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Topic: Lantibiotics

	Lantibiotics - Wikipedia, the free encyclopedia
		Lantibiotics are polycyclic peptides containing uncommon amino acids like the lanthionine, 2-aminoisobutyric acid, and unsaturated amino acids such as dehydroalanine.
		Lantibiotics show substantial specificity for some components of bacterial cell membranes.
		This page was last modified 03:24, 24 March 2006.
	en.wikipedia.org /wiki/Lantibiotics (63 words)

	Patent 7,034,113
		The complexes are preferably chelated complexes wherein the bacteriocin is a lantibiotic, non-lanthionine containing peptide, large heat labile protein and complex bacteriocin, fusion protein thereof, mixture thereof, and fragment, homolog and variant thereof, and (b) a detectable label comprising a transition or lanthanide metal.
		The chelated complexes of the present invention are comprised of (a) a bacteriocin selected from the group consisting of lantibiotics, non-lanthionine containing peptides, large heat labile proteins and complex bacteriocins, fusion proteins thereof, mixtures thereof, and fragments, homologs and variants thereof, and (b) a detectable label comprising a transition or lanthanide metal.
		While lantibiotics are the preferred bacteriocins, any of the generally cationic peptides synthesized by bacteria, plants, mammals or insects having antimicrobial activity and forming complexes with transition or lanthanide metals could be used.
	www.pharmcast.com /Patents100/Yr2006/April2006/042506/7034113_Bacteriocin042506.htm (7926 words)

	Lantibiotics (Site not responding. Last check: 2007-11-01)
		Lantibiotics differ from the other anti-microbial peptides described in this project because they are derived from bacteria rather than host cells.
		Lantibiotics are expressed during late-exponential and early-stationary growth-phases meaning that they reduce competition from other flora once they themselves have become established (1).
		For instance, lantibiotics with future potential for medical applications include nisin for the treatment of peptic ulcers caused by Helicobacter pylori (7) and gallidermin (from Propionibacterium acnes) as a topical treatment for acne (8).
	www.portfolio.mvm.ed.ac.uk /studentwebs/session1/group11/Lantibiotics.htm (440 words)

	Patent 6,794,181
		In preferred embodiments, the lantibiotic is nisin, although the common structural features of lantibiotics dictate the effectiveness of the disclosed purification methods for other members of the lantibiotic genus.
		In preferred embodiments, the lantibiotic is nisin, although the common structural features of lantibiotics govern the effectiveness of the disclosed purification methods for other members of the lantibiotic genus.
		Thus, white the Exemplification section focuses primarily on the lantibiotic nisin, the principles established herein would be expected to apply to all lantibiotics due to the presence of their defining structural characteristics.
	www.pharmcast.com /Patents100/Yr2004/Sept2004/092104/6794181_Lantiobiotics092104.htm (2560 words)

	Dual Role of GdmH in Producer Immunity and Secretion of the Staphylococcal Lantibiotics Gallidermin and Epidermin -- ...
		The biosynthetic gene clusters of the staphylococcal lantibiotics epidermin and gallidermin are distinguished by the presence
		The biosynthesis of the lantibiotics epidermin, gallidermin, pep5 and epilancin K7.
		Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis.
	aem.asm.org /cgi/content/full/67/3/1380 (1816 words)

	Chapter Abstracts: Research and Applications in Bacteriocins
		Replacement of non-standard residues in lantibiotics revealed that these residues generally stabilize conformations that are essential for activity and protection against proteases, and that the residues are often required for optimal bacteriocin-production.
		Genetic modification of lantibiotics has also revealed that the lantibiotic-modifying enzyme is rather permissive with respect to substrate specificity, but the presence of a correct leader sequence is a requirement for substrate-recognition as well as for bacteriocin-export.
		Genetically modified constructs of lantibiotics and pediocin-like bacteriocins have especially been useful for elucidating their structure and interaction with the wall and membrane of target-cells.
	www.horizonpress.com /hsp/abs/absbact.html (1575 words)

	C&EN: TODAY'S HEADLINES - TOWARD NOVEL LANTIBIOTICS (Site not responding. Last check: 2007-11-01)
		Although the genes encoding lantibiotic biosynthetic enzymes have been known for a long time, this is the first time that one of these enzymes has been purified in its active form.
		Other lantibiotics are used as natural preservatives in a variety of foods, including milk, meat, and canned vegetables.
		Lantibiotics are peptide-based compounds produced by bacteria that live on lactic acid.
	pubs.acs.org /cen/topstory/8205/8205notw8.html (451 words)

