Show legend Show as text

Structure type: cyclic polymer repeating unit ; 1404.67572 [M+Na]+, n=1
C₆₂H₉₉N₁₁O₂₄
Trivial name: hassalidin A
Compound class: glycopeptide
Contained glycoepitopes: IEDB_137485,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_72

• Article ID: 5580
  Neuhof T, Schmieder P, Preussel K, Dieckmann R, Pham H, Bartl F, von Döhren H "Hassallidin A, a glycosylated lipopeptide with antifungal activity from the cyanobacterium Hassallia sp." - Journal of Natural Products 68(5) (2005) 695-700
  

  Hassallidin A (1), a new antifungal glycosylated lipopeptide, was isolated from an epilithic cyanobacterium collected in Bellano, Italy, identified as Tolypothrix (basionym Hassallia) species. Chemical, mass spectrometric, and spectroscopic analyses, including one- and two-dimensional NMR, were performed to determine an esterified eight-residue cyclic peptide linked with a carbohydrate and a fatty acid residue. Chiral GC-MS analysis revealed the occurrence of the nonproteinogenic amino acids D-allo-Thr, D-Thr, D-Tyr, D-Gln, and dehydroaminobutyric acid (Dhb) within the peptide moiety. The additional components of hassallidin A could be identified as alpha,beta-dihydroxytetradecanoic acid (Dht) and mannose. This is the first report on a cyclic peptide of cyanobacterial origin that contains both a fatty acid and a carbohydrate moiety. Compound 1 exhibits antifungal activity against Aspergillus fumigatus and Candida albicans with MIC values of 4.8 μg/mL for both test organisms

  hassalidin A, antifungal activity, Tolypothrix, cyclic peptide

  NCBI PubMed ID: 15921412
  Publication DOI: 10.1021/np049671r
  Journal NLM ID: 7906882
  Publisher: American Society of Pharmacognosy
  Correspondence: doehren@chem.tu-berlin.de
  Institutions: Institut für Chemie, Fak. II, Technische Universität Berlin, Berlin, Germany, Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany, Institut für Medizinische Physik und Biophysik, Charité-Universitätsmedizin Berlin, Humboldt-Universität, Berlin, Germany, Zentrum für Biophysik und Bioinformatik, Humboldt-Universität, Berlin, Germany
  Methods: 13C NMR, 1H NMR, NMR-2D, IR, GC-MS, ESI-MS, acid hydrolysis, ESI-ICR-MS, amino acid analysis, MALDI-TOF MS, HPLC, UV, extraction, 15N NMR, cell growth, derivatization, evaporation, centrifugation, antifungal activity test, optical density measurement
  
   
  
  Hassallia sp. B02-07
  CSDB ID 47392 (all data & tools)

Show legend Show as text

Structure type: cyclic polymer repeating unit ; n=1
Trivial name: mannopeptimycin δ
Compound class: glycopeptide
Contained glycoepitopes: IEDB_130701,IEDB_144983,IEDB_150900,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 5599
  Wu MC, Styles MQ, Law BJ, Struck AW, Nunns L, Micklefield J "Engineered biosynthesis of enduracidin lipoglycopeptide antibiotics using the ramoplanin mannosyltransferase Ram29" - Microbiology 161(7) (2015) 1338-1347
  

  The lipopeptides ramoplanin from Actinoplanes sp. ATCC 33076 and enduracidin produced by Streptomyces fungicidicus are effective antibiotics against a number of drug-resistant Gram-positive pathogens. While these two antibiotics share a similar cyclic peptide structure, comprising 17 amino acids with an N-terminal fatty acid side chain, ramoplanin has a di-mannose moiety that enduracidin lacks. The mannosyl substituents of ramoplanin enhance aqueous solubility, which was important in the development of ramoplanin as a potential treatment for Clostridium difficile infections. In this study we have determined the function of the putative mannosyltransferase encoded by ram29 from the ramoplanin biosynthetic gene cluster. Bioinformatics revealed that Ram29 is an integral membrane protein with a putative DxD motif that is suggested to bind to, and activate, a polyprenyl phosphomannose donor and an extracytoplasmic C-terminal domain that is predicted to bind the ramoplanin aglycone acceptor. The ram29 gene was cloned into the tetracycline inducible plasmid pMS17 and integrated into the genome of the enduracidin producer S. fungicidicus. Induction of ram29 expression in S. fungicidicus resulted in the production of monomannosylated enduracidin derivatives, which are not present in the WT strain. Tandem MS analysis showed that mannosylation occurs on the Hpg11 residue of enduracidin. In addition to confirming the function of Ram29, these findings demonstrate how the less common, membrane-associated, polyprenyl phosphosugar-dependent glycosyltransferases can be used in natural product glycodiversification. Such a strategy may be valuable in future biosynthetic engineering approaches aimed at improving the physico-chemical and biological properties of bioactive secondary metabolites including antibiotics

