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Peng Luo, Long Yun, Yingying Li, Yushun Tian, Qiuting Liu, Wen Huang, Chaoqun Hu
BACKGROUND: Biocontrol of bacterial pathogens by bacteriophages (phages) represents a promising strategy. Vibrio alginolyticus, a gram-negative bacterium, is a notorious pathogen responsible for the loss of economically important farmed marine animals. To date, few V. alginolyticus phages have been successfully isolated, and only three complete genome sequences of them have been released. The limited available phage resources and poor genomic data hamper research on V. alginolyticus phages and their applications for the biocontrol of V...
October 11, 2018: BMC Genomics
Xia Wu, Keith Fraser, Jian Zha, Jonathan S Dordick
Chemical linkers are frequently used in enzyme immobilization to improve enzyme flexibility and activity, while peptide linkers, although ubiquitous in protein engineering, are much less explored in enzyme immobilization. Here, we report peptide linker-assisted non-covalent immobilization of the bacteriolytic enzyme lysostaphin (Lst) to generate anti-Staphylococcus aureus surfaces. Lst was immobilized through affinity tags onto a silica surface (glass slides) and nickel nitrolotriacetic acid (NiNTA) agarose beads via silica-binding peptides (SiBPs) or a hexahistidine tag (His-tag) fused at the C-terminus of Lst, respectively...
October 3, 2018: ACS Applied Materials & Interfaces
Patricia Letrado, Bruno Corsini, Roberto Díez-Martínez, Noemí Bustamante, José E Yuste, Pedro García
AIM: To test the synergistic effect of Cpl-711 endolysin and antibiotics for antipneumococcal activity. MATERIALS & METHODS: A combination of Cpl-711 and different antibiotics (amoxicillin, cefotaxime, levofloxacin and vancomycin) was tested in a checkerboard assay against several multidrug-resistant Streptococcus pneumoniae strains. Mouse and zebrafish models of pneumococcal sepsis were used to confirm the in vitro data. RESULTS: The activity of Cpl-711 combined with amoxicillin or cefotaxime was synergistic in the bactericidal effect against a serotype 23F multiresistant clinical isolate of S...
September 2018: Future Microbiology
Sebastian S Broendum, Ashley M Buckle, Sheena McGowan
Bacteriophage-encoded endolysins can recognize and bind specific bacteria, and act to cleave the glycosidic and/or amide bonds in the peptidoglycan bacterial cell wall. Cleavage of the cell wall generally results in the death of the bacteria. Their utility as bacteriolytic agents could be exploited for human and veterinary medicines and as well as various biotechnological applications. As interest grows in the commercial uses of these proteins, there has been much effort to successfully employ rational design and engineering to produce endolysins with bespoke properties...
September 19, 2018: Molecular Microbiology
Rohit Kongari, Jeffrey Snowden, Joel D Berry, Ry Young
Spanins are bacteriophage lysis proteins responsible for disruption of the outer membrane, the final step of Gram-negative host lysis. The absence of spanins results in a terminal phenotype of fragile spherical cells. The phage T1 employs a unimolecular spanin gp 11 that has an N-terminal lipoylation signal and a C-terminal transmembrane domain. Upon maturation and localization, gp 11 ends up as an outer membrane lipoprotein with a C-terminal transmembrane domain embedded in the inner membrane, thus connecting both the membranes as a covalent polypeptide chain...
August 22, 2018: Journal of Virology
Yuhui Yang, Shuai Le, Wei Shen, Qian Chen, Youying Huang, Shuguang Lu, Yinling Tan, Ming Li, Fuquan Hu, Yang Li
Multidrug-resistant Pseudomonas aeruginosa is one of the most life-threatening pathogens for global health. In this regard, phage encoded lytic proteins, including endolysins and virion-associated peptidoglycan hydrolases (VAPGH), have been proposed as promising antimicrobial agents to treat P. aeruginosa . Most dsDNA phages use VAPGH to degrade peptidoglycan (PG) during infection, and endolysin to lyse the host cells at the end of lytic cycle. By contrast, dsRNA phage encodes only one lytic protein, which is located in the viral membrane to digest the PG during penetration, and also serves as an endolysin to release the phage...
2018: Frontiers in Microbiology
Nanna M C Olsen, Elowine Thiran, Tobias Hasler, Thomas Vanzieleghem, Georgios N Belibasakis, Jacques Mahillon, Martin J Loessner, Mathias Schmelcher
Staphylococcus aureus is an important pathogen and biofilm former. Biofilms cause problems in clinics and food production and are highly recalcitrant to antibiotics and sanitizers. Bacteriophage endolysins kill bacteria by degrading their cell wall and are therefore deemed promising antimicrobials and anti-biofilm agents. Depolymerases targeting polysaccharides in the extracellular matrix have been suggested as parts of a multi-enzyme approach to eradicate biofilms. The efficacy of endolysins and depolymerases against S...
