Abstract
Lasso peptides are members of the ribosomally synthesized and post-translationally modified peptides produced by bacteria. Currently known lasso peptides are produced in the phyla of Proteobacteria or Actinobacteria. They attract considerable attention because of their original interlocked structure endowed with high stability and important biological activities ranging from antimicrobials to enzyme inhibitors or receptor antagonists. The structure of lasso peptides consists of a peptidic tail trapped and locked into a macrolactam ring, forming a loop standing above and a threaded tail below the ring. This chapter describes the currently known lasso peptides concerning their origin, production and purification, structure and factors that contribute to maintain the lasso topology.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Arnison PG, Bibb MJ, Bierbaum G, Bowers AA, Bugni TS, Bulaj G, Camarero JA, Campopiano DJ, Challis GL, Clardy J, Cotter PD, Craik DJ, Dawson M, Dittmann E, Donadio S, Dorrestein PC, Entian KD, Fischbach MA, Garavelli JS, Goransson U, Gruber CW, Haft DH, Hemscheidt TK, Hertweck C, Hill C, Horswill AR, Jaspars M, Kelly WL, Klinman JP, Kuipers OP, Link AJ, Liu W, Marahiel MA, Mitchell DA, Moll GN, Moore BS, Muller R, Nair SK, Nes IF, Norris GE, Olivera BM, Onaka H, Patchett ML, Piel J, Reaney MJ, Rebuffat S, Ross RP, Sahl HG, Schmidt EW, Selsted ME, Severinov K, Shen B, Sivonen K, Smith L, Stein T, Sussmuth RD, Tagg JR, Tang GL, Truman AW, Vederas JC, Walsh CT, Walton JD, Wenzel SC, Willey JM, van der Donk WA (2013) Ribosomally synthesized and posttranslationally modified peptide natural products: overview and recommendations for a universal nomenclature. Nat Prod Rep 30(1):108–160. doi:10.1039/c2np20085f
Bayro MJ, Mukhopadhyay J, Swapna GV, Huang JY, Ma LC, Sineva E, Dawson PE, Montelione GT, Ebright RH (2003) Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot. J Am Chem Soc 125(41):12382–12383
Blond A, Peduzzi J, Goulard C, Chiuchiolo MJ, Barthelemy M, Prigent Y, Salomón RA, Farías RN, Moreno F, Rebuffat S (1999) The cyclic structure of microcin J25, a 21-residue peptide antibiotic from Escherichia coli. Eur J Biochem 259(3):747–755
Blond A, Cheminant M, Segalas-Milazzo I, Peduzzi J, Barthelemy M, Goulard C, Salomon R, Moreno F, Farias R, Rebuffat S (2001) Solution structure of microcin J25, the single macrocyclic antimicrobial peptide from Escherichia coli. Eur J Biochem 268(7):2124–2133
Blond A, Cheminant M, Destoumieux-Garzón D, Segalas-Milazzo I, Peduzzi J, Goulard C, Rebuffat S (2002) Thermolysin-linearized microcin J25 retains the structured core of the native macrocyclic peptide and displays antimicrobial activity. Eur J Biochem 269(24):6212–6222
Brett PJ, DeShazer D, Woods DE (1998) Burkholderia thailandensis sp. nov., a Burkholderia pseudomallei-like species. Int J Syst Bacteriol 48(Pt 1):317–320
Chiuchiolo MJ, Delgado MA, Farias RN, Salomon RA (2001) Growth-phase-dependent expression of the cyclopeptide antibiotic microcin J25. J Bacteriol 183(5):1755–1764. doi:10.1128/JB.183.5.1755-1764.2001
Constantine KL, Friedrichs MS, Detlefsen D, Nishio M, Tsunakawa M, Furumai T, Ohkuma H, Oki T, Hill S, Bruccoleri RE et al (1995) High-resolution solution structure of siamycin II: novel amphipathic character of a 21-residue peptide that inhibits HIV fusion. J Biomol NMR 5(3):271–286
Craik DJ, Daly NL (2007) NMR as a tool for elucidating the structures of circular and knotted proteins. Mol Biosyst 3(4):257–265. doi:10.1039/b616856f
Craik DJ, Malik U (2013) Cyclotide biosynthesis. Curr Opin Chem Biol 17(4):546–554. doi:10.1016/j.cbpa.2013.05.033
Dasgupta S, Huang KW, Wu J (2012) Trifluoromethyl acting as stopper in [2]rotaxane. Chem Commun (Camb) 48(40):4821–4823. doi:10.1039/c2cc31009k