  biosynthesis, antibiotics, nonribosomal peptides, lipoglycopeptides, mannosylation, glycodiversification

  NCBI PubMed ID: 25878261
  Publication DOI: 10.1099/mic.0.000095
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: Jason.micklefield@manchester.ac.uk
  Institutions: School of Chemistry and Manchester Institute of Biotechnology, The University of Manchester, Manchester, UK
  Methods: PCR, DNA sequencing, DNA techniques, HPLC, UV, extraction, ESI-QTOF-MS/MS, LC-ESI-MS, cell growth, centrifugation
  
   
  
  Streptomyces hygroscopicus LL-AC98
  CSDB ID 47729 (all data & tools)
• Article ID: 5602
  Singh MP, Petersen PJ, Weiss WJ, Janso JE, Luckman SW, Lenoy EB, Bradford PA, Testa RT, Greenstein M "Mannopeptimycins, new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98: antibacterial and mechanistic activities" - Antimicrobial Agents and Chemotherapy 47(1) (2003) 62-69
  

  Mannopeptimycins alpha, beta, gamma, delta, and epsilon are new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98. Mannopeptimycins gamma, delta, and epsilon, which have an isovaleryl substitution at various positions on the terminal mannose of the disaccharide moiety, demonstrated moderate to good antibacterial activities. Mannopeptimycin epsilon was the most active component against methicillin-resistant staphylococci and vancomycin-resistant enterococci (MICs, 2 to 4 μg/ml for staphylococci and streptococci and 4 to 32 μg/ml for enterococci), while mannopeptimycins gamma and delta were two- to fourfold less active. Mannopeptimycins alpha and beta, which lack the isovaleryl substitution and the disaccharide moiety, respectively, had poor antibacterial activities. The in vivo efficacies of the mannopeptimycins in Staphylococcus aureus mouse protection studies paralleled their in vitro activities. The median effective doses of mannopeptimycins gamma, delta, and epsilon were 3.8, 2.6, and 0.59 mg/kg of body weight, respectively. The mannopeptimycins were inactive against cell wall-deficient S. aureus and caused spheroplasting of Escherichia coli imp similar to that observed with penicillin G in an osmotically protective medium. Mannopeptimycin delta rapidly inhibited [(3)H]N-acetylglucosamine incorporation into peptidoglycan in Bacillus subtilis and had no effect on DNA, RNA, or protein biosynthesis. On the basis of the observations presented above, an effect on cell wall biosynthesis was suggested as the primary mode of action for mannopeptimycin delta. The mannopeptimycins were inactive against Candida albicans, did not initiate hemolysis of human erythrocytes, and did not promote potassium ion leakage from E. coli imp, suggesting a lack of membrane damage to prokaryotic or eukaryotic cells

  glycopeptides, antibiotics, mannopeptimycins, Streptomyces hygroscopicus LL-AC98

  NCBI PubMed ID: 12499170
  Publication DOI: 10.1128/aac.47.1.62-69.2003
  Journal NLM ID: 0315061
  Correspondence: singhm@wyeth.com
  Institutions: Natural Products Microbiology, Wyeth Research, Pearl River, NY, USA, Antibacterial Research, Infectious Disease Section, Wyeth Research, Pearl River, NY, USA
  Methods: biological assays, cell growth, antibacterial assay
  
   
  
  Streptomyces hygroscopicus LL-AC98
  CSDB ID 47740 (all data & tools)

