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Lanthipeptide

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https://www.readbyqxmd.com/read/28809560/recombinant-macrocyclic-lanthipeptides-incorporating-non-canonical-amino-acids
#1
Claudio Zambaldo, Xiaozhou Luo, Angad P Mehta, Peter G Schultz
Nisin is a complex lanthipeptide that has broad spectrum antibacterial activity. In efforts to broaden the structural diversity of this ribosomally synthesized lantibiotic, we now report the recombinant expression of Nisin variants that incorporate noncanonical amino acids (ncAAs) at discrete positions. This is achieved by expressing the nisA structural gene, cyclase (nisC) and dehydratase (nisB), together with an orthogonal nonsense suppressor tRNA/aminoacyl-tRNA synthetase pair in Escherichia coli. A number of ncAAs with novel chemical reactivity were genetically incorporated into NisA, including an α-chloroacetamide-containing ncAA that allowed for the expression of Nisin variants with novel macrocyclic topologies...
August 15, 2017: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/28691075/chimeric-leader-peptides-for-the-generation-of-non-natural-hybrid-ripp-products
#2
Brandon J Burkhart, Nidhi Kakkar, Graham A Hudson, Wilfred A van der Donk, Douglas A Mitchell
Combining biosynthetic enzymes from multiple pathways is an attractive approach for producing molecules with desired structural features; however, progress has been hampered by the incompatibility of enzymes from unrelated pathways and intolerance toward alternative substrates. Ribosomally synthesized and posttranslationally modified peptides (RiPPs) are a diverse natural product class that employs a biosynthetic logic that is highly amenable to engineering new compounds. RiPP biosynthetic proteins modify their substrates by binding to a motif typically located in the N-terminal leader region of the precursor peptide...
June 28, 2017: ACS Central Science
https://www.readbyqxmd.com/read/28675292/substrate-specificity-of-the-secreted-nisin-leader-peptidase-nisp
#3
Marcel Lagedroste, Sander H J Smits, Lutz Schmitt
Nisin (NisA) is an antimicrobial peptide produced by Lactococcus lactis and belongs to the class of lanthipeptides, more specifically to the class of lantibiotics. They are ribosomally synthesized as a precursor peptide and are comprised of an N-terminal leader peptide and a C-terminal core peptide. The core peptide is post-translationally modified and contains dehydrated amino acids in addition to five (methyl)-lanthionine rings, which are crucial for its activity. The leader peptide serves as a signal sequence and ensures that NisA remains inactive but secretion-competent within the cell...
August 1, 2017: Biochemistry
https://www.readbyqxmd.com/read/28667105/bacteriocins-of-non-aureus-staphylococci-isolated-from-bovine-milk
#4
Domonique A Carson, Herman W Barkema, Sohail Naushad, Jeroen De Buck
Non-aureus staphylococci (NAS), the bacteria most commonly isolated from the bovine udder, potentially protect the udder against infection by major mastitis pathogens due to bacteriocin production. In this study, we determined the inhibitory capability of 441 bovine NAS isolates (comprising 26 species) against bovine S. aureus Furthermore, inhibiting isolates were tested against a human methicillin-resistant S. aureus (MRSA) isolate using a cross-streaking method. We determined the presence of bacteriocin clusters in NAS whole genomes using genome mining tools, BLAST, and comparison of genomes of closely related inhibiting and non-inhibiting isolates and determined the genetic organization of any identified bacteriocin biosynthetic gene clusters...
June 30, 2017: Applied and Environmental Microbiology
https://www.readbyqxmd.com/read/28650175/bioactive-peptide-natural-products-as-lead-structures-for-medicinal-use
#5
Tam Dang, Roderich D Süssmuth
The need for new drugs for the treatment of various diseases is enormous. From the previous century until the present, numerous peptide and peptide-derived natural products have been isolated from bacteria and fungi. Hence, microorganisms play a pivotal role as sources for novel drugs with an emphasis on anti-infective agents. Various disciplines from biology, chemistry, and medicine are involved in early stages of the search for peptide natural products including taxonomy, microbiology, bioanalytics, bioinformatics, and medicinal chemistry...