Diep DB, Havarstein LS, Nes IF (1995) A bacteriocin-like peptide induces bacteriocin synthesis in Lactobacillus plantarum C11. Mol Microbiol 18(4):631–639
Diep DB, Havarstein LS, Nes IF (1996) Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11. J Bacteriol 178(15):4472–4483
Doidge EM (1915) A bacterial disease of the mango. Bacillus mangiferae n. sp. Ann Appl Biol 2:1–45
Ducasse R, Li Y, Blond A, Zirah S, Lescop E, Goulard C, Guittet E, Pernodet JL, Rebuffat S (2012a) Sviceucin, a lasso peptide from Streptomyces sviceus: isolation and structure analysis. J Pep Sci 18(Supp 1):67–68
Ducasse R, Yan K-P, Goulard C, Blond A, Li Y, Lescop E, Guittet E, Rebuffat S, Zirah S (2012b) Sequence determinants governing the topology and biological activity of a lasso peptide, microcin J25. ChemBioChem 13(3):371–380
Duquesne S, Destoumieux-Garzón D, Peduzzi J, Rebuffat S (2007) Microcins, gene-encoded antibacterial peptides from enterobacteria. Nat Prod Rep 24(4):708–734. doi:10.1039/b516237h
Eaton TE, Ford LM, Godfrey OW, Huber MLB, Zmijewski MJ (1989) Process for producing the A-21978C antibiotics. Vol US 4800157A. Google Patents
Esumi Y, Suzuki Y, Itoh Y, Uramoto M, Kimura K, Goto M, Yoshihama M, Ichikawa T (2002) Propeptin, a new inhibitor of prolyl endopeptidase produced by microbispora II. Determination of chemical structure. J Antibiot 55(3):296–300
Frechet D, Guitton JD, Herman F, Faucher D, Helynck G, Monegier du Sorbier B, Ridoux JP, James-Surcouf E, Vuilhorgne M (1994) Solution structure of RP 71955, a new 21 amino acid tricyclic peptide active against HIV-1 virus. Biochemistry 33(1):42–50
Gai Z, Yu B, Li L, Wang Y, Ma C, Feng J, Deng Z, Xu P (2007) Cometabolic degradation of dibenzofuran and dibenzothiophene by a newly isolated carbazole-degrading Sphingomonas sp. strain. Appl Environ Microbiol 73(9):2832–2838. doi:10.1128/AEM.02704-06
Hanka LJ, Dietz A (1973) U-42, 126, a new antimetabolite antibiotic: production, biological activity, and taxonomy of the producing microorganism. Antimicrob Agents Chemother 3(3):425–431
Hegemann JD, Zimmermann M, Xie X, Marahiel MA (2013a) Caulosegnins I-III: a highly diverse group of lasso peptides derived from a single biosynthetic gene cluster. J Am Chem Soc 135(1):210–222. doi:10.1021/ja308173b
Hegemann JD, Zimmermann M, Zhu S, Klug D, Marahiel MA (2013b) Lasso peptides from proteobacteria: genome mining employing heterologous expression and mass spectrometry. Biopolymers. doi:10.1002/bip.22326
Hegemann JD, Zimmermann M, Zhu S, Steuber H, Harms K, Xie X, Marahiel MA (2014) Xanthomonins I-III: a new class of lasso peptides with a seven-residue macrolactam ring. Angew Chem Int Ed Engl. doi:10.1002/anie.201309267
Helynck G, Dubertret C, Mayaux JF, Leboul J (1993) Isolation of RP 71955, a new anti-HIV-1 peptide secondary metabolite. J Antibiot 46(11):1756–1757
Hibbing ME, Fuqua C, Parsek MR, Peterson SB (2010) Bacterial competition: surviving and thriving in the microbial jungle. Nat Rev Microbiol 8(1):15–25. doi:10.1038/nrmicro2259
Hoshino Y, Satoh T (1985) Dependence on calcium ions of gelatin hydrolysis by Rhodopseudomonas capsulata but not Rhodopseudomonas gelatinosa. Agric Biol Chem 49(11):3331–3332
Inokoshi J, Matsuhama M, Miyake M, Ikeda H, Tomoda H (2012) Molecular cloning of the gene cluster for lariatin biosynthesis of Rhodococcus jostii K01-B0171. Appl Microbiol Biotechnol 95(2):451–460. doi:10.1007/s00253-012-3973-8
Iwatsuki M, Tomoda H, Uchida R, Gouda H, Hirono S, Omura S (2006) Lariatins, antimycobacterial peptides produced by Rhodococcus sp. K01-B0171, have a lasso structure. J Am Chem Soc 128(23):7486–7491
