled cultivation conditions, respectively. The use of polyhistidine tags facilitates endolysin purification and alters antimicrobial activity. Outer membrane permeabilizers, such as organic acids, act synergistically with endolysins, but some endolysins permeate the outer membrane of Gram-negative bacteria per se. However, the outer membrane permeation mechanisms of endolysins remain unclear. Other strategies, such as the co-administration of endolysins with polymyxins, silver nanoparticles, and liposomes confer additional outer membrane permeation. Engineered endolysins comprising domains for outer membrane permeation is also a strategy used to overcome the current challenges on the control of multidrug-resistant Gram-negative bacteria. Metagenomics is a new strategy for screening endolysins with interesting antimicrobial properties from uncultured phage genomes. Here, we review the current state of the art on the heterologous expression of endolysin, showing the potential of bacteriophage endolysins in controlling bacterial infections.
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Chang, Yoonjee. "Bacteriophage-Derived Endolysins Applied as Potent Biocontrol Agents to Enhance Food Safety." Microorganisms 8, no. 5 (May 13, 2020): 724. http://dx.doi.org/10.3390/microorganisms8050724.

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Endolysins, bacteriophage-encoded enzymes, have emerged as antibacterial agents that can be actively applied in food processing systems as food preservatives to control pathogens and ultimately enhance food safety. Endolysins break down bacterial peptidoglycan structures at the terminal step of the phage reproduction cycle to enable phage progeny release. In particular, endolysin treatment is a novel strategy for controlling antibiotic-resistant bacteria, which are a severe and increasingly frequent problem in the food industry. In addition, endolysins can eliminate biofilms on the surfaces of utensils. Furthermore, the cell wall-binding domain of endolysins can be used as a tool for rapidly detecting pathogens. Research to extend the use of endolysins toward Gram-negative bacteria is now being extensively conducted. This review summarizes the trends in endolysin research to date and discusses the future applications of these enzymes as novel food preservation tools in the field of food safety.
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Son, Bokyung, Minsuk Kong, Yoyeon Cha, Jaewoo Bai, and Sangryeol Ryu. "Simultaneous Control of Staphylococcus aureus and Bacillus cereus Using a Hybrid Endolysin LysB4EAD-LysSA11." Antibiotics 9, no. 12 (December 14, 2020): 906. http://dx.doi.org/10.3390/antibiotics9120906.

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Bacteriophage endolysins have attracted attention as promising alternatives to antibiotics, and their modular structure facilitates endolysin engineering to develop novel endolysins with enhanced versatility. Here, we constructed hybrid proteins consisting of two different endolysins for simultaneous control of two critical foodborne pathogens, Staphylococcus aureus and Bacillus cereus. The full-length or enzymatically active domain (EAD) of LysB4, an endolysin from the B. cereus-infecting phage B4, was fused to LysSA11, an endolysin of the S. aureus-infecting phage SA11, via a helical linker in both orientations. The hybrid proteins maintained the lytic activity of their parental endolysins against both S. aureus and B. cereus, but they showed an extended antimicrobial spectrum. Among them, the EAD of LysB4 fused with LysSA11 (LysB4EAD-LyaSA11) showed significantly increased thermal stability compared to its parental endolysins. LysB4EAD-LysSA11 exhibited high lytic activity at pH 8.0–9.0 against S. aureus and at pH 5.0–10.0 against B. cereus, but the lytic activity of the protein decreased in the presence of NaCl. In boiled rice, treatment with 3.0 µM of LysB4EAD-LysSA11 reduced the number of S. aureus and B. cereus to undetectable levels within 2 h and also showed superior antimicrobial activity to LyB4EAD and LysSA11 in combination. These results suggest that LysB4EAD-LysSA11 could be a potent antimicrobial agent for simultaneous control of S. aureus and B. cereus.
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Love, Michael J., David Coombes, Sarah H. Manners, Gayan S. Abeysekera, Craig Billington, and Renwick C. J. Dobson. "The Molecular Basis for Escherichia coli O157:H7 Phage FAHEc1 Endolysin Function and Protein Engineering to Increase Thermal Stability." Viruses 13, no. 6 (June 9, 2021): 1101. http://dx.doi.org/10.3390/v13061101.