Show legend Show as text

Structure type: cyclic polymer repeating unit ; n=1
Trivial name: mannopeptimycin α
Compound class: glycopeptide
Contained glycoepitopes: IEDB_130701,IEDB_144983,IEDB_150900,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 5602
  Singh MP, Petersen PJ, Weiss WJ, Janso JE, Luckman SW, Lenoy EB, Bradford PA, Testa RT, Greenstein M "Mannopeptimycins, new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98: antibacterial and mechanistic activities" - Antimicrobial Agents and Chemotherapy 47(1) (2003) 62-69
  

  Mannopeptimycins alpha, beta, gamma, delta, and epsilon are new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98. Mannopeptimycins gamma, delta, and epsilon, which have an isovaleryl substitution at various positions on the terminal mannose of the disaccharide moiety, demonstrated moderate to good antibacterial activities. Mannopeptimycin epsilon was the most active component against methicillin-resistant staphylococci and vancomycin-resistant enterococci (MICs, 2 to 4 μg/ml for staphylococci and streptococci and 4 to 32 μg/ml for enterococci), while mannopeptimycins gamma and delta were two- to fourfold less active. Mannopeptimycins alpha and beta, which lack the isovaleryl substitution and the disaccharide moiety, respectively, had poor antibacterial activities. The in vivo efficacies of the mannopeptimycins in Staphylococcus aureus mouse protection studies paralleled their in vitro activities. The median effective doses of mannopeptimycins gamma, delta, and epsilon were 3.8, 2.6, and 0.59 mg/kg of body weight, respectively. The mannopeptimycins were inactive against cell wall-deficient S. aureus and caused spheroplasting of Escherichia coli imp similar to that observed with penicillin G in an osmotically protective medium. Mannopeptimycin delta rapidly inhibited [(3)H]N-acetylglucosamine incorporation into peptidoglycan in Bacillus subtilis and had no effect on DNA, RNA, or protein biosynthesis. On the basis of the observations presented above, an effect on cell wall biosynthesis was suggested as the primary mode of action for mannopeptimycin delta. The mannopeptimycins were inactive against Candida albicans, did not initiate hemolysis of human erythrocytes, and did not promote potassium ion leakage from E. coli imp, suggesting a lack of membrane damage to prokaryotic or eukaryotic cells

  glycopeptides, antibiotics, mannopeptimycins, Streptomyces hygroscopicus LL-AC98

  NCBI PubMed ID: 12499170
  Publication DOI: 10.1128/aac.47.1.62-69.2003
  Journal NLM ID: 0315061
  Correspondence: singhm@wyeth.com
  Institutions: Natural Products Microbiology, Wyeth Research, Pearl River, NY, USA, Antibacterial Research, Infectious Disease Section, Wyeth Research, Pearl River, NY, USA
  Methods: biological assays, cell growth, antibacterial assay
  
   
  
  Streptomyces hygroscopicus LL-AC98
  CSDB ID 47737 (all data & tools)

Show legend Show as text

Structure type: cyclic polymer repeating unit ; n=1
Trivial name: mannopeptimycin β
Compound class: glycopeptide
Contained glycoepitopes: IEDB_150900

• Article ID: 5602
  Singh MP, Petersen PJ, Weiss WJ, Janso JE, Luckman SW, Lenoy EB, Bradford PA, Testa RT, Greenstein M "Mannopeptimycins, new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98: antibacterial and mechanistic activities" - Antimicrobial Agents and Chemotherapy 47(1) (2003) 62-69
  