Iwatsuki M, Uchida R, Takakusagi Y, Matsumoto A, Jiang CL, Takahashi Y, Arai M, Kobayashi S, Matsumoto M, Inokoshi J, Tomoda H, Omura S (2007) Lariatins, novel anti-mycobacterial peptides with a lasso structure, produced by Rhodococcus jostii K01-B0171. J Antibiot 60(6):357–363. doi:10.1038/ja.2007.48
Jones JB, Lacy GH, Bouzar H, Stall RE, Schaad NW (2004) Reclassification of the xanthomonads associated with bacterial spot disease of tomato and pepper. Syst Appl Microbiol 27(6):755–762. doi:10.1078/0723202042369884
Katahira R, Shibata K, Yamasaki M, Matsuda Y, Yoshida M (1995) Solution structure of endothelin B receptor selective antagonist RES-701-1 determined by 1H NMR spectroscopy. Bioorg Med Chem 3(9):1273–1280
Katahira R, Yamasaki M, Matsuda Y, Yoshida M (1996) MS-271, a novel inhibitor of calmodulin-activated myosin light chain kinase from Streptomyces sp.–II. Solution structure of MS-271: characteristic features of the “lasso” structure. Bioorg Med Chem 4(1):121–129
Kersten RD, Yang YL, Xu Y, Cimermancic P, Nam SJ, Fenical W, Fischbach MA, Moore BS, Dorrestein PC (2011) A mass spectrometry-guided genome mining approach for natural product peptidogenomics. Nat Chem Biol 7(11):794–802. doi:10.1038/nchembio.684
Kimura K, Kanou F, Takahashi H, Esumi Y, Uramoto M, Yoshihama M (1997) Propeptin, a new inhibitor of prolyl endopeptidase produced by Microbispora. I. Fermentation, isolation and biological properties. J Antibiot 50(5):373–378
Kimura K, Yamazaki M, Sasaki N, Yamashita T, Negishi S, Nakamura T, Koshino H (2007) Novel propeptin analog, propeptin-2, missing two amino acid residues from the propeptin C-terminus loses antibiotic potency. J Antibiot 60(8):519–523
Knappe TA, Linne U, Robbel L, Marahiel MA (2009) Insights into the biosynthesis and stability of the lasso peptide capistruin. Chem Biol 16(12):1290–1298. doi:10.1016/j.chembiol.2009.11.009
Knappe TA, Linne U, Zirah S, Rebuffat S, Xie X, Marahiel MA (2008) Isolation and structural characterization of capistruin, a lasso peptide predicted from the genome sequence of Burkholderia thailandensis E264. J Am Chem Soc 130(34):11446–11454
Knappe TA, Linne U, Xie X, Marahiel MA (2010) The glucagon receptor antagonist BI-32169 constitutes a new class of lasso peptides. FEBS Lett 584(4):785–789. doi:10.1016/j.febslet.2009.12.046
Knappe TA, Manzenrieder F, Mas-Moruno C, Linne U, Sasse F, Kessler H, Xie X, Marahiel MA (2011) Introducing lasso peptides as molecular scaffolds for drug design: engineering of an integrin antagonist. Angew Chem Int Ed Engl 50(37):8714–8717. doi:10.1002/anie.201102190
Kuipers OP, Beerthuyzen MM, de Ruyter PG, Luesink EJ, de Vos WM (1995) Autoregulation of nisin biosynthesis in Lactococcus lactis by signal transduction. J Biol Chem 270(45):27299–27304
Lee CS, Kim KK, Aslam Z, Lee ST (2007) Rhodanobacter thiooxydans sp. nov., isolated from a biofilm on sulfur particles used in an autotrophic denitrification process. Int J Syst Evol Microbiol 57(8):1175–1179
Maksimov MO, Link AJ (2014) Prospecting genomes for lasso peptides. J Ind Microbiol Biotechnol 41(2):333–344. doi:10.1007/s10295-013-1357-4
Maksimov MO, Pelczer I, Link AJ (2012) Precursor-centric genome-mining approach for lasso peptide discovery. Proc Natl Acad Sci U S A. doi:10.1073/pnas.1208978109
Morishita Y, Chiba S, Tsukuda E, Tanaka T, Ogawa T, Yamasaki M, Yoshida M, Kawamoto I, Matsuda Y (1994) RES-701-1, a novel and selective endothelin type B receptor antagonist produced by Streptomyces sp. RE-701. I. Characterization of producing strain, fermentation, isolation, physico-chemical and biological properties. J Antibiot 47(3):269–275
Nar H, Schmid A, Puder C, Potterat O (2010) High-resolution crystal structure of a lasso peptide. ChemMedChem 5(10):1689–1692. doi:10.1002/cmdc.201000264