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Bacteriophage-encoded endolysins have been identified as antibacterial candidates. However, the development of endolysins as mainstream antibacterial agents first requires a comprehensive biochemical understanding. This study defines the atomic structure and enzymatic function of Escherichia coli O157:H7 phage FAHEc1 endolysin, LysF1. Bioinformatic analysis suggests this endolysin belongs to the T4 Lysozyme (T4L)-like family of proteins and contains a highly conserved catalytic triad. We then solved the structure of LysF1 with x-ray crystallography to 1.71 Å. LysF1 was confirmed to exist as a monomer in solution by sedimentation velocity experiments. The protein architecture of LysF1 is conserved between T4L and related endolysins. Comparative analysis with related endolysins shows that the spatial orientation of the catalytic triad is conserved, suggesting the catalytic mechanism of peptidoglycan degradation is the same as that of T4L. Differences in the sequence illustrate the role coevolution may have in the evolution of this fold. We also demonstrate that by mutating a single residue within the hydrophobic core, the thermal stability of LysF1 can be increased by 9.4 °C without compromising enzymatic activity. Overall, the characterization of LysF1 provides further insight into the T4L-like class of endolysins. Our study will help advance the development of related endolysins as antibacterial agents, as rational engineering will rely on understanding mutable positions within this protein fold.
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Swift, Steven M., Kevin P. Reid, David M. Donovan, and Timothy G. Ramsay. "Thermophile Lytic Enzyme Fusion Proteins that Target Clostridium perfringens." Antibiotics 8, no. 4 (November 8, 2019): 214. http://dx.doi.org/10.3390/antibiotics8040214.

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Clostridium perfringens is a bacterial pathogen that causes necrotic enteritis in poultry and livestock, and is a source of food poisoning and gas gangrene in humans. As the agriculture industry eliminates the use of antibiotics in animal feed, alternatives to antibiotics will be needed. Bacteriophage endolysins are enzymes used by the virus to burst their bacterial host, releasing bacteriophage particles. This type of enzyme represents a potential replacement for antibiotics controlling C. perfringens. As animal feed is often heat-treated during production of feed pellets, thermostable enzymes would be preferred for use in feed. To create thermostable endolysins that target C. perfringens, thermophile endolysin catalytic domains were fused to cell wall binding domains from different C. perfringens prophage endolysins. Three thermostable catalytic domains were used, two from prophage endolysins from two Geobacillus strains, and a third endolysin from the deep-sea thermophilic bacteriophage Geobacillus virus E2 (GVE2). These domains harbor predicted L-alanine-amidase, glucosaminidase, and L-alanine-amidase activities, respectively and degrade the peptidoglycan of the bacterial cell wall. The cell wall binding domains were from C. perfringens prophage endolysins (Phage LYtic enzymes; Ply): PlyCP18, PlyCP10, PlyCP33, PlyCP41, and PlyCP26F. The resulting fifteen chimeric proteins were more thermostable than the native C. perfringens endolysins, and killed swine and poultry disease-associated strains of C. perfringens.
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Rodríguez-Rubio, Lorena, Hans Gerstmans, Simon Thorpe, Stéphane Mesnage, Rob Lavigne, and Yves Briers. "DUF3380 Domain from a Salmonella Phage Endolysin Shows PotentN-Acetylmuramidase Activity." Applied and Environmental Microbiology 82, no. 16 (June 10, 2016): 4975–81. http://dx.doi.org/10.1128/aem.00446-16.