  Mannopeptimycins alpha, beta, gamma, delta, and epsilon are new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98. Mannopeptimycins gamma, delta, and epsilon, which have an isovaleryl substitution at various positions on the terminal mannose of the disaccharide moiety, demonstrated moderate to good antibacterial activities. Mannopeptimycin epsilon was the most active component against methicillin-resistant staphylococci and vancomycin-resistant enterococci (MICs, 2 to 4 μg/ml for staphylococci and streptococci and 4 to 32 μg/ml for enterococci), while mannopeptimycins gamma and delta were two- to fourfold less active. Mannopeptimycins alpha and beta, which lack the isovaleryl substitution and the disaccharide moiety, respectively, had poor antibacterial activities. The in vivo efficacies of the mannopeptimycins in Staphylococcus aureus mouse protection studies paralleled their in vitro activities. The median effective doses of mannopeptimycins gamma, delta, and epsilon were 3.8, 2.6, and 0.59 mg/kg of body weight, respectively. The mannopeptimycins were inactive against cell wall-deficient S. aureus and caused spheroplasting of Escherichia coli imp similar to that observed with penicillin G in an osmotically protective medium. Mannopeptimycin delta rapidly inhibited [(3)H]N-acetylglucosamine incorporation into peptidoglycan in Bacillus subtilis and had no effect on DNA, RNA, or protein biosynthesis. On the basis of the observations presented above, an effect on cell wall biosynthesis was suggested as the primary mode of action for mannopeptimycin delta. The mannopeptimycins were inactive against Candida albicans, did not initiate hemolysis of human erythrocytes, and did not promote potassium ion leakage from E. coli imp, suggesting a lack of membrane damage to prokaryotic or eukaryotic cells

  glycopeptides, antibiotics, mannopeptimycins, Streptomyces hygroscopicus LL-AC98

  NCBI PubMed ID: 12499170
  Publication DOI: 10.1128/aac.47.1.62-69.2003
  Journal NLM ID: 0315061
  Correspondence: singhm@wyeth.com
  Institutions: Natural Products Microbiology, Wyeth Research, Pearl River, NY, USA, Antibacterial Research, Infectious Disease Section, Wyeth Research, Pearl River, NY, USA
  Methods: biological assays, cell growth, antibacterial assay
  
   
  
  Streptomyces hygroscopicus LL-AC98
  CSDB ID 47738 (all data & tools)

Show legend Show as text

Structure type: cyclic polymer repeating unit ; n=1
Trivial name: mannopeptimycin γ
Compound class: glycopeptide
Contained glycoepitopes: IEDB_130701,IEDB_144983,IEDB_150900,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 5602
  Singh MP, Petersen PJ, Weiss WJ, Janso JE, Luckman SW, Lenoy EB, Bradford PA, Testa RT, Greenstein M "Mannopeptimycins, new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98: antibacterial and mechanistic activities" - Antimicrobial Agents and Chemotherapy 47(1) (2003) 62-69
  

  Mannopeptimycins alpha, beta, gamma, delta, and epsilon are new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98. Mannopeptimycins gamma, delta, and epsilon, which have an isovaleryl substitution at various positions on the terminal mannose of the disaccharide moiety, demonstrated moderate to good antibacterial activities. Mannopeptimycin epsilon was the most active component against methicillin-resistant staphylococci and vancomycin-resistant enterococci (MICs, 2 to 4 μg/ml for staphylococci and streptococci and 4 to 32 μg/ml for enterococci), while mannopeptimycins gamma and delta were two- to fourfold less active. Mannopeptimycins alpha and beta, which lack the isovaleryl substitution and the disaccharide moiety, respectively, had poor antibacterial activities. The in vivo efficacies of the mannopeptimycins in Staphylococcus aureus mouse protection studies paralleled their in vitro activities. The median effective doses of mannopeptimycins gamma, delta, and epsilon were 3.8, 2.6, and 0.59 mg/kg of body weight, respectively. The mannopeptimycins were inactive against cell wall-deficient S. aureus and caused spheroplasting of Escherichia coli imp similar to that observed with penicillin G in an osmotically protective medium. Mannopeptimycin delta rapidly inhibited [(3)H]N-acetylglucosamine incorporation into peptidoglycan in Bacillus subtilis and had no effect on DNA, RNA, or protein biosynthesis. On the basis of the observations presented above, an effect on cell wall biosynthesis was suggested as the primary mode of action for mannopeptimycin delta. The mannopeptimycins were inactive against Candida albicans, did not initiate hemolysis of human erythrocytes, and did not promote potassium ion leakage from E. coli imp, suggesting a lack of membrane damage to prokaryotic or eukaryotic cells

  glycopeptides, antibiotics, mannopeptimycins, Streptomyces hygroscopicus LL-AC98

  NCBI PubMed ID: 12499170
  Publication DOI: 10.1128/aac.47.1.62-69.2003
  Journal NLM ID: 0315061
  Correspondence: singhm@wyeth.com
  Institutions: Natural Products Microbiology, Wyeth Research, Pearl River, NY, USA, Antibacterial Research, Infectious Disease Section, Wyeth Research, Pearl River, NY, USA
  Methods: biological assays, cell growth, antibacterial assay
  