Ogawa T, Ochiai K, Tanaka T, Tsukuda E, Chiba S, Yano K, Yamasaki M, Yoshida M, Matsuda Y (1995) RES-701-2, -3 and -4, novel and selective endothelin type B receptor antagonists produced by Streptomyces sp. I. Taxonomy of producing strains, fermentation, isolation, and biochemical properties. J Antibiot 48(11):1213–1220
Pal R, Bala S, Dadhwal M, Kumar M, Dhingra G, Prakash O, Prabagaran SR, Shivaji S, Cullum J, Holliger C, Lal R (2005) Hexachlorocyclohexane-degrading bacterial strains Sphingomonas paucimobilis B90A, UT26 and Sp+, having similar lin genes, represent three distinct species, Sphingobium indicum sp. nov., Sphingobium japonicum sp. nov. and Sphingobium francense sp. nov., and reclassification of [Sphingomonas] chungbukensis as Sphingobium chungbukense comb. nov. Int J Syst Evol Microbiol 55(Pt 5):1965–1972. doi:10.1099/ijs.0.63201-0
Pan SJ, Link AJ (2011) Sequence diversity in the lasso peptide framework: discovery of functional microcin J25 variants with multiple amino acid substitutions. J Am Chem Soc 133(13):5016–5023. doi:10.1021/ja1109634
Pan SJ, Cheung WL, Link AJ (2010) Engineered gene clusters for the production of the antimicrobial peptide microcin J25. Protein Expr Purif 71(2):200–206. doi:10.1016/j.pep.2009.12.010
Pan SJ, Rajniak J, Maksimov MO, Link AJ (2011) The role of a conserved threonine residue in the leader peptide of lasso peptide precursors. Chem Commun (in press)
Partida-Martinez LP, Groth I, Schmitt I, Richter W, Roth M, Hertweck C (2007b) Burkholderia rhizoxinica sp. nov. and Burkholderia endofungorum sp. nov., bacterial endosymbionts of the plant-pathogenic fungus Rhizopus microsporus. Int J Syst Evol Microbiol 57(Pt 11):2583–2590. doi:10.1099/ijs.0.64660-0
Pérot-Taillandier M, Zirah S, Rebuffat S, Linne U, Marahiel MA, Cole RB, Tabet JC, Afonso C (2012) Determination of peptide topology through time-resolved double-resonance under electron capture dissociation conditions. Anal Chem 84(11):4957–4964. doi:10.1021/ac300607y
Poindexter JS (1964) Biological properties and classification of the Caulobacter group. Bacteriol Rev 28:231–295
Potterat O, Stefan H, Metzger JW, Gnau V, Zähner H, Jung G (1994) Aborycin—a tricyclic 21-peptide antibiotic isolated from Streptomyces griseoflavus. Liebigs Ann Chem 1994(7):741–743
Potterat O, Wagner K, Gemmecker G, Mack J, Puder C, Vettermann R, Streicher R (2004) BI-32169, a bicyclic 19-peptide with strong glucagon receptor antagonist activity from Streptomyces sp. J Nat Prod 67(9):1528–1531. doi:10.1021/np040093o
Rebuffat S, Blond A, Destoumieux-Garzón D, Goulard C, Peduzzi J (2004) Microcin J25, from the macrocyclic to the lasso structure: implications for biosynthetic, evolutionary and biotechnological perspectives. Curr Protein Pept Sci 5(5):383–391
Riley MA, Wertz JE (2002) Bacteriocins: evolution, ecology, and application. Annu Rev Microbiol 56:117–137. doi:10.1146/annurev.micro.56.012302.161024
Rosengren KJ, Clark RJ, Daly NL, Goransson U, Jones A, Craik DJ (2003) Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone. J Am Chem Soc 125(41):12464–12474
Rosengren KJ, Blond A, Afonso C, Tabet JC, Rebuffat S, Craik DJ (2004) Structure of thermolysin cleaved microcin J25: extreme stability of a two-chain antimicrobial peptide devoid of covalent links. Biochemistry 43(16):4696–4702
Salomón RA, Farías RN (1992) Microcin 25, a novel antimicrobial peptide produced by Escherichia coli. J Bacteriol 174(22):7428–7435
Scannell AG, Hill C, Ross RP, Marx S, Hartmeier W, Arendt EK (2000) Continuous production of lacticin 3147 and nisin using cells immobilized in calcium alginate. J Appl Microbiol 89(4):573–579. doi:jam1149