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ABSTRACTBacteriophage-encoded endolysins are highly diverse enzymes that cleave the bacterial peptidoglycan layer. Current research focuses on their potential applications in medicine, in food conservation, and as biotechnological tools. Despite the wealth of applications relying on the use of endolysin, little is known about the enzymatic properties of these enzymes, especially in the case of endolysins of bacteriophages infecting Gram-negative species. Automated genome annotations therefore remain to be confirmed. Here, we report the biochemical analysis and cleavage site determination of a novelSalmonellabacteriophage endolysin, Gp110, which comprises an uncharacterizeddomain ofunknownfunction (DUF3380; pfam11860) in its C terminus and shows a higher specific activity (34,240 U/μM) than that of 14 previously characterized endolysins active against peptidoglycan from Gram-negative bacteria (corresponding to 1.7- to 364-fold higher activity). Gp110 is a modular endolysin with an optimal pH of enzymatic activity of pH 8 and elevated thermal resistance. Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis coupled to mass spectrometry showed that DUF3380 hasN-acetylmuramidase (lysozyme) activity cleaving the β-(1,4) glycosidic bond betweenN-acetylmuramic acid andN-acetylglucosamine residues. Gp110 is active against directly cross-linked peptidoglycans with various peptide stem compositions, making it an attractive enzyme for developing novel antimicrobial agents.IMPORTANCEWe report the functional and biochemical characterization of theSalmonellaphage endolysin Gp110. This endolysin has a modular structure with an enzymatically active domain and a cell wall binding domain. The enzymatic activity of this endolysin exceeds that of all other endolysins previously characterized using the same methods. A domain of unknown function (DUF3380) is responsible for this high enzymatic activity. We report that DUF3380 hasN-acetylmuramidase activity against directly cross-linked peptidoglycans with various peptide stem compositions. This experimentally verified activity allows better classification and understanding of the enzymatic activities of endolysins, which mostly are inferred by sequence similarities. Three-dimensional structure predictions for Gp110 suggest a fold that is completely different from that of known structures of enzymes with the same peptidoglycan cleavage specificity, making this endolysin quite unique. All of these features, combined with increased thermal resistance, make Gp110 an attractive candidate for engineering novel endolysin-based antibacterials.
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Kuty, Gabriel F., Min Xu, Douglas K. Struck, Elizabeth J. Summer, and Ry Young. "Regulation of a Phage Endolysin by Disulfide Caging." Journal of Bacteriology 192, no. 21 (September 10, 2010): 5682–87. http://dx.doi.org/10.1128/jb.00674-10.

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ABSTRACT In contrast to canonical phage endolysins, which require holin-mediated disruption of the membrane to gain access to attack the cell wall, signal anchor release (SAR) endolysins are secreted by the host sec system, where they accumulate in an inactive form tethered to the membrane by their N-terminal SAR domains. SAR endolysins become activated by various mechanisms upon release from the membrane. In its inactive form, the prototype SAR endolysin, LyzP1, of coliphage P1, has an active-site Cys covalently blocked by a disulfide bond; activation involves a disulfide bond isomerization driven by a thiol in the newly released SAR domain, unblocking the active-site Cys. Here, we report that Lyz103, the endolysin of Erwinia phage ERA103, is also a SAR endolysin. Although Lyz103 does not have a catalytic Cys, genetic evidence suggests that it also is activated by a thiol-disulfide isomerization triggered by a thiol in the SAR domain. In this case, the inhibitory disulfide in nascent Lyz103 is formed between cysteine residues flanking a catalytic glutamate, caging the active site. Thus, LyzP1 and Lyz103 define subclasses of SAR endolysins that differ in the nature of their inhibitory disulfide, and Lyz103 is the first enzyme found to be regulated by disulfide bond caging of its active site.
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Murray, Ellen, Lorraine A. Draper, R. Paul Ross, and Colin Hill. "The Advantages and Challenges of Using Endolysins in a Clinical Setting." Viruses 13, no. 4 (April 15, 2021): 680. http://dx.doi.org/10.3390/v13040680.

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Antibiotic-resistant pathogens are increasingly more prevalent and problematic. Traditional antibiotics are no longer a viable option for dealing with these multidrug-resistant microbes and so new approaches are needed. Bacteriophage-derived proteins such as endolysins could offer one effective solution. Endolysins are bacteriophage-encoded peptidoglycan hydrolases that act to lyse bacterial cells by targeting their cell’s wall, particularly in Gram-positive bacteria due to their naturally exposed peptidoglycan layer. These lytic enzymes have received much interest from the scientific community in recent years for their specificity, mode of action, potential for engineering, and lack of resistance mechanisms. Over the past decade, a renewed interest in endolysin therapy has led to a number of successful applications. Recombinant endolysins have been shown to be effective against prominent pathogens such as MRSA, Listeria monocytogenes, Staphylococcus strains in biofilm formation, and Pseudomonas aeruginosa. Endolysins have also been studied in combination with other antimicrobials, giving a synergistic effect. Although endolysin therapy comes with some regulatory and logistical hurdles, the future looks promising, with the emergence of engineered “next-generation” lysins. This review will focus on the likelihood that endolysins will become a viable new antimicrobial therapy and the challenges that may have to be overcome along the way.
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Gerstmans, Hans, Lorena Rodríguez-Rubio, Rob Lavigne, and Yves Briers. "From endolysins to Artilysin®s: novel enzyme-based approaches to kill drug-resistant bacteria." Biochemical Society Transactions 44, no. 1 (February 9, 2016): 123–28. http://dx.doi.org/10.1042/bst20150192.