	MD/PhD - Medical Scholars Program : Student Research Synopsis
		Lantibiotics (from lanthionine-containing antibiotic) derive their name from the unusual amino acid lanthionine, which consists of two alanine residues cross-linked by a thioether bridge that connects their ?-carbons.
		For this reason and because lantibiotics possess high levels of antimicrobial activity against several pathogenic gram-positive bacteria such as staphylococci, streptococci, and clostridia, nisin, the prototypical lantibiotic, has been used extensively for the past 40 years as a commercial food preservative.
		The lantibiotic nisin is a 34-residue bacteriocin produced by the gram-positive bacteria Lactococcus lactis spp where it is first ribosomally synthesized as an inactive precursor and then post-translationally modified into its mature biologically active form.
	www.med.uiuc.edu /msp/ResearchSynopsis.asp?NetID=jjyu (310 words)

	[No title]
		Lantibiotics are antimicrobial peptides that contain the amino acid lanthionine.
		Lantibiotics are produced from peptides after these peptides have left the ribosome.
		The only lantibiotic currently approved for use a a food preservative is nisin, which is produced by Lactococcus lactis.
	www.smccd.net /accounts/case/antibiotics.html (1075 words)

	Oragenics - Press
		Although the funded research will focus on the production of analogs from the potentially important class of antibiotics called lantibiotics, the technology has broader applications and may also be used for the cost-effective manufacture of a number of commercially important bioactive peptides.
		Lantibiotics, including Oragenics’ lead antibiotic, MU1140, are a family of polycyclic peptides that are produced by bacteria and are highly modified structurally.
		Attempts to study lantibiotics for their potential usefulness as therapeutic agents have been hindered by difficulties in producing sufficiently pure material in amounts adequate for the required preclinical testing.
	www.oragenics.com /announce.php?subaction=showfull&id=1146651010&archive=&start_from=&ucat=2& (482 words)

	Insights into In Vivo Activities of Lantibiotics from Gallidermin and Epidermin Mode-of-Action Studies -- Bonelli et ... (Site not responding. Last check: 2007-11-01)
		Primary structures of gallidermin, gallidermin mutant peptides, and epidermin (A) and the related lantibiotic nisin (B).
		The lantibiotic mersacidin inhibits peptidoglycan synthesis by tageting lipid II.
		Lipid II induces a transmembrane orientation of the pore-forming peptide lantibiotic nisin.
	aac.asm.org /cgi/content/full/50/4/1449 (5520 words)

	New method for manufacturing complex peptides receives funding
		Lantibiotics, such as Oragenics' lead antibiotic MU1140, are a family of polycyclic peptides that are produced by bacteria and are highly modified structurally, however, attempts to study them as therapeutic agents have been hindered by difficulties in producing sufficiently pure material in amounts adequate for the required preclinical testing.
		There are curently at least 25 reported lantibiotics that have an intertwining ring structure but no one has been able to find fermentation methods for cost effective production and/or purification.
		Thus, DPOLT allows to rapidly synthesise and screen the known lantibiotics to identify the ones that are best suited for further development, and could potentially be used for large-scale manufacturing.
	www.in-pharmatechnologist.com /news/ng.asp?n=67818-oragenics-peptides-mu-lantibiotics (712 words)

	BioMed Central \| Full text \| Mutacin H-29B is identical to mutacin II (J-T8)
		Lantibiotics contain unusual amino acids such as Lan, BM-Lan and dehydrated amino acid residues [9].
		Woodruff WA, Novak J, Caufield PW: Sequence analysis of mutA and mutM genes involved in the biosynthesis of the lantibiotic mutacin II in Streptococcus mutans.
		Ross KF, Ronson CW, Tagg JR: Isolation and characterization of the lantibiotic salivaricin A and its structural gene salA from Streptococcus salivarius 20P3.
	www.biomedcentral.com /1471-2180/6/36 (2965 words)

	FEBS Abstract
		One well-studied lantibiotic is nisin that kills bacteria by targeted pore formation using Lipid II as receptor [1].
		Surprisingly, nisin variants and related lantibiotics that effectively kill bacteria and specifically dock on Lipid II do not form pores in the membrane and thus must use another mechanism to kill bacteria.
		These studies reveal that the lantibiotics are promising candidates for the development of new antibiotics that are highly needed with the alarming rise of drug resistant bacteria.
	www.blackwellpublishing.com /febsabstracts2005/abstract.asp?id=40825 (260 words)