Severinov K, Semenova E, Kazakov A, Kazakov T, Gelfand MS (2007) Low-molecular-weight posttranslationally modified microcins. Mol Microbiol 65(6):1380–1394
Solbiati JO, Ciaccio M, Farias RN, Salomon RA (1996) Genetic analysis of plasmid determinants for microcin J25 production and immunity. J Bacteriol 178(12):3661–3663
Solbiati JO, Ciaccio M, Farías RN, González-Pastor JE, Moreno F, Salomón RA (1999) Sequence analysis of the four plasmid genes required to produce the circular peptide antibiotic microcin J25. J Bacteriol 181(8):2659–2662
Um S, Kim YJ, Kwon H, Wen H, Kim SH, Kwon HC, Park S, Shin J, Oh DC (2013) Sungsanpin, a lasso peptide from a deep-sea streptomycete. J Nat Prod 76(5):873–879. doi:10.1021/np300902g
Vancanneyt M, Schut F, Snauwaert C, Goris J, Swings J, Gottschal JC (2001) Sphingomonas alaskensis sp. nov., a dominant bacterium from a marine oligotrophic environment. Int J Syst Evol Microbiol 51(Pt 1):73–79
Weber W, Fischli W, Hochuli E, Kupfer E, Weibel EK (1991) Anantin–a peptide antagonist of the atrial natriuretic factor (ANF). I. Producing organism, fermentation, isolation and biological activity. J Antibiot 44(2):164–171
Wilson KA, Kalkum M, Ottesen J, Yuzenkova J, Chait BT, Landick R, Muir T, Severinov K, Darst SA (2003) Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail. J Am Chem Soc 125(41):12475–12483
Wyss DF, Lahm HW, Manneberg M, Labhardt AM (1991) Anantin—a peptide antagonist of the atrial natriuretic factor (ANF). II. Determination of the primary sequence by NMR on the basis of proton assignments. J Antibiot 44(2):172–180
Xie X, Marahiel MA (2012) NMR as an effective tool for the structure determination of lasso peptides. Chembiochem 13(5):621–625. doi:10.1002/cbic.201100754
Yamasaki M, Yano K, Yoshida M, Matsuda Y, Yamaguchi K (1994) RES-701-1, a novel and selective endothelin type B receptor antagonist produced by Streptomyces sp. RE-701. II. Determination of the primary sequence. J Antibiot 47(3):276–280
Yano K, Yamasaki M, Yoshida M, Matsuda Y, Yamaguchi K (1995) RES-701-2, a novel and selective endothelin type B receptor antagonist produced by Streptomyces sp. II. Determination of the primary structure. J Antibiot 48(11):1368–1370
Yano K, Toki S, Nakanishi S, Ochiai K, Ando K, Yoshida M, Matsuda Y, Yamasaki M (1996) MS-271, a novel inhibitor of calmodulin-activated myosin light chain kinase from Streptomyces sp.-I. Isolation, structural determination and biological properties of MS-271. Bioorg Med Chem 4(1):115–120
Zhang K, Han W, Zhang R, Xu X, Pan Q, Hu X (2007) Phenylobacterium zucineum sp. nov., a facultative intracellular bacterium isolated from a human erythroleukemia cell line K562. Syst Appl Microbiol 30(3):207–212. doi:10.1016/j.syapm.2006.07.002
Zimmermann M, Hegemann JD, Xie X, Marahiel MA (2013) The astexin-1 lasso peptides: biosynthesis, stability, and structural studies. Chem Biol 20(4):558–569. doi:10.1016/j.chembiol.2013.03.013
Zirah S, Afonso C, Linne U, Knappe TA, Marahiel MA, Rebuffat S, Tabet JC (2011) Topoisomer differentiation of molecular knots by FTICR MS: lessons from class II lasso peptides J Am Soc Mass Spectrom 22(3):467–479
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
Copyright information
© 2015 Yanyan Li, Séverine Zirah and Sylvie Rebuffat
About this chapter
Cite this chapter
Li, Y., Zirah, S., Rebuffat, S. (2015). From the Producer Microorganisms to the Lasso Scaffold. In: Lasso Peptides. SpringerBriefs in Microbiology. Springer, New York, NY. https://doi.org/10.1007/978-1-4939-1010-6_2
Download citation
DOI: https://doi.org/10.1007/978-1-4939-1010-6_2
Published:
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4939-1009-0
Online ISBN: 978-1-4939-1010-6
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)