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One of the last untapped reservoirs in nature for the identification of new anti-microbials is bacteriophages, the natural killers of bacteria. Lytic bacteriophages encode peptidoglycan (PG) lytic enzymes able to degrade the PG layer in different steps of their infection cycle. Endolysins degrade the bacterial cell wall at the end of the infection cycle, causing lysis of the host to release the viral progeny. Recombinant endolysins have been successfully applied as anti-bacterial agent against antibiotic-resistant Gram-positive pathogens. This has boosted the study of these enzymes as new anti-microbials in different fields (e.g. medical, food technology). A key example is the recent development of endolysin-based anti-bacterials against Gram-negative pathogens in which the exogenous application of endolysins is hindered by the outer membrane (OM). These novel anti-microbials, termed Artilysin®s, are able to pass through the OM and reach the PG where they exert their action. In addition, mycobacteria whose cell wall is structurally different from both Gram-positive and Gram-negative bacteria have also been reported to be inhibited by mycobacteriophage-encoded endolysins. Endolysins and endolysin-based anti-microbials can be considered as ideal candidates for an alternative to antibiotics for several reasons: (1) their unique mode of action and activity against bacterial persisters (independent of an active host metabolism), (2) their selective activity against both Gram-positive and Gram-negative pathogens (including antibiotic resistant strains) and mycobacteria, (3) the limited resistance development reported so far. The present review summarizes and discusses the potential applications of endolysins as new anti-microbials.
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Wu, Zhifeng, Yang Zhang, Xinyang Xu, Temoor Ahmed, Yong Yang, Belinda Loh, Sebastian Leptihn, Chenqi Yan, Jianping Chen, and Bin Li. "The Holin-Endolysin Lysis System of the OP2-Like Phage X2 Infecting Xanthomonas oryzae pv. oryzae." Viruses 13, no. 10 (September 28, 2021): 1949. http://dx.doi.org/10.3390/v13101949.

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Most endolysins of dsDNA phages are exported by a holin-dependent mechanism, while in some cases endolysins are exported via a holin-independent mechanism. However, it is still unclear whether the same endolysins can be exported by both holin-dependent and holin-independent mechanisms. This study investigated the lysis system of OP2-like phage X2 infecting Xanthomonas oryzae pv. oryzae, causing devastating bacterial leaf blight disease in rice. Based on bioinformatics and protein biochemistry methods, we show that phage X2 employs the classic "holin-endolysin" lysis system. The endolysin acts on the cell envelope and exhibits antibacterial effects in vitro, while the holin facilitates the release of the protein into the periplasm. We also characterized the role of the transmembrane domain (TMD) in the translocation of the endolysin across the inner membrane. We found that the TMD facilitated the translocation of the endolysin via the Sec secretion system. The holin increases the efficiency of protein release, leading to faster and more efficient lysis. Interestingly, in E. coli, the expression of either holin or endolysin with TMDs resulted in the formation of long rod shaped cells. We conclude that the TMD of X2-Lys plays a dual role: One is the transmembrane transport while the other is the inhibition of cell division, resulting in larger cells and thus in a higher number of released viruses per cell.
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Dissertations / Theses on the topic "Endolysins"

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Schmelcher, Mathias. "Engineering of bacteriophage endolysins for detection and control of Listeria /." Zürich : ETH, 2007. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=17721.

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Settle, Lori L. "Characterization of the Bacteriophage Felix O1 Endolysin and Potential Application for Salmonella Bioremediation." Diss., Virginia Tech, 2012. http://hdl.handle.net/10919/39222.