	PMID: 7601145 (Site not responding. Last check: 2007-11-01)
		Lantibiotics are biologically active peptides which contain the thioether amino acid lanthionine as well as several other modified amino acids.
		In the last decade there has been a marked increase in research interest in these peptides due both to the novel biosynthetic mechanisms by which they are produced, as well as to their potential applications.
		While the principle biological activity of most type-B lantibiotics appears to be directed at the inhibition of enzyme functions, the type-A lantibiotics kill bacterial cells by forming pores in the cytoplasmic membrane.
	lethargy.swmed.edu /cgi-bin/etblast/abstract_local?pmid=7601145&user_id=1015735726&application=0 (187 words)

	Lantibiotic Biosynthesis: Interactions between Prelacticin 481 and Its Putative Modification Enzyme, LctM -- Uguen et ...
		Biosynthesis of the lantibiotic mersacidin: organization of a type B lantibiotic gene cluster.
		Nucleotide sequence of the lantibiotic Pep5 biosynthetic gene cluster and functional analysis of PepP and PepC.
		Sequence analysis of mutA and mutM genes involved in the biosynthesis of the lantibiotic mutacin II in Streptococcus mutans.
	jb.asm.org /cgi/content/full/182/18/5262 (2993 words)

	Pharmalicensing.com
		Hansen is an expert in the field of antimicrobial peptides, called lantibiotics.
		We are pleased to have established a collaboration with Dr. Hansen, who is clearly a leader in the field of lantibiotics," said Larry Ellingsworth, Ph.D., Vice President Research and Development at Antex.
		Lantibiotics have great potential to fight serious infections in people because they are very effective at killing many pathogenic bacteria on contact.
	pharmalicensing.com /news/adisp/972580249_39f86599b3634 (395 words)

	Novacta drug discover - Lantibiotics printable page (Site not responding. Last check: 2007-11-01)
		Novacta has identified an exciting class of compounds, known as lantibiotics, as a target for development.
		The lantibiotics are highly modified peptides, combining the beneficial biological interactions and versatility of peptides with desirable pharmaceutical properties such as stability in the systemic circulation.
		Lantibiotics have shown promising activity against bacteria resistant to commonly used antibacterials, including methicillin resistant Staphylococcus aureus (MRSA).
	www.novactabio.com /printlantib.htm (181 words)

	Lanthionine - Wikipedia, the free encyclopedia
		Lanthionines are found widely in nature and have been isolated from human hair, lactalbumin, and feathers.
		Lanthionines have also been found in bacterial cell walls and are the components of a group of gene encoded peptide antibiotics called lantibiotics, which includes nisin (a food preservative), subtilin, epidermin (an anti staphylococcus and streptococcus agent), and ancovenin (an enzyme inhibitor).
		The sulfur extrusion method is, however, the only pathway for lanthionine that has been employed in the total synthesis of a lantibiotic.
	en.wikipedia.org /wiki/Lanthionine (287 words)

	Generation of Food-Grade Lactococcal Starters Which Produce the Lantibiotics Lacticin 3147 and Lacticin 481 -- ...
		Elevated enzyme release from lactococcal starter cultures on exposure to the lantibiotic lacticin 481, produced by L.
		Lantibiotics produced by lactic acid bacteria: structure, function and applications.
		The structure of the lantibiotic lacticin 481 produced by Lactococcus lactis: location of the thioether bridges.
	aem.asm.org /cgi/content/full/69/6/3681 (2401 words)

	Available Technologies - Office of Technology Management (Site not responding. Last check: 2007-11-01)
		This invention allows the engineering of semi-synthetic lantibiotics to a much larger extent than using typically practiced in vivo methods.
		The method is the first in vitro reconstruction lantibiotic photosynthesis and introduces non-proteinogenic amino acids.
		This approach, the first in vitro reconstruction of lantibiotic biosynthesis, allows for lantibiotic engineering and opens the door to possible generations of new lantibiotics with greatly increased yields and improved activities.
	www.otm.uiuc.edu /techs/techdetail.asp?id=313 (297 words)

	Food Additive May Pave Way to New Antibiotics (Site not responding. Last check: 2007-11-01)
		One type of lantibiotic, known as nisin, kills germs in food and helps them to stay fresh longer.
		One kind of lantibiotic, for instance, could stop inflammation in the body, he says.
		If lantibiotics begin to be used in humans, they will almost certainly be banned from use in foods, van der Donk says.
	www.genesishcs.org /healthyliving/nutrition/dec04foodadditive.htm (627 words)