June 26, 2017: Accounts of Chemical Research
https://www.readbyqxmd.com/read/28630351/evolutionary-radiation-of-lanthipeptides-in-marine-cyanobacteria
#6
Andres Cubillos-Ruiz, Jessie W Berta-Thompson, Jamie W Becker, Wilfred A van der Donk, Sallie W Chisholm
Lanthipeptides are ribosomally derived peptide secondary metabolites that undergo extensive posttranslational modification. Prochlorosins are a group of lanthipeptides produced by certain strains of the ubiquitous marine picocyanobacteria Prochlorococcus and Synechococcus Unlike other lanthipeptide-producing bacteria, picocyanobacteria use an unprecedented mechanism of substrate promiscuity for the production of numerous and diverse lanthipeptides using a single lanthionine synthetase. Through a cross-scale analysis of prochlorosin biosynthesis genes-from genomes to oceanic populations-we show that marine picocyanobacteria have the collective capacity to encode thousands of different cyclic peptides, few of which would display similar ring topologies...
July 3, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28499008/rippminer-a-bioinformatics-resource-for-deciphering-chemical-structures-of-ripps-based-on-prediction-of-cleavage-and-cross-links
#7
Priyesh Agrawal, Shradha Khater, Money Gupta, Neetu Sain, Debasisa Mohanty
Ribosomally synthesized and post-translationally modified peptides (RiPPs) constitute a rapidly growing class of natural products with diverse structures and bioactivities. We have developed RiPPMiner, a novel bioinformatics resource for deciphering chemical structures of RiPPs by genome mining. RiPPMiner derives its predictive power from machine learning based classifiers, trained using a well curated database of more than 500 experimentally characterized RiPPs. RiPPMiner uses Support Vector Machine to distinguish RiPP precursors from other small proteins and classify the precursors into 12 sub-classes of RiPPs...
May 12, 2017: Nucleic Acids Research
https://www.readbyqxmd.com/read/28155176/erratum-to-pharmacological-and-pharmacokinetic-properties-of-lanthipeptides-undergoing-clinical-studies
#8
Elvis Legala Ongey, Hüseyin Yassi, Stephan Pflugmacher, Peter Neubauer
No abstract text is available yet for this article.
February 2, 2017: Biotechnology Letters
https://www.readbyqxmd.com/read/28135077/mechanistic-understanding-of-lanthipeptide-biosynthetic-enzymes
#9
REVIEW
Lindsay M Repka, Jonathan R Chekan, Satish K Nair, Wilfred A van der Donk
Lanthipeptides are ribosomally synthesized and post-translationally modified peptides (RiPPs) that display a wide variety of biological activities, from antimicrobial to antiallodynic. Lanthipeptides that display antimicrobial activity are called lantibiotics. The post-translational modification reactions of lanthipeptides include dehydration of Ser and Thr residues to dehydroalanine and dehydrobutyrine, a transformation that is carried out in three unique ways in different classes of lanthipeptides. In a cyclization process, Cys residues then attack the dehydrated residues to generate the lanthionine and methyllanthionine thioether cross-linked amino acids from which lanthipeptides derive their name...
April 26, 2017: Chemical Reviews
https://www.readbyqxmd.com/read/28106097/lancl-proteins-are-not-involved-in-lanthionine-synthesis-in-mammals
#10
Chang He, Min Zeng, Debapriya Dutta, Tong Hee Koh, Jie Chen, Wilfred A van der Donk
LanC-like (LanCL) proteins are mammalian homologs of bacterial LanC enzymes, which catalyze the addition of the thiol of Cys to dehydrated Ser residues during the biosynthesis of lanthipeptides, a class of natural products formed by post-translational modification of precursor peptides. The functions of LanCL proteins are currently unclear. A recent proposal suggested that LanCL1 catalyzes the addition of the Cys of glutathione to protein- or peptide-bound dehydroalanine (Dha) to form lanthionine, analogous to the reaction catalyzed by LanC in bacteria...