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There is an increasing incidence of antimicrobial-resistant organisms isolated from food and food products. Coupled with that rising incidence is increased media scrutiny and coverage of outbreaks of foodborne illnesses. Consequently, consumers increasingly demand safer food, and that the antimicrobial measures used be other than antimicrobial drugs. A possible solution is to use bacteriophages, or the purified holin and endolysin proteins that make them lethal and lytic, as antimicrobial food treatments or additives. The bacteriophage Felix O1 is a promising candidate for development as an anti-Salmonella food treatment. This dissertation describes the work done to determine if these proteins could be of value as bioremedial agents. Endolysin treatments of Gram negative bacteria require two agents: the lytic endolysin, and a second agent to permeabilize the outer membrane of the bacterium. The holin protein was proposed as an outer membrane permeabilization agent. Methods used to locate the holin gene included BLAST analysis, analysis of putative Felix O1 proteins for transmembrane domains, and examination of the lysin sequence for an N-terminal signal sequence. Analyses did not reveal a promising candidate. Cloning of rIIA as a potential holin was attempted without success. Results of various analyses are discussed, as are chemical alternatives to the use of purified holin as a permeabilization agent. The endolysin, LysO1, was successfully cloned and characterized. PHYRE analysis predicted that the enzyme structure is composed of α helices arranged into two lobes, with the active site in a cleft between them. The enzyme lysed all tested strains of Salmonella and a tested strain of the foodborne pathogen Escherichia coli. Campylobacter jejuni susceptibility remains ambiguous, and the enzyme had no effect on Listeria monocytogenes or Micrococcus luteus. LysO1 was most active at alkaline pH and low ionic strength; optimal activity was observed in 25 mM buffer at pH 10. If removed from frozen storage, the enzyme was most thermostable at 30 °C. Lytic activity was adversely affected by the presence of the divalent cations calcium, magnesium, and zinc, and by high ionic strength. Considerable time was devoted to development of the activity assay used to further characterize the enzyme, and details of those experiments are provided. Logical extensions of the research project, such as further characterization and testing needed to obtain government approval for widespread use of the treatment, and possible pursuit of treatment based on an enzyme derivative such as an antimicrobial peptide, are discussed.
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Forchheim, Michael. "Isolierung und Optimierung antimikrobiell wirkender Phagenproteine zur Bekämpfung antibiotikaresistenter Staphylokokken." kostenfrei, 2009. http://www.opus-bayern.de/uni-regensburg/volltexte/2009/1343/.

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Xu, Min. "Bacteriophage P1: a new paradigm for control of phage lysis." Texas A&M University, 2004. http://hdl.handle.net/1969.1/2734.

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The N-terminal hydrophobic domain of the phage P1 endolysin Lyz was found to facilitate the export of Lyz in a sec-dependent fashion, explaining the ability of Lyz to cause lysis of E.coli in the absence of the P1 holin. The N-terminal domain of Lyz is demonstrated to be both necessary and sufficient not only for export to the membrane but also for release into the periplasm of this endolysin. We propose that this unusual N-terminal domain functions as a "signal arrest- release" (SAR) sequence, which first directs the endolysin to the periplasm in membrane-tethered form and then allows it to be released as a soluble active enzyme in the periplasm. To understand why release from the membrane is required for the physiological expression of the lytic activity of Lyz, we examined the role of its seven cysteine residues in the biogenesis of the active endolysin. The inactive, membrane-tethered and the active, soluble forms of Lyz differ in their pattern of intramolecular disulfide bonding. We conclude that the release of Lyz from the membrane leads to an intramolecular thiol-disulfide bond isomerization causing a dramatic conformational change in the Lyz protein. As a result, an active site cleft that is missing in nascent Lyz is generated in the mature form of the endolysin. Examination of the protein sequences of related bacteriophage endolysins suggests that the presence of an SAR sequence is not unique to Lyz. Studies on holin and antiholin indicated that P1 encodes two holins, LydA and LydC. The antiholin LydB inhibits LydA by binding to it directly on the membrane. All above results demonstrate a new paradigm for control of phage lysis, which is, upon depolarization of the membrane by holin function at a programmed time, endolysin is released from the bilayer leading to the immediate lysis of the host.
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Maulner, Stéphanie. "Les endolysines de Clostridium difficile : Potentiel thérapeutique pour traiter les infections à C. difficile (ICD)." Mémoire, Université de Sherbrooke, 2010. http://savoirs.usherbrooke.ca/handle/11143/4059.

