دورية أكاديمية

Co-occurrence of linear and cyclic pelgipeptins in broth cultures of Paenibacillus elgii AC13.

التفاصيل البيبلوغرافية
العنوان: Co-occurrence of linear and cyclic pelgipeptins in broth cultures of Paenibacillus elgii AC13.
المؤلفون: de Araújo TF; Graduate Program in Genomic Sciences and Biotechnology, Universidade Católica de Brasília, SGAN 916, Brasília, DF, 70790-160, Brazil., Ortega DB; Graduate Program in Genomic Sciences and Biotechnology, Universidade Católica de Brasília, SGAN 916, Brasília, DF, 70790-160, Brazil., da Costa RA; Graduate Program in Genomic Sciences and Biotechnology, Universidade Católica de Brasília, SGAN 916, Brasília, DF, 70790-160, Brazil., Andrade IEPC; Graduate Program in Genomic Sciences and Biotechnology, Universidade Católica de Brasília, SGAN 916, Brasília, DF, 70790-160, Brazil., Fulgêncio DLA; Graduate Program in Genomic Sciences and Biotechnology, Universidade Católica de Brasília, SGAN 916, Brasília, DF, 70790-160, Brazil., Mendonça ML; Graduate Program in Genomic Sciences and Biotechnology, Universidade Católica de Brasília, SGAN 916, Brasília, DF, 70790-160, Brazil., Costa FS; Graduate Program in Genomic Sciences and Biotechnology, Universidade Católica de Brasília, SGAN 916, Brasília, DF, 70790-160, Brazil., Leite ML; Graduate Program in Genomic Sciences and Biotechnology, Universidade Católica de Brasília, SGAN 916, Brasília, DF, 70790-160, Brazil., Ramada MHS; Graduate Program in Genomic Sciences and Biotechnology, Universidade Católica de Brasília, SGAN 916, Brasília, DF, 70790-160, Brazil., Barreto CC; Graduate Program in Genomic Sciences and Biotechnology, Universidade Católica de Brasília, SGAN 916, Brasília, DF, 70790-160, Brazil. criscbarreto@gmail.com.
المصدر: Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] [Braz J Microbiol] 2021 Dec; Vol. 52 (4), pp. 1825-1833. Date of Electronic Publication: 2021 Aug 26.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Springer International Publishing Country of Publication: Brazil NLM ID: 101095924 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1678-4405 (Electronic) Linking ISSN: 15178382 NLM ISO Abbreviation: Braz J Microbiol Subsets: MEDLINE
أسماء مطبوعة: Publication: 2019- : Switzerland, AG : Springer International Publishing
Original Publication: Rio de Janeiro, RJ, Brasil : Sociedade Brasileira de Microbiologia
مواضيع طبية MeSH: Lipopeptides*/chemistry , Lipopeptides*/genetics , Lipopeptides*/isolation & purification , Lipopeptides*/pharmacology , Paenibacillus*/chemistry , Paenibacillus*/genetics, Anti-Infective Agents/chemistry ; Anti-Infective Agents/isolation & purification ; Anti-Infective Agents/pharmacology ; Bacteria/drug effects
مستخلص: Paenibacillus elgii AC13 produces antimicrobial lipopeptides of agricultural and pharmaceutical importance. It secretes four cyclic lipopeptides named pelgipeptins, previously characterized in P. elgii B69. These lipopeptides result from the expression of a nonribosomal peptide gene cluster. P. elgii AC13 also produced two linear lipopeptides with ratios of [M + H] + 1105 and 1119 m/z. These compounds were previously observed in Paenibacillus sp. strain OSY-N, but due to purification difficulties, their characterization was executed using synthetically produced linear pelgipeptins. In the present study, purification was achieved from the supernatants of cultures from three complex media by high-performance liquid chromatography. The partial characterization of linear pelgipeptins revealed the similar antimicrobial activity and cytotoxicity of their synthetically produced counterparts, known as paenipeptins. Cyclic forms were highly stable to changes in pH, temperature, and organic extraction with n-butanol as shown by mass spectrometry (MALDI-TOF); therefore, these steps did not cause the hydrolysis of pelgipeptins. A low-activity thioesterase could also generate the linear isoforms observed; this enzyme catalyzes the cyclization process and is coded in the same gene cluster. Alternatively, the cyclic forms were hydrolyzed by an unknown protease produced during growth in the complex medium used in the present study. Although culture conditions are known to produce pelgipeptins with different yields and amino acid compositions, the occurrence of linear and cyclic forms simultaneously has not yet been reported. A mixture of cyclic and linear pelgipeptins presents a potential advantage of the higher antimicrobial activity of cyclic forms combined with the lower cytotoxicity of linear isoforms.