January 20, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28044226/pharmacological-and-pharmacokinetic-properties-of-lanthipeptides-undergoing-clinical-studies
#11
REVIEW
Elvis Legala Ongey, Hüseyin Yassi, Stephan Pflugmacher, Peter Neubauer
The intrinsic qualities of lanthipeptides for their use as therapeutic drugs present several challenges because of their properties, which include stability, solubility and bioavailability, which, under physiological conditions, are very low. Researches have encouraged clinical evaluation of a few compounds, such as mutacin 1140, microbisporicin, actagardine and duramycin, with pharmacokinetic profiles showing rapid distribution and elimination rates, good bioavailability and fecal excretion, as well as high protein binding...
April 2017: Biotechnology Letters
https://www.readbyqxmd.com/read/27934350/synthesis-and-bioactivity-of-diastereomers-of-the-virulence-lanthipeptide-cytolysin
#12
Subha Mukherjee, Liujie Huo, Gabrielle N Thibodeaux, Wilfred A van der Donk
Cytolysin, a two-component lanthipeptide comprising cytolysin S (CylLS″) and cytolysin L (CylLL″), is the only family member to exhibit lytic activity against mammalian cells in addition to synergistic antimicrobial activity. A subset of the thioether cross-links of CylLS″ and CylLL″ have ll stereochemistry instead of the canonical dl stereochemistry in all previously characterized lanthipeptides. The synthesis of a CylLS″ variant with dl stereochemistry is reported. Its antimicrobial activity was found to be decreased, but not its lytic activity against red blood cells...
December 2, 2016: Organic Letters
https://www.readbyqxmd.com/read/27924934/one-pot-synthesis-of-class-ii-lanthipeptide-bovicin-hj50-via-an-engineered-lanthipeptide-synthetase
#13
Jian Wang, Xiaoxuan Ge, Li Zhang, Kunling Teng, Jin Zhong
Lanthipeptides are a large class of bacteria-produced, ribosomally-synthesized and post-translationally modified peptides. They are recognized as peptide antibiotics because most of them exhibit potent antimicrobial activities against Gram-positive bacteria especially those that are phylogenetically related to producers. Maturation of class II lanthipeptide like bovicin HJ50 undergoes precursor modification by LanM and a subsequent leader peptide cleavage by LanT. Herein, via co-expression of precursor gene bovA, modification gene bovM and transporter gene bovT in Escherichia coli C43 (DE3), bioactive bovicin HJ50 was successfully produced and secreted...
December 7, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27584723/a-lanthipeptide-like-n-terminal-leader-region-guides-peptide-epimerization-by-radical-sam-epimerases-implications-for-ripp-evolution
#14
Sebastian W Fuchs, Gerald Lackner, Brandon I Morinaka, Yohei Morishita, Teigo Asai, Sereina Riniker, Jörn Piel
Ribosomally synthesized and posttranslationally modified peptide natural products (RiPPs) exhibit diverse structures and bioactivities and are classified into distinct biosynthetic families. A recently reported family is the proteusins, with the prototype members polytheonamides being generated by almost 50 maturation steps, including introduction of d-residues at multiple positions by an unusual radical SAM epimerase. A region in the protein-like N-terminal leader of proteusin precursors is identified that is crucial for epimerization...
September 26, 2016: Angewandte Chemie
https://www.readbyqxmd.com/read/27382781/-recent-advances-in-lanthipeptide-biosynthesis-a-review
#15
REVIEW
Tianlu Mo, Lingui Xue, Qi Zhang
Lanthipeptides are a growing class of ribosomally synthesized and posttranslationally modified peptide (RiPP) natural products. These compounds are widely distributed among taxonomically distant species, and their structures and biological activities are diverse, providing an important source for drug research and developement. In this review, we summarized the recent advances in the understanding of structure, classification, evolution and substrate-controlled biosynthetic mechanism of lanthipeptide, attempting to highlight the intriguing chemistry and enzymology in the biosynthesis of this growing family of natural products...
