Relevant bibliographies by topics / Two-peptide lantibiotics

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Academic literature on the topic 'Two-peptide lantibiotics'

Author: Grafiati
Published: 7 September 2021
Last updated: 29 July 2025

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Journal articles on the topic "Two-peptide lantibiotics"

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Begley, M�ire, Paul D. Cotter, Colin Hill, and R. Paul Ross. "Identification of a Novel Two-Peptide Lantibiotic, Lichenicidin, following Rational Genome Mining for LanM Proteins." Applied and Environmental Microbiology 75, no. 17 (2009): 5451–60. http://dx.doi.org/10.1128/aem.00730-09.

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ABSTRACT Lantibiotics are ribosomally synthesized peptide antimicrobials which contain considerable posttranslational modifications. Given their usually broad host range and their highly stable structures, there have been renewed attempts to identify and characterize novel members of the lantibiotic family in recent years. The increasing availability of bacterial genome sequences means that in addition to traditional microbiological approaches, in silico screening strategies may now be employed to the same end. Taking advantage of the highly conserved nature of lantibiotic biosynthetic enzymes
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Birri, Dagim Jirata, Dag Anders Brede, and Ingolf F. Nes. "Salivaricin D, a Novel Intrinsically Trypsin-Resistant Lantibiotic from Streptococcus salivarius 5M6c Isolated from a Healthy Infant." Applied and Environmental Microbiology 78, no. 2 (2011): 402–10. http://dx.doi.org/10.1128/aem.06588-11.

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ABSTRACTIn this work, we purified and characterized a newly identified lantibiotic (salivaricin D) fromStreptococcus salivarius5M6c. Salivaricin D is a 34-amino-acid-residue peptide (3,467.55 Da); the locus of the gene encoding this peptide is a 16.5-kb DNA segment which contains genes encoding the precursor of two lantibiotics, two modification enzymes (dehydratase and cyclase), an ABC transporter, a serine-like protease, immunity proteins (lipoprotein and ABC transporters), a response regulator, and a sensor histidine kinase. The immunity gene (salI) was heterologously expressed in a sensiti
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Antoshina, D. V., S. V. Balandin, A. A. Tagaev, A. A. Potemkina, and T. V. Ovchinnikova. "Biotechnological Production of the Recombinant Two-Component Lantibiotic Lichenicidin in a Bacterial Expression System." Russian Journal of Bioorganic Chemistry 50, no. 4 (2024): 1150–61. http://dx.doi.org/10.1134/s1068162024040459.

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Abstract Objective: Lantibiotics are a family of bacterial antimicrobial peptides synthesized by ribosomes, that undergo post-translational modification to form lanthionine (Lan) and methyllanthionine (MeLan) residues. Lantibiotics are currently considered promising agents for combating antibiotic-resistant bacterial infections. This paper presents a biotechnological method for obtaining two components of the lantibiotic lichenicidin from Bacillus licheniformis B-511, Lchα and Lchβ. Such a system has the potential to facilitate the production of not only lichenicidin, but also other lantibioti
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Lawton, Elaine, R. Ross, Colin Hill, and Paul Cotter. "Two-Peptide Lantibiotics: A Medical Perspective." Mini-Reviews in Medicinal Chemistry 7, no. 12 (2007): 1236–47. http://dx.doi.org/10.2174/138955707782795638.

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Antoshina, D. V., S. V. Balandin, A. A. Tagaev, A. A. Potemkina, and T. V. Ovchinnikova. "Biotechnological Production of the Recombinant Two-Component Lantibiotic Lichenicidin in the Bacterial Expression System." Биоорганическая химия 50, no. 4 (2024): 485–97. http://dx.doi.org/10.31857/s0132342324040081.

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Lantibiotics are a family of bacterial antimicrobial peptides synthesized by ribosomes that undergo post-translational modification to form lanthionine (Lan) and methyllanthionine (MeLan) residues. Lantibiotics are considered promising agents for combating antibiotic-resistant bacterial infections. This paper presents a biotechnological method for obtaining two components of the lantibiotic lichenicidin from Bacillus licheniformis B-511 – Lchα and Lchβ. A system has been developed that allows co-expression of the lchA1 or lchA2 genes, encoding the precursors of the α- or β-components, respecti
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Navaratna, Maduwe A. D. B., Hans-Georg Sahl, and John R. Tagg. "Identification of Genes Encoding Two-Component Lantibiotic Production in Staphylococcus aureus C55 and Other Phage Group II S. aureus Strains and Demonstration of an Association with the Exfoliative Toxin B Gene." Infection and Immunity 67, no. 8 (1999): 4268–71. http://dx.doi.org/10.1128/iai.67.8.4268-4271.1999.