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Clostridium difficile, un bacille à Gram positif anaérobie strict qui forme des spores, est un pathogène opportuniste responsable de simples diarrhées ou de colites pseudomembraneuses qui peuvent provoquer la mort. Le traitement de base réside en l'arrêt des antibiotiques qui ont détruit la flore de l'hôte et provoqué les symptômes, ou en la prescription de vancomycine et/ou de métronidazole. Malheureusement, l'efficacité de ces antibiotiques est variable et le nombre de rechutes est élevé. En outre, de plus en plus de souches deviennent résistantes aux antibiotiques. C'est pour cette raison qu'un besoin d'alternatives thérapeutiques s'est fait ressentir. Une des approches prometteuses est l'utilisation des endolysines, qui sont des enzymes hydrolytiques encodées par les bactériophages et qui se sont déjà révélées être efficaces contre plusieurs bactéries à Gram positif. Dans cette étude, nous avons démontré l'activité lytique d'endolysines encodées par des phages de Clostridium difficile sur des cellules vivantes. Différentes endolysines ont été clonées dans E. coli, exprimées et purifiées, puis leur activité a été vérifiée de plusieurs manières. Certains facteurs biochimiques propres à ces enzymes ont été étudiés, tels que les cofacteurs nécessaires pour une meilleure activité lytique, le pH optimal et le spectre d'efficacité sur différentes souches bactériennes. Finalement, l'étude de ces enzymes comme outil de diagnostic ou de biologie moléculaire est abordée. Les résultats de nos travaux indiquent que les endolysines PlyCD52 et PlyCD38-2 de C. difficile possèdent une faible activité lytique. L'activité des endolysines n'est pas influencée par les cofacteurs Tween 0,5%, Triton 0,1%, MgCl[indice inférieur 2] contrairement à l'EDTA qui inhibe celle-ci. Le pH optimum semble être compris entre 7 et 8,5 et ces enzymes agissent sur différentes souches de C. difficile à l'exception de la souche CD630. Malgré ces résultats encourageants, des travaux supplémentaires seront nécessaires afin de stabiliser les enzymes qui ont une forte tendance à précipiter et d'obtenir une meilleure activité.
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Deutsch, Stéphanie-Marie. "Lien entre lyse et lysogénie chez lactobacillus helveticus : mécanisme et impact sur l'affinage de l'emmental." Rennes, Agrocampus Ouest, 2002. http://www.theses.fr/2002NSARI028.

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Barros, Marilia Cabral do Rego. "Revealing the Structural and Molecular Basis of Retroviral Assembly and Endolysin PlyC Membrane Translocation Using Surface Plasmon Resonance and Neutron Reflectometry." Research Showcase @ CMU, 2016. http://repository.cmu.edu/dissertations/973.

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In this thesis we focus on the mechanistic understanding of two membrane mediated biological processes: retroviral assembly and endolysin PlyC plasma membrane translocation. Retroviral Gag polyprotein is the structural determinant that assembles in a protein lattice on the hosts plasma membrane to trigger formation of the viral protein/membrane shell.
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Bretfeld, Falko [Verfasser], and Reinhard [Akademischer Betreuer] Wirth. "Isolierung und Charakterisierung von Endolysinen aus Bakteriophagen gegen Enterococcus faecalis und Enterococcus faecium / Falko Bretfeld. Betreuer: Reinhard Wirth." Regensburg : Universitätsbibliothek Regensburg, 2010. http://d-nb.info/1022872745/34.

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Wittmann, Johannes [Verfasser]. "Die Endolysine von Clavibacter michiganensis-Phagen als Kandidaten für den biologischen Pflanzenschutz von Tomatenpflanzen / Johannes Wittmann. Lehrstuhl für Gentechnologie/Mikrobiologie -- Fakultät für Biologie." Bielefeld : Universitätsbibliothek Bielefeld, Hochschulschriften, 2011. http://d-nb.info/1013913000/34.

