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Srinivas Suda, Des Field, Niall Barron
Antimicrobial peptides (AMPs) are natural defense compounds which are synthesized as ribosomal gene-encoded pre-peptides and produced by all living organisms. AMPs are small peptides, usually cationic and typically have hydrophobic residues which interact with cell membranes and have either a narrow or broad spectrum of biological activity. AMPs are isolated from the natural host or heterologously expressed in other hosts such as Escherichia coli. The proto-typical lantibiotic Nisin is a widely used AMP that is produced by the food-grade organism Lactococcus lactis...
2017: Methods in Molecular Biology
Marcus Lívio Varella Coelho, Andreza Freitas de Souza Duarte, Maria do Carmo de Freire Bastos
One of the biggest challenges faced presently by clinicians is the emergence of multi drug--resistant pathogens that can infect humans and animals.To control the infections caused by such pathogens the development of new drugs is required. Bacteria are a rich source of ribosomally-synthesized antimicrobial peptides known as bacteriocins, which are characterized by the presence of a self-defense immunity system. Labionin-containing lantibiotics and sactibiotics are post-translationally modified bacteriocins with peculiar features...
September 30, 2016: Current Topics in Medicinal Chemistry
Françoise Hullin-Matsuda, Asami Makino, Motohide Murate, Toshihide Kobayashi
In this mini-review, we summarize current knowledge about the lipid-binding characteristics of two types of toxins used to visualize the membrane distribution of phosphoethanolamine-containing lipid species: the glycerophospholipid, phosphatidylethanolamine (PE) and the sphingolipid, ceramide phosphoethanolamine (CPE). The lantibiotic cinnamycin and the structurally-related peptide duramycin produced by some Gram-positive bacteria were among the first toxins characterized by their specificity for PE which is widely present in animal kingdoms from bacteria to mammals...
September 28, 2016: Biochimie
Josephine C Moran, Emma L Crank, Hanaa A Ghabban, Malcolm J Horsburgh
Competitive exclusion can occur in microbial communities when, for example, an inhibitor-producing strain outcompetes its competitor for an essential nutrient or produces antimicrobial compounds that its competitor is not resistant to. Here we describe a deferred growth inhibition assay, a method for assessing the ability of one bacterium to inhibit the growth of another through the production of antimicrobial compounds or through competition for nutrients. This technique has been used to investigate the correlation of nasal isolates with the exclusion of particular species from a community...
2016: Journal of Visualized Experiments: JoVE
Juan M Palazzini, Christopher A Dunlap, Michael J Bowman, Sofía N Chulze
Bacillus subtilis RC 218 was originally isolated from wheat anthers as a potential antagonist of Fusarium graminearum, the causal agent of Fusarium head blight (FHB). It was demonstrated to have antagonist activity against the plant pathogen under in vitro and greenhouse assays. The current study extends characterizing B. subtilis RC 218 with a field study and genome sequencing. The field study demonstrated that B. subtilis RC 218 could reduce disease severity and the associated mycotoxin (deoxynivalenol) accumulation, under field conditions...
November 2016: Microbiological Research
Anja Kuthning, Patrick Durkin, Stefan Oehm, Michael G Hoesl, Nediljko Budisa, Roderich D Süssmuth
Genetic code engineering that enables reassignment of genetic codons to non-canonical amino acids (ncAAs) is a powerful strategy for enhancing ribosomally synthesized peptides and proteins with functions not commonly found in Nature. Here we report the expression of a ribosomally synthesized and post-translationally modified peptide (RiPP), the 32-mer lantibiotic lichenicidin with a canonical tryptophan (Trp) residue replaced by the ncAA L-β-(thieno[3,2-b]pyrrolyl)alanine ([3,2]Tpa) which does not sustain cell growth in the culture...
2016: Scientific Reports
Manuel Montalbán-López, Auke J van Heel, Oscar P Kuipers
As the number of new antibiotics that reach the market is decreasing and the demand for them is rising, alternative sources of novel antimicrobials are needed. Lantibiotics are potent peptide antimicrobials that are ribosomally synthesized and stabilized by post-translationally introduced lanthionine rings. Their ribosomal synthesis and enzymatic modifications provide excellent opportunities to design and engineer a large variety of novel antimicrobial compounds. The research conducted in this area demonstrates that the modularity present in both the peptidic rings as well as in the combination of promiscuous modification enzymes can be exploited to further increase the diversity of lantibiotics...