August 18, 2018: Viruses
Colin Buttimer, Alan Lucid, Horst Neve, Charles M A P Franz, Jim O'Mahony, Dann Turner, Rob Lavigne, Aidan Coffey
Pectobacterium atrosepticum is a phytopathogen of economic importance as it is the causative agent of potato blackleg and soft rot. Here we describe the Pectobacterium phage vB_PatP_CB5 (abbreviated as CB5), which specifically infects the bacterium. The bacteriophage is characterized in detail and TEM micrographs indicate that it belongs to the Podoviridae family . CB5 shares significant pairwise nucleotide identity (≥80%) with P. atrosepticum phages φM1, Peat1, and PP90 and also shares common genome organization...
July 26, 2018: Viruses
Nak-Hyun Kim, Wan Beom Park, Jeong Eun Cho, Yoon Jeong Choi, Su Jin Choi, Soo Youn Jun, Chang Kyung Kang, Kyoung-Ho Song, Pyoeng Gyun Choe, Ji-Hwan Bang, Eu Suk Kim, Sang Won Park, Nam-Joong Kim, Myoung-Don Oh, Hong Bin Kim
Phages and their derivatives are increasingly being reconsidered for use in the treatment of bacterial infections due to the rising rates of antibiotic resistance. We assessed the antistaphylococcal effect of the endolysin SAL200 in combination with standard-of-care (SOC) antibiotics. The activity of SAL200 when it was combined with SOC antibiotics was assessed in vitro by checkerboard and time-kill assays and in vivo with murine bacteremia and Galleria mellonella infection models. SAL200 reduced the SOC antibiotic MICs and showed a ≥3-log10 -CFU/ml reduction of Staphylococcus aureus counts within 30 min in time-kill assays...
October 2018: Antimicrobial Agents and Chemotherapy
Casey Stamereilers, Christopher P Fajardo, Jamison K Walker, Katterinne N Mendez, Eduardo Castro-Nallar, Julianne H Grose, Sandra Hope, Philippos K Tsourkas
The antibiotic-resistant bacterium Paenibacillus larvae is the causative agent of American foulbrood (AFB), currently the most destructive bacterial disease in honeybees. Phages that infect P. larvae were isolated as early as the 1950s, but it is only in recent years that P. larvae phage genomes have been sequenced and annotated. In this study we analyze the genomes of all 48 currently sequenced P. larvae phage genomes and classify them into four clusters and a singleton. The majority of P. larvae phage genomes are in the 38⁻45 kbp range and use the cohesive ends (cos) DNA-packaging strategy, while a minority have genomes in the 50⁻55 kbp range that use the direct terminal repeat (DTR) DNA-packaging strategy...
July 19, 2018: Viruses
Steven M Swift, Jerel J Waters, D Treva Rowley, Brian B Oakley, David M Donovan
Clostridium perfringens, a spore-forming anaerobic bacterium, causes food poisoning and gas gangrene in humans, and is an agent of necrotizing enteritis in poultry, swine and cattle. Endolysins are peptidoglycan hydrolases from bacteriophage that degrade the bacterial host cell wall causing lysis and thus harbor antimicrobial therapy potential. The genes for the PlyCP10 and PlyCP41 endolysins were found in prophage regions of the genomes from Clostridium perfringens strains Cp10 and Cp41, respectively. The gene for PlyCP10 encodes a protein of 351 amino acids, while the gene for PlyCP41 encodes a protein of 335 amino acids...
July 13, 2018: FEMS Microbiology Letters
Qin Peng, Yihui Yuan
Bacillus cereus is widely distributed food-borne pathogenic bacterium. Due to the harmness to human hearth and the generation of multidrug-resistant B. cereus, it is urgent to develop novel antimicrobial agents. Phage and phage endolysin were taken as novel antimicrobial substance for their specific lytic activity against pathogenic bacteria. In this study, a Myoviridae family phage, designated as vB_BceM-HSE3, infecting the pathogenic multidrug-resistant B. cereus strain was isolated and characterized along with its endolysin...
July 14, 2018: Applied Microbiology and Biotechnology
Jie Zhang, Lu-Lu Xu, Dan Gan, Xingping Zhang
BACKGROUND: The increase in the prevalence of drug-resistant Acinetobacter baumannii is a serious public health concern, which is closely linked to the formation of biofilm. It is reported that the bacteriophage and its endolysin have a good ability to degrade biofilms. The goals of this study were to compare the ability of A. baumannii bacteriophage AB3, its endolysin AB3, and three antibiotics to degrade A. baumannii biofilm and biofilm-bound A. baumannii and to understand the antibacterial mechanism of LysAB3...