March 4, 2016: Wei Sheng Wu Xue Bao, Acta Microbiologica Sinica
https://www.readbyqxmd.com/read/27348535/the-enterococcal-cytolysin-synthetase-coevolves-with-substrate-for-stereoselective-lanthionine-synthesis
#16
Weixin Tang, Gabrielle N Thibodeaux, Wilfred A van der Donk
Stereochemical control is critical in natural product biosynthesis. For ribosomally synthesized and post-translationally modified peptides (RiPPs), the mechanism(s) by which stereoselectivity is achieved is still poorly understood. In this work, we focused on the stereoselective lanthionine synthesis in lanthipeptides, a major class of RiPPs formed by the addition of Cys residues to dehydroalanine (Dha) or dehydrobutyrine (Dhb). Nonenzymatic cyclization of the small subunit of a virulence lanthipeptide, the enterococcal cytolysin, resulted in the native modified peptide as the major product, suggesting that both regioselectivity and stereoselectivity are inherent to the dehydrated peptide sequence...
September 16, 2016: ACS Chemical Biology
https://www.readbyqxmd.com/read/27267232/lanthipeptides-chemical-synthesis-versus-in-vivo-biosynthesis-as-tools-for-pharmaceutical-production
#17
REVIEW
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...
June 7, 2016: Microbial Cell Factories
https://www.readbyqxmd.com/read/27184432/complete-genome-sequence-of-bacillus-subtilis-bsd-2-a-microbial-germicide-isolated-from-cultivated-cotton
#18
Hongwei Liu, Shuli Yin, Likang An, Genwei Zhang, Huicai Cheng, Yanhua Xi, Guanhui Cui, Feiyan Zhang, Liping Zhang
Bacillus subtilis BSD-2, isolated from cotton (Gossypium spp.), had strong antagonistic activity to Verticillium dahlia Kleb and Botrytis cinerea. We sequenced and annotated the BSD-2 complete genome to help us the better use of this strain, which has surfactin, bacilysin, bacillibactin, subtilosin A, Tas A and a potential class IV lanthipeptide biosynthetic pathways.
July 20, 2016: Journal of Biotechnology
https://www.readbyqxmd.com/read/27178086/characterization-of-the-stereochemical-configuration-of-lanthionines-formed-by-the-lanthipeptide-synthetase-geom
#19
Neha Garg, Yuki Goto, Ting Chen, Wilfred A van der Donk
The biosynthesis of the class II lanthipeptide geobacillin II was reconstituted in vitro. The purified precursor peptide was modified by the lanthipeptide synthetase GeoM at temperatures ranging between 37 and 80°C demonstrating the thermostability of the enzyme. Geobacillin II shares with cytolysin, haloduracin, and carnolysin a DhxDhxXxxXxxCys motif (Dhx = dehydroalanine or dehydrobutyrine) as precursor to its N-terminal A-ring. Like in these other three lantibiotics, the lanthionine in the A-ring of geobacillin II had the LL stereochemical configuration as shown by chiral gas chromatography/mass spectrometry...
November 2016: Biopolymers
https://www.readbyqxmd.com/read/27128996/transcriptional-response-of-prochlorococcus-to-co-culture-with-a-marine-alteromonas-differences-between-strains-and-the-involvement-of-putative-infochemicals
#20
Dikla Aharonovich, Daniel Sher
Interactions between marine microorganisms may determine the dynamics of microbial communities. Here, we show that two strains of the globally abundant marine cyanobacterium Prochlorococcus, MED4 and MIT9313, which belong to two different ecotypes, differ markedly in their response to co-culture with a marine heterotrophic bacterium, Alteromonas macleodii strain HOT1A3. HOT1A3 enhanced the growth of MIT9313 at low cell densities, yet inhibited it at a higher concentration, whereas it had no effect on MED4 growth...
December 2016: ISME Journal
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