September 2, 2016: FEMS Microbiology Reviews
Abdelahhad Barbour, John Tagg, Osama K Abou-Zied, Koshy Philip
Salivaricin B is a 25 amino acid polycyclic peptide belonging to the type AII lantibiotics and first shown to be produced by Streptococcus salivarius. In this study we describe the bactericidal mode of action of salivaricin B against susceptible Gram-positive bacteria. The killing action of salivaricin B required micro-molar concentrations of lantibiotic whereas the prototype lantibiotic nisin A was shown to be potent at nano-molar levels. Unlike nisin A, salivaricin B did not induce pore formation or dissipate the membrane potential in susceptible cells...
2016: Scientific Reports
Min-Jung Kwak, Soon-Kyeong Kwon, Jae-Kyung Yoon, Ju Yeon Song, Jae-Gu Seo, Myung Jun Chung, Jihyun F Kim
Bifidobacteria, often associated with the gastrointestinal tract of animals, are well known for their roles as probiotics. Among the dozens of Bifidobacterium species, Bifidobacterium bifidum, B. breve, and B. longum are the ones most frequently isolated from the feces of infants and known to help the digestion of human milk oligosaccharides. To investigate the correlation between the metabolic properties of bifidobacteria and their phylogeny, we performed a phylogenomic analysis based on 452 core genes of forty-four completely sequenced Bifidobacterium species...
October 2016: Systematic and Applied Microbiology
Bingyue Xin, Jinshui Zheng, Hualin Liu, Junhua Li, Lifang Ruan, Donghai Peng, Muhammad Sajid, Ming Sun
Due to the rapidly increasing prevalence of multidrug-resistant bacterial strains, the need for new antimicrobial drugs to treat infections has become urgent. Bacteriocins, which are antimicrobial peptides of bacterial origin, are considered potential alternatives to conventional antibiotics and have attracted widespread attention in recent years. Among these bacteriocins, lantibiotics, especially two-component lantibiotics, exhibit potent antimicrobial activity against some clinically relevant Gram-positive pathogens and have potential applications in the pharmaceutical industry...
2016: Frontiers in Microbiology
Miki Kawada-Matsuo, Ichiro Tatsuno, Kaoru Arii, Takeshi Zendo, Yuichi Oogai, Kazuyuki Noguchi, Tadao Hasegawa, Kenji Sonomoto, Hitoshi Komatsuzawa
UNLABELLED: Two-component systems (TCSs) are regulatory systems in bacteria that play important roles in sensing and adapting to the environment. In this study, we systematically evaluated the roles of TCSs in the susceptibility of the group A Streptococcus (GAS; Streptococcus pyogenes) SF370 strain to several types of lantibiotics. Using individual TCS deletion mutants, we found that the deletion of srtRK (spy_1081-spy_1082) in SF370 increased the susceptibility to nisin A, which is produced by Lactococcus lactis ATCC 11454, but susceptibility to other types of lantibiotics (nukacin ISK-1, produced by Staphylococcus warneri, and staphylococcin C55, produced by Staphylococcus aureus) was not altered in the TCS mutants tested...
October 1, 2016: Applied and Environmental Microbiology
Muhammad Imran, Anne-Marie Revol-Junelles, Grégory Francius, Stéphane Desobry
Application of nano-biotechnology to improve the controlled release of drugs or functional agents is widely anticipated to transform the biomedical, pharmaceutical, and food safety trends. The purpose of the current study was to assess and compare the release rates of fluorescently labeled antimicrobial peptide nisin (lantibiotic/biopreservative) from liposomal nanocarriers. The elevated temperature, high electrostatic attraction between anionic bilayers and cationic nisin, larger size, and higher encapsulation efficiency resulted in rapid and elevated release through pore formation...
August 24, 2016: ACS Applied Materials & Interfaces
Fergus W J Collins, Paula M O'Connor, Orla O'Sullivan, Mary C Rea, Colin Hill, R Paul Ross
Bacteriocins represent a rather underutilized class of antimicrobials despite often displaying activity against many drug-resistant pathogens. Lantibiotics are a post-translationally modified class of bacteriocins, characterized by the presence of lanthionine and methyllanthionine bridges. In this study, a novel two-peptide lantibiotic was isolated and characterized. Formicin was isolated from Bacillus paralicheniformis APC 1576, an antimicrobial-producing strain originally isolated from the intestine of a mackerel...
September 2016: Microbiology
Nagarajan Kayalvizhi, Neelamegam Rameshkumar, Paramasamy Gunasekaran
A putative gene encoding mersacidin like lantibiotic bacteriocin (lanA) was identified in Bacillus licheniformis genome. The lanA open reading frame codes for 74 amino acids with calculated isoelectric point of 6.7 and molecular mass of 8.2 kDa. The lanA gene was amplified from B. licheniformis MKU3, cloned in pQE30 vector and overexpressed in Escherichia coli M15. The recombinant peptide was purified to homogeneity using Ni-NTA chromatography and the SDS-PAGE analysis of the purified peptide revealed it to be a monomer with molecular mass of ~8...