(© 2021. Sociedade Brasileira de Microbiologia.)
References: Ding R, Wu X-CC, Qian C-DD, Teng Y, Li O, Zhan Z-JJ, Zhao Y-HH (2011) Isolation and identification of lipopeptide antibiotics from Paenibacillus elgii B69 with inhibitory activity against methicillin-resistant Staphylococcus aureus. J Microbiol 49:942–949. https://doi.org/10.1007/s12275-011-1153-7. (PMID: 10.1007/s12275-011-1153-722203557)
Wu XC, Shen XB, Ding R, Qian CD, Fang HH, Li O (2010) Isolation and partial characterization of antibiotics produced by Paenibacillus elgii B69. FEMS Microbiol Lett 310:32–38. https://doi.org/10.1111/j.1574-6968.2010.02040.x. (PMID: 10.1111/j.1574-6968.2010.02040.x20618851)
Qian CD, Liu TZ, Zhou SL, Ding R, Zhao WP, Li O, Wu XC (2012) Identification and functional analysis of gene cluster involvement in biosynthesis of the cyclic lipopeptide antibiotic pelgipeptin produced by Paenibacillus elgii. BMC Microbiol 12:197. https://doi.org/10.1186/1471-2180-12-197. (PMID: 10.1186/1471-2180-12-197229584533479019)
Kim J, Il Kim P, Bong KM, Il Kim J, Shin SY, Song J, Min HJ, Lee CW (2018) Isolation and structural elucidation of pelgipeptin E, a novel pore-forming pelgipeptin analog from Paenibacillus elgii with low hemolytic activity. J Antibiot (Tokyo) 71:1008–1017. https://doi.org/10.1038/s41429-018-0095-2. (PMID: 10.1038/s41429-018-0095-2)
Huang E, Yang X, Zhang L, Moon SH, Yousef AE (2017) New Paenibacillus strain produces a family of linear and cyclic antimicrobial lipopeptides: cyclization is not essential for their antimicrobial activity. FEMS Microbiol Lett 364(8). https://doi.org/10.1093/femsle/fnx049.
Moon SH, Huang E (2019) Novel linear lipopeptide paenipeptin C’ binds to lipopolysaccharides and lipoteichoic acid and exerts bactericidal activity by the disruption of cytoplasmic membrane. BMC Microbiol 19:6. https://doi.org/10.1186/s12866-018-1381-7. (PMID: 10.1186/s12866-018-1381-7306215906325689)
Ortega DB, Costa RA, Pires AS, Araújo TF, Araújo JF, Kurokawa AS, Magalhães BS, Reis AMM, Franco OL, Kruger RH, Pappas GJ, Barreto CC (2018) Draft genome sequence of the antimicrobial-producing strain Paenibacillus elgii AC13. Genome Announc 6(26). https://doi.org/10.1128/genomeA.00573-18.
Costa RA, Ortega DB, Fulgêncio DLA, Costa FS, Araújo TF, Barreto CC (2019) Checkerboard testing method indicates synergic effect of pelgipeptins against multidrug resistant Klebsiella pneumoniae. Biotechnol Res Innov 3:187–191. https://doi.org/10.1016/j.biori.2018.12.001. (PMID: 10.1016/j.biori.2018.12.001)
Murphy JB, Kies MW (1960) Note on spectrophotometric determination of proteins in dilute solutions. BBA - Biochim Biophys Acta 45:382–384. https://doi.org/10.1016/0006-3002(60)91464-5. (PMID: 10.1016/0006-3002(60)91464-5)
Clinical and Laboratory Standards Institute - CLSI (2004) Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically. Document M07-A6. Wayne, PA.