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Veloso, Pedro Miguel Azevedo. "Improving derived Listeria phage endolysins properties at low temperatures." Master's thesis, 2014. http://hdl.handle.net/1822/41826.

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Dissertação de mestrado em Bioengenharia
Listeria monocytogenes is a Gram-positive opportunistic pathogen that can grow in a wide variety of conditions and is responsible for listeriosis, a potential fatal disease, associated to the ingestion of contaminated food. The concerns about the upsurge of widespread reported cases, combined with emerging antibiotic-resistance amongst pathogenic bacteria, such as L. monocytogenes, demand for the development of novel preservation techniques that ensure the safety of food products. Endolysins, which originate from virulent bacteriophages, are responsible for the hydrolysis of the covalent bonds in peptidoglycan layer of the host cell. These enzyme properties represents a good alternatively approach against Gram-positive foodborne pathogens without altering the organoleptic properties of food products. However, in most of the cases, the activity and stability of naturally occurring enzymes is significantly lower than the biotechnological industry needs. Besides, there is a lack of research advances in lytic activity improvements of endolysins in food storage conditions. The experimental work developed in the scope of this thesis aimed at directing endolysin activity towards refrigeration temperatures against L. monocytogenes through the use of directed evolution strategies – error-prone PCR and cryodrilling. Different attempts were done for the isolation of listerial phages from livestock industries effluents and consequently identification and improvement of lytic activity of its derived endolysins. An in silico analysis of two different lysins – Ply500 and Ply511 – were performed to provide contextualization about their structure and domains. Although both proteins possess modular structure, Ply511 has a central catalytic domain and a not well characterized binding domain which contrasts to Ply500 domain organization. Protein expression in large and micro-scales of wild-type proteins was successfully done and confirmed by performing antibacterial tests against L. monocytogenes 5725. To enhance the activity of endolysins against L. monocytogenes cells, modified endolysins were constructed by amplifying their sequences using error-prone PCR technique and cloning into pQE-30 vector. The cloned vectors were transformed in E. coli JM109 competent cells, however no colonies were obtained. At the same time, using PlyP100 endolysin, a second approach based on the biotic interaction between phage-host at successively temperature was done to promote phage adaptation and consequently enzymatic evolution.
Listeria monocytogenes é um agente patogénico oportunista Gram-positivo, responsável por provocar listeriose, doença potencialmente mortal associada ao consumo de alimentos contaminados. A preocupação inerente à sua capacidade de sobreviver numa grande variedade de condições, o crescente número de surtos da doença e o aumento da resistência a antibióticos obrigam a que novas estratégias de conservação e preservação dos alimentos sejam desenvolvidas. Endolisinas derivadas de fagos são enzimas responsáveis pela lise das células do hospedeiro. Uma vez que não alteram as propriedades organoléticas dos alimentos, o uso destas enzimas representa uma boa alternativa na eliminação de agentes patogénicos Gram-positivos. Contudo, a baixa atividade e estabilidade das enzimas no seu estado natural torna-se incompatível com as necessidades industriais. Este trabalho experimental visou o melhoramento das propriedades líticas das endolisinas a temperaturas de refrigeração recorrendo a técnicas de evolução direta – error-prone PCR e cryodrilling. Numa primeira abordagem foram efectuadas tentativas para o isolamento de fagos de Listeria a partir de efluentes de indústria pecuária com posterior identificação e melhoramento das propriedades líticas das respetivas endolisinas. No entanto, as tentativas não foram bem-sucedidas. Foi efetuada a análise bioinformática das duas diferentes endolisinas – Ply500 and Ply511 – para se obter informações precisas sobre a sua estrutura. Apesar das duas proteínas possuírem uma estrutura modular, Ply511 apresenta um domínio catalítico central com função desconhecida e por conseguinte, pouco caracterizado, relativamente à organização modular de Ply500. A expressão das respetivas endolisinas wild-type em larga e micro escalas foi efetuada com sucesso e confirmada através de testes antibacterianos contra L. monocytogenes 5725. Para melhorar a atividade lítica das respetivas endolisinas, as sequências foram amplificadas por error-prone PCR, clonadas no vetor pQE-30 e transformados em células competentes E. coli JM109. No entanto, não foram obtidas quaisquer colónias. Ao mesmo tempo, usando a endolisina PlyP100, uma nova abordagem baseada no princípio de interação biótica entre fago-hospedeiro, foi efetuada a temperaturas sucessivamente mais baixas de forma a promover a evolução/adaptação do fago e consequentemente da endolisina.
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Book chapters on the topic "Endolysins"