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ABSTRACT The production of exfoliative toxin B (ET-B), but not ET-A, was shown to be specifically associated with production of a highly conserved two-component lantibiotic peptide system in phage group IIStaphylococcus aureus. Two previously studied but incompletely characterized S. aureus bacteriocins, staphylococcins C55 and BacR1, were found to be members of this lantibiotic system, and considerable homology was also found with the two-component Lactococcus lactis bacteriocin, lacticin 3147. sacαA and sacβA, the structural genes of the lantibiotics staphylococcins C55α and C55β and two put
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Goldbeck, Oliver, Dominik Weixler, Bernhard J. Eikmanns, and Christian U. Riedel. "In Silico Prediction and Analysis of Unusual Lantibiotic Resistance Operons in the Genus Corynebacterium." Microorganisms 9, no. 3 (2021): 646. http://dx.doi.org/10.3390/microorganisms9030646.

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Post-translationally modified, (methyl-)lanthionine-containing peptides are produced by several Gram-positive bacteria. These so-called lantibiotics have potent activity against various bacterial pathogens including multidrug-resistant strains and are thus discussed as alternatives to antibiotics. Several naturally occurring mechanisms of resistance against lantibiotics have been described for bacteria, including cell envelope modifications, ABC-transporters, lipoproteins and peptidases. Corynebacterium species are widespread in nature and comprise important pathogens, commensals as well as en
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Upton, M., J. R. Tagg, P. Wescombe, and H. F. Jenkinson. "Intra- and Interspecies Signaling betweenStreptococcus salivarius and Streptococcus pyogenes Mediated by SalA and SalA1 Lantibiotic Peptides." Journal of Bacteriology 183, no. 13 (2001): 3931–38. http://dx.doi.org/10.1128/jb.183.13.3931-3938.2001.

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ABSTRACT Streptococcus salivarius 20P3 produces a 22-amino-acid residue lantibiotic, designated salivaricin A (SalA), that inhibits the growth of a range of streptococci, including all strains ofStreptococcus pyogenes. Lantibiotic production is associated with the sal genetic locus comprisingsalA, the lantibiotic structural gene; salBCTXgenes encoding peptide modification and export machinery proteins; andsalYKR genes encoding a putative immunity protein and two-component sensor-regulator system. Insertional inactivation ofsalB in S. salivarius 20P3 resulted in abrogation of SalA peptide produ
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Kalmokoff, M. L., D. Lu, M. F. Whitford, and R. M. Teather. "Evidence for Production of a New Lantibiotic (Butyrivibriocin OR79A) by the Ruminal Anaerobe Butyrivibrio fibrisolvensOR79: Characterization of the Structural Gene Encoding Butyrivibriocin OR79A." Applied and Environmental Microbiology 65, no. 5 (1999): 2128–35. http://dx.doi.org/10.1128/aem.65.5.2128-2135.1999.

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ABSTRACT The ruminal anaerobe Butyrivibrio fibrisolvens OR79 produces a bacteriocin-like activity demonstrating a very broad spectrum of activity. An inhibitor was isolated from spent culture fluid by a combination of ammonium sulfate and acidic precipitations, reverse-phase chromatography, and high-resolution gel filtration. N-terminal analysis of the isolated inhibitor yielded a 15-amino-acid sequence (G-N/Q-G/P-V-I-L-X-I-X-H-E-X-S-M-N). Two different amino acid residues were detected in the second and third positions from the N terminus, indicating the presence of two distinct peptides. A g
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Majchrzykiewicz, Joanna A., Jacek Lubelski, Gert N. Moll, et al. "Production of a Class II Two-Component Lantibiotic of Streptococcus pneumoniae Using the Class I Nisin Synthetic Machinery and Leader Sequence." Antimicrobial Agents and Chemotherapy 54, no. 4 (2010): 1498–505. http://dx.doi.org/10.1128/aac.00883-09.

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ABSTRACT Recent studies showed that the nisin modification machinery can successfully dehydrate serines and threonines and introduce lanthionine rings in small peptides that are fused to the nisin leader sequence. This opens up exciting possibilities to produce and engineer larger antimicrobial peptides in vivo. Here we demonstrate the exploitation of the class I nisin production machinery to generate, modify, and secrete biologically active, previously not-yet-isolated and -characterized class II two-component lantibiotics that have no sequence homology to nisin. The nisin synthesis machinery
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Dissertations / Theses on the topic "Two-peptide lantibiotics"

1

Barbosa, Joana Cristina Pacheco. "Deepening the study of the two-peptide lantibiotic lichenicidin: bioengineering, toxicity and mode of action." Doctoral thesis, 2020. http://hdl.handle.net/10773/30177.

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Many novel peptides have recently been discovered and characterized that have been shown to be effective against clinically relevant strains, including multi-drug resistant bacteria. Lantibiotics are presented as an alternative to the more traditional antibiotics. The present study aimed to clarify aspects of the biosynthesis, structure, mode of action and toxicity of lichenicidin. Lichenicidin is a two peptide (Bliα and Bliβ) lantibiotic produced by B. licheniformis with bioactivity against Staphylococcus aureus and Listeria monocytogenes. It was the first lantibiotic to be produced totally i
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