	PMID: 7646850 (Site not responding. Last check: 2007-11-01)
		The lantibiotics are a unique class of bacterium-derived peptide antibiotics, all of which contain the rare amino acid lanthionine, as well as a number of other nonprotein amino acids.
		Unlike most other peptide antibiotics, lantibiotics are produced on the ribosome as a prepeptide, and a series of post-translational modifications converts this precursor into the biologically active peptide.
		A complex set of gene products involved in lantibiotic biosynthesis have been identified, including the genes for specific amino acid modifications, as well as other ancillary biosynthetic functions.
	lethargy.swmed.edu /cgi-bin/etblast/abstract_local?pmid=7646850&user_id=1015735726&application=0 (145 words)

	Sequential Actions of the Two Component Peptides of the Lantibiotic Lacticin 3147 Explain Its Antimicrobial Activity at ... (Site not responding. Last check: 2007-11-01)
		The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation.
		Plantaricin W from Lactobacillus plantarum belongs to a new family of two-peptide lantibiotics.
		Structural characterization of lacticin 3147, a two-peptide lantibiotic with synergistic activity.
	aac.asm.org /cgi/content/full/49/7/2606 (3637 words)

	Plantaricin W from Lactobacillus plantarum belongs to a new family of two-peptide lantibiotics -- Holo et al. 147 (3): ...
		Plantaricin W from Lactobacillus plantarum belongs to a new family of two-peptide lantibiotics -- Holo et al.
		Three-dimensional structure of the lantibiotic nisin in the presence of membrane-mimetic micelles of dodecylphosphocholine and of sodium dodecylsulphate.
		Paik, S. H., Chakicherla, A. and Hansen, J. Identification and characterization of the structural and transporter genes for, and the chemical and biological properties of, sublancin 168, a novel lantibiotic produced by Bacillus subtilis 168.
	mic.sgmjournals.org /cgi/content/full/147/3/643 (4180 words)

	Pfam 20.0 : L_biotic_typeA (Site not responding. Last check: 2007-11-01)
		Lantibiotics are antibiotic peptides distinguished by the presence of the rare thioether amino acids lanthionine and/or methyllanthionine.
		They are produced by Gram-positive bacteria as gene-encoded precursor peptides and undergo post-translational modification to generate the mature peptide.
		Based on their structural and functional features lantibiotics are currently divided into two major groups: the flexible amphiphilic type-A and the rather rigid and globular type-B. Type-A lantibiotics act primarily by pore formation in the bacterial membrane by a mechanism involving the interaction with specific docking molecules such as the membrane precursor lipid II [1].
	pfam.wustl.edu /cgi-bin/getdesc?name=L_biotic_typeA (147 words)

	Identification of Genes Encoding Two-Component Lantibiotic Production in Staphylococcus aureus C55 and Other Phage ...
		Isolation, characterization, and heterologous expression of the novel lantibiotic epicidin 280 and analysis of its biosynthetic gene cluster.
		Comparison of the lantibiotic gene clusters and encoded proteins.
		Altena, K., Guder, A., Cramer, C., Bierbaum, G. Biosynthesis of the Lantibiotic Mersacidin: Organization of a Type B Lantibiotic Gene Cluster.
	iai.asm.org /cgi/content/full/67/8/4268?view=full&pmid=10417203 (2555 words)

	Each peptide of the two-component lantibiotic lacticin 3147 requires a separate modification enzyme for activity -- ...
		Meyer, C., Bierbaum, G., Heidrich, C., Reis, M., Süling, J., Iglesias-Wind, M. I., Kempter, C., Molitor, E. and Sahl, H.-G. Nucleotide sequence of the lantibiotic Pep5 biosynthetic gene cluster and functional analysis of PepP and PepC: evidence for a role of PepC in thioether formation.
		Navaratna, M. A., Sahl, H.-G. and Tagg, J. Identification of genes encoding two-component lantibiotic production in Staphylococcus aureus strain C55 and other phage group II aureus strains and demonstration of an association with the exfoliative toxin B gene.
		Siegers, K., Heinzmann, S. and Entian, K.-D. Biosynthesis of lantibiotic nisin: post-translational modification of its prepeptide occurs at a multimeric membrane-associated lanthionine synthetase complex.
	mic.sgmjournals.org /cgi/content/full/146/9/2147 (3761 words)

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