Fulgêncio DLA, da Costa RA, Guilhelmelli F, de Silva CM, S, Ortega DB, de Araujo TF, Silva PS, Silva-Pereira I, Albuquerque P, Barreto CC, (2021) In vitro antifungal activity of pelgipeptins against human pathogenic fungi and Candida albicans biofilms. AIMS Microbiol 7:28–39. https://doi.org/10.3934/microbiol.2021003. (PMID: 10.3934/microbiol.2021003336597677921374)
Mosmann T (1983) Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 65:55–63. https://doi.org/10.1016/0022-1759(83)90303-4. (PMID: 10.1016/0022-1759(83)90303-46606682)
Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ (1990) Basic local alignment search tool. J Mol Biol 215:403–410. https://doi.org/10.1016/S0022-2836(05)80360-2. (PMID: 10.1016/S0022-2836(05)80360-2)
Kearse M, Moir R, Wilson A, Stones-Havas S, Cheung M, Sturrock S, Buxton S, Cooper A, Markowitz S, Duran C, Thierer T, Ashton B, Meintjes P, Drummond A (2012) Geneious Basic: an integrated and extendable desktop software platform for the organization and analysis of sequence data. Bioinformatics 28:1647–1649. https://doi.org/10.1093/bioinformatics/bts199. (PMID: 10.1093/bioinformatics/bts19933718323371832)
Blin K, Shaw S, Steinke K, Villebro R, Ziemert N, Lee SY, Medema MH, Weber T (2019) antiSMASH 5.0: updates to the secondary metabolite genome mining pipeline. Nucleic Acids Res 47:W81–W87. https://doi.org/10.1093/nar/gkz310. (PMID: 10.1093/nar/gkz310310325196602434)
Shaligram NS, Singhal RS (2010) Surfactin - a review on biosynthesis, fermentation, purification and applications. Food Technol Biotechnol 48:119–134.
Sieber SA, Marahiel MA (2005) Molecular mechanisms underlying nonribosomal peptide synthesis: approaches to new antibiotics. Chem Rev 105(2):715–738. https://doi.org/10.1021/cr0301191. (PMID: 10.1021/cr030119115700962)
Grangemard I, Wallach J, Peypoux F (1999) Evidence of surfactin hydrolysis by a bacterial endoprotease. Biotechnol Lett 21:241–244. https://doi.org/10.1023/A:1005444717166. (PMID: 10.1023/A:1005444717166)
Hoefler BC, Gorzelnik KV, Yang JY, Hendricks N, Dorrestein PC, Straight PD (2012) Enzymatic resistance to the lipopeptide surfactin as identified through imaging mass spectrometry of bacterial competition. Proc Natl Acad Sci 109:13082–13087. https://doi.org/10.1073/pnas.1205586109. (PMID: 10.1073/pnas.1205586109228262293420176)
Geissler M, Heravi KM, Henkel M, Hausmann R (2019) Lipopeptide biosurfactants from Bacillus species. Elsevier Inc, Second Edi. (PMID: 10.1016/B978-0-12-812705-6.00006-X)
Akpa E, Jacques P, Wathelet B, Paquot M, Fuchs R, Budzikiewicz H, Thonart P (2001) Influence of culture conditions on lipopeptide production by Bacillus subtilis. Appl Biochem Biotechnol 91–93:551–562. https://doi.org/10.1385/ABAB:91-93:1-9:551. (PMID: 10.1385/ABAB:91-93:1-9:55111963884)
معلومات مُعتمدة: 560915/2010-1 Conselho Nacional de Desenvolvimento Científico e Tecnológico; 001 Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
فهرسة مساهمة: Keywords: Antimicrobial agent; Lipopeptides; MALDI-TOF; NRP isoforms; Paenibacillus elgii; Pelgipeptin
المشرفين على المادة: 0 (Anti-Infective Agents)
0 (Lipopeptides)
SCR Organism: Paenibacillus elgii
تواريخ الأحداث: Date Created: 20210826 Date Completed: 20211214 Latest Revision: 20220827
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC8578282
DOI: 10.1007/s42770-021-00597-x
PMID: 34435341
قاعدة البيانات: MEDLINE
الوصف
تدمد:1678-4405
DOI:10.1007/s42770-021-00597-x