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Heselpoth, Ryan D., Steven M. Swift, Sara B. Linden, Michael S. Mitchell, and Daniel C. Nelson. "Enzybiotics: Endolysins and Bacteriocins." In Bacteriophages, 1–42. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-40598-8_34-1.

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Heselpoth, Ryan D., Steven M. Swift, Sara B. Linden, Michael S. Mitchell, and Daniel C. Nelson. "Enzybiotics: Endolysins and Bacteriocins." In Bacteriophages, 989–1030. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-319-41986-2_34.

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Gondil, Vijay Singh, Fazal Mehmood Khan, Nancy Mehra, Deepak Kumar, Aastha Khullar, Tanvi Sharma, Abhishek Sharma, Rahul Mehta, and Hang Yang. "Clinical Potential of Bacteriophage and Endolysin Based Therapeutics: A Futuristic Approach." In Microorganisms for Sustainability, 39–58. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-1947-2_3.

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Nelson, Daniel C., Mathias Schmelcher, Lorena Rodriguez-Rubio, Jochen Klumpp, David G. Pritchard, Shengli Dong, and David M. Donovan. "Endolysins as Antimicrobials." In Advances in Virus Research, 299–365. Elsevier, 2012. http://dx.doi.org/10.1016/b978-0-12-394438-2.00007-4.

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Sanz-Gaitero, Marta, and Mark J. van Raaij. "Crystallographic Structure Determination of Bacteriophage Endolysins." In Bacterial Viruses: Exploitation for Biocontrol and Therapeutics. Caister Academic Press, 2020. http://dx.doi.org/10.21775/9781913652517.13.

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Ulrich Picoli, Simone, Nicole Mariele Santos Röhnelt, and Tiago Sfredo Schenkel. "Bacteriophages as Anti-Methicillin Resistant Staphylococcus aureus Agents." In Staphylococcus aureus [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.98313.

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Abstract:
Staphylococcus aureus is a colonizing microorganism of the nasal region of both humans and animals and represents an important opportunistic pathogen. The acquisition of the mecA and mecC genes by S. aureus led to the emergence of methicillin resistance (MRSA), becoming a public health problem in both human and animal areas. In addition to resistance to β-lactam antibiotics, MRSA strains have multidrug resistance to antimicrobials, significantly limiting therapeutic options, making it crucial to have effective alternatives for treating staphylococcal infections. In this context, the use of lytic bacteriophages, which are viruses that infect and lyse bacteria, as well as the use of their by-products, such as endolysins, has shown potential in the control of S. aureus, including MRSA. Due to the specificity of bacteriophages to infect particular prokaryotic hosts, these viruses represent an antibacterial resource for the control of public health relevant microorganisms, especially antibiotic-resistant bacteria.
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"Endolysin." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 604. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_5302.

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Conference papers on the topic "Endolysins"

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Bałdysz, Sophia, and Jakub Barylski. "Lyse with Class – classification of endolysins through machine learning." In 1st International PhD Student’s Conference at the University of Life Sciences in Lublin, Poland: ENVIRONMENT – PLANT – ANIMAL – PRODUCT. Publishing House of The University of Life Sciences in Lublin, 2022. http://dx.doi.org/10.24326/icdsupl1.t023.

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Liu, Shan-Na, Timo M. Takala, Justus Reunanen, Ossian Saris, and Per E. J. Saris. "Investigation of Listeria Phage Endolysin Cell-wall Binding Domain (CBD) Surface Display in Escherichia coli." In The International Conference on Biological Sciences and Technology. Paris, France: Atlantis Press, 2016. http://dx.doi.org/10.2991/bst-16.2016.6.

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