June 1, 2018: Clinical Laboratory
Mengzhe Li, Yanqiu Jin, Hong Lin, Jingxue Wang, Xiuping Jiang
Vibrio parahaemolyticus is an important foodborne pathogen that is generally transmitted via raw or undercooked seafood. Endolysins originating from bacteriophages offer a new way to control bacterial pathogens. The objectives of this study were to sequence a novel lytic V. parahaemolyticus phage VPp1 and determine the antibacterial activities of the recombinant endolysin (LysVPp1) derived from this phage. The complete VPp1 genome contained a double-stranded DNA of 50,431 bp with a total G+C content of 41.35%...
July 2018: Journal of Food Protection
Irina Etobayeva, Sara B Linden, Farhang Alem, Laith Harb, Lucas Rizkalla, Philip D Mosier, Allison A Johnson, Louise Temple, Ramin M Hakami, Daniel C Nelson
Three Bacillus bacteriophage-derived endolysins, designated PlyP56, PlyN74, and PlyTB40, were identified, cloned, purified, and characterized for their antimicrobial properties. Sequence alignment reveals these endolysins have an N-terminal enzymatically active domain (EAD) linked to a C-terminal cell wall binding domain (CBD). PlyP56 has a Peptidase_M15_4/VanY superfamily EAD with a conserved metal binding motif and displays biological dependence on divalent ions for activity. In contrast, PlyN74 and PlyTB40 have T7 lysozyme-type Amidase_2 and carboxypeptidase T-type Amidase_3 EADs, respectively, which are members of the MurNAc-LAA superfamily, but are not homologs and thus do not have a shared protein fold...
May 21, 2018: Viruses
Nina N Sykilinda, Alena Y Nikolaeva, Mikhail M Shneider, Dmitry V Mishkin, Artem A Patutin, Vladimir O Popov, Konstantin M Boyko, Natalia L Klyachko, Konstantin A Miroshnikov
Proteins that include enzymatic domain degrading the bacterial cell wall and a domain providing transport through the bacterial outer membrane are considered as prospective compounds to combat pathogenic Gram-negative bacteria. This paper presents an isolation and study of an enzyme of this class naturally encoded in the prophage region of Acinetobacter baumannii AB 5075 genome. Recombinant protein expressed in E. coli exhibits an antimicrobial activity with respect to live cultures of Gram-negative bacteria reducing the population of viable bacteria by 1...
June 6, 2018: Viruses
Iris Fernández-Ruiz, Felipe H Coutinho, Francisco Rodriguez-Valera
Bacteriophages express endolysins toward the end of their replication cycle to degrade the microbial cell wall from within, allowing viral progeny to be released. Endolysins can also degrade the prokaryotic cell wall from the outside, thus have potential to be used for biotechnological and medical purposes. Multiple endolysins have been identified within the genomes of isolated phages, but their diversity in uncultured phages has been overlooked. We used a bioinformatics pipeline to identify novel endolysins from nearly 200,000 uncultured viruses...
2018: Frontiers in Microbiology
Katharina Springer, Sandra Reuter, Mandy Knüpfer, Lukas Schmauder, Philipp-Albert Sänger, Angela Felsl, Thilo M Fuchs
Yersinia enterocolitica is a pathogen that causes gastroenteritis in humans. Because of its low-temperature-dependent insecticidal activity, it can oscillate between invertebrates and mammals as host organisms. The insecticidal activity of strain W22703 is associated with a pathogenicity island of 19 kb (Tc-PAI Ye ), which carries regulators and genes encoding the toxin complex (Tc). The island also harbors four phage-related and highly conserved genes of unknown functions, which are polycistronically transcribed...
August 15, 2018: Journal of Bacteriology
Hugo Oliveira, Carlos São-José, Joana Azeredo
Peptidoglycan degrading enzymes are of increasing interest as antibacterial agents, especially against multi-drug resistant pathogens. Herein we present a review about the biological features of virion-associated lysins and endolysins, phage-derived enzymes that have naturally evolved to compromise the bacterial peptidoglycan from without and from within, respectively. These natural features may determine the adaptability of the enzymes to kill bacteria in different environments. Endolysins are by far the most studied group of peptidoglycan-degrading enzymes, with several studies showing that they can exhibit potent antibacterial activity under specific conditions...
May 29, 2018: Viruses
Bokyung Son, Minsuk Kong, Sangryeol Ryu
In response to increasing concern over antibiotic-resistant Staphylococcus aureus , the development of novel antimicrobials has been called for, with bacteriophage endolysins having received considerable attention as alternatives to antibiotics. Most staphylococcal phage endolysins have a modular structure consisting of an N-terminal cysteine, histidine-dependent amidohydrolases/peptidase domain (CHAP), a central amidase domain, and a C-terminal cell wall binding domain (CBD). Despite extensive studies using truncated staphylococcal endolysins, the precise function of the amidase domain has not been determined...
May 25, 2018: Viruses
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