Ingeborg Grgurina , Feliciana Mariotti , Vincenzo Fogliano , Monica Gallo , Andrea Scaloni , Nicola S. Iacobellis , Pietro Lo Cantore , Luisa Mannina , Valeria van Axel Castelli , Maria Luigia Greco , Antonio Graniti
{"title":"A new syringopeptin produced by bean strains of Pseudomonas syringae pv. syringae","authors":"Ingeborg Grgurina , Feliciana Mariotti , Vincenzo Fogliano , Monica Gallo , Andrea Scaloni , Nicola S. Iacobellis , Pietro Lo Cantore , Luisa Mannina , Valeria van Axel Castelli , Maria Luigia Greco , Antonio Graniti","doi":"10.1016/S0167-4838(02)00283-2","DOIUrl":null,"url":null,"abstract":"<div><p>Two strains (B728a and Y37) of the phytopathogenic bacterium <em>Pseudomonas syringae</em> pv. <em>syringae</em> isolated from bean (<em>Phaseolus vulgaris</em>) plants were shown to produce in culture both syringomycin, a lipodepsinonapeptide secreted by the majority of the strains of the bacterium, and a new form of syringopeptin, SP<sub>22</sub>Phv. The structure of the latter metabolite was elucidated by the combined use of mass spectrometry (MS), nuclear magnetic resonance (NMR) spectroscopy and chemical procedures. Comparative phytotoxic and antimicrobial assays showed that SP<sub>22</sub>Phv did not differ substantially from the previously characterized syringopeptin 22 (SP<sub>22</sub>) as far as toxicity to plants was concerned, but was less active in inhibiting the growth of the test fungi <em>Rhodotorula pilimanae</em> and <em>Geotrichum candidum</em> and of the Gram-positive bacterium <em>Bacillus megaterium</em>.</p></div>","PeriodicalId":100166,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2002-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0167-4838(02)00283-2","citationCount":"38","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0167483802002832","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 38
Abstract
Two strains (B728a and Y37) of the phytopathogenic bacterium Pseudomonas syringae pv. syringae isolated from bean (Phaseolus vulgaris) plants were shown to produce in culture both syringomycin, a lipodepsinonapeptide secreted by the majority of the strains of the bacterium, and a new form of syringopeptin, SP22Phv. The structure of the latter metabolite was elucidated by the combined use of mass spectrometry (MS), nuclear magnetic resonance (NMR) spectroscopy and chemical procedures. Comparative phytotoxic and antimicrobial assays showed that SP22Phv did not differ substantially from the previously characterized syringopeptin 22 (SP22) as far as toxicity to plants was concerned, but was less active in inhibiting the growth of the test fungi Rhodotorula pilimanae and Geotrichum candidum and of the Gram-positive bacterium Bacillus megaterium.