May 2016: Journal of Food Science and Technology
Thomas T Thomsen, Biljana Mojsoska, João C S Cruz, Stefano Donadio, Håvard Jenssen, Anders Løbner-Olesen, Kim Rewitz
We used the fruit fly Drosophila melanogaster as a cost-effective in vivo model to evaluate the efficacy of novel antibacterial peptides and peptoids for treatment of methicillin-resistant Staphylococcus aureus (MRSA) infections. A panel of peptides with known antibacterial activity in vitro and/or in vivo was tested in Drosophila Although most peptides and peptoids that were effective in vitro failed to rescue lethal effects of S. aureus infections in vivo, we found that two lantibiotics, nisin and NAI-107, rescued adult flies from fatal infections...
September 2016: Antimicrobial Agents and Chemotherapy
Elma Laura Salazar-Marroquín, Luis J Galán-Wong, Víctor Ricardo Moreno-Medina, Miguel Ángel Reyes-López, Benito Pereyra-Alférez
The members of the Bacillus thuringiensis group, commonly known as Bt, produce a huge number of metabolites, which show biocidal and antagonistic activity. B. thuringiensis is widely known for synthesizing Cry, Vip and Cyt proteins, active against insects and other parasporins with biocidal activity against certain types of cancerous cells. Nevertheless, B. thuringiensis also synthesizes compounds with antimicrobial activity, especially bacteriocins. Some B. thuringiensis bacteriocins resemble lantibiotics and other small linear peptides (class IIa) from the lactic acid bacteria bacteriocins classification system...
July 2016: Reviews in Medical Microbiology: a Journal of the Pathological Society of Great Britain and Ireland
Auke J van Heel, Tomas G Kloosterman, Manuel Montalban-Lopez, Jingjing Deng, Annechien Plat, Baptiste Baudu, Djoke Hendriks, Gert N Moll, Oscar P Kuipers
To find the right conditions to isolate natively expressed antimicrobial peptides from a wide range of different microorganisms can be a challenge. Here, we exploited a heterologous expression system to produce and characterize several novel lantibiotics. We identified 54 novel putative class I and class II lantibiotics after inspecting all publicly available prokaryotic genomes using the in-house developed mining tool BAGEL3. The genes encoding these new lantibiotics fused to the nisin leader peptide gene sequence were synthesized, and the constructs were plugged into the nisin expression and modification system...
October 21, 2016: ACS Synthetic Biology
Elvis Legala Ongey, Peter Neubauer
Lanthipeptides (also called lantibiotics for those with antibacterial activities) are ribosomally synthesized post-translationally modified peptides having thioether cross-linked amino acids, lanthionines, as a structural element. Lanthipeptides have conceivable potentials to be used as therapeutics, however, the lack of stable, high-yield, well-characterized processes for their sustainable production limit their availability for clinical studies and further pharmaceutical commercialization. Though many reviews have discussed the various techniques that are currently employed to produce lanthipeptides, a direct comparison between these methods to assess industrial applicability has not yet been described...
2016: Microbial Cell Factories
Shinya Kodani, Hisayuki Komaki, Sho Ishimura, Hikaru Hemmi, Mayumi Ohnishi-Kameyama
New lantibiotic cinnamycin B was isolated from the extract of Actinomadura atramentaria NBRC 14695(T), based on genome mining and chemical investigation. The partial structure of cinnamycin B was established by 2D NMR experiments, which indicated that cinnamycin B had same methyl lanthionine bridging pattern with cinnamycin. The reduction with NaBH4-NiCl2 afforded the reduced cinnamycin B, and MS/MS experiment indicated the presence of hydroxy asparatic acid in the molecule. Cinnamycin B showed an antibacterial activity against Streptomyces antibioticus with dosage of 5 μg (0...
August 2016: Journal of Industrial Microbiology & Biotechnology
Kong Boon Lim, Marilen P Balolong, Sang Hoon Kim, Ju Kyoung Oh, Ji Yoon Lee, Dae-Kyung Kang
We isolated a Bacillus strain, RX7, with inhibitory activity against Listeria monocytogenes from soil and identified it as Bacillus amyloliquefaciens based on 16S rRNA gene sequencing. The inhibitory activity was stable over a wide range of pH and was fully retained after 30 min at 80°C, after which it decreased gradually at higher temperatures. The activity was sensitive to the proteolytic action of α-chymotrypsin, proteinase-K, and trypsin, indicating its proteinaceous nature. This bacteriocin was active against a broad spectrum of bacteria and the fungus Candida albicans...
2016: BioMed Research International
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