   
  
  Streptomyces hygroscopicus LL-AC98
  CSDB ID 47739 (all data & tools)

Show legend Show as text

Structure type: cyclic polymer repeating unit ; n=1
Trivial name: mannopeptimycin ε
Compound class: glycopeptide
Contained glycoepitopes: IEDB_130701,IEDB_144983,IEDB_150900,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 5602
  Singh MP, Petersen PJ, Weiss WJ, Janso JE, Luckman SW, Lenoy EB, Bradford PA, Testa RT, Greenstein M "Mannopeptimycins, new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98: antibacterial and mechanistic activities" - Antimicrobial Agents and Chemotherapy 47(1) (2003) 62-69
  

  Mannopeptimycins alpha, beta, gamma, delta, and epsilon are new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98. Mannopeptimycins gamma, delta, and epsilon, which have an isovaleryl substitution at various positions on the terminal mannose of the disaccharide moiety, demonstrated moderate to good antibacterial activities. Mannopeptimycin epsilon was the most active component against methicillin-resistant staphylococci and vancomycin-resistant enterococci (MICs, 2 to 4 μg/ml for staphylococci and streptococci and 4 to 32 μg/ml for enterococci), while mannopeptimycins gamma and delta were two- to fourfold less active. Mannopeptimycins alpha and beta, which lack the isovaleryl substitution and the disaccharide moiety, respectively, had poor antibacterial activities. The in vivo efficacies of the mannopeptimycins in Staphylococcus aureus mouse protection studies paralleled their in vitro activities. The median effective doses of mannopeptimycins gamma, delta, and epsilon were 3.8, 2.6, and 0.59 mg/kg of body weight, respectively. The mannopeptimycins were inactive against cell wall-deficient S. aureus and caused spheroplasting of Escherichia coli imp similar to that observed with penicillin G in an osmotically protective medium. Mannopeptimycin delta rapidly inhibited [(3)H]N-acetylglucosamine incorporation into peptidoglycan in Bacillus subtilis and had no effect on DNA, RNA, or protein biosynthesis. On the basis of the observations presented above, an effect on cell wall biosynthesis was suggested as the primary mode of action for mannopeptimycin delta. The mannopeptimycins were inactive against Candida albicans, did not initiate hemolysis of human erythrocytes, and did not promote potassium ion leakage from E. coli imp, suggesting a lack of membrane damage to prokaryotic or eukaryotic cells

  glycopeptides, antibiotics, mannopeptimycins, Streptomyces hygroscopicus LL-AC98

  NCBI PubMed ID: 12499170
  Publication DOI: 10.1128/aac.47.1.62-69.2003
  Journal NLM ID: 0315061
  Correspondence: singhm@wyeth.com
  Institutions: Natural Products Microbiology, Wyeth Research, Pearl River, NY, USA, Antibacterial Research, Infectious Disease Section, Wyeth Research, Pearl River, NY, USA
  Methods: biological assays, cell growth, antibacterial assay
  
   
  
  Streptomyces hygroscopicus LL-AC98
  CSDB ID 47741 (all data & tools)

Show legend Show as text

Structure type: cyclic polymer repeating unit ; 1388.7577 [M+H]+
C₆₆H₁₀₅N₁₁O₂₁
Trivial name: desmamides A
Compound class: lipoglycopeptide
Contained glycoepitopes: IEDB_114701,IEDB_150900

• Article ID: 6224
  Freitas S, Castelo-Branco R, Wenzel-Storjohann A, Vasconcelos VM, Tasdemir D, Leão PN "Structure and Biosynthesis of Desmamides A-C, Lipoglycopeptides from the Endophytic Cyanobacterium Desmonostoc muscorum LEGE 12446" - Journal of Natural Products 85(7) (2022) 1704-1714
  

  Certain cyanobacteria of the secondary metabolite-rich order Nostocales can establish permanent symbioses with a large number of cycads, by accumulating in their coralloid roots and shifting their metabolism to dinitrogen fixation. Here, we report the discovery of two new lipoglycopeptides, desmamides A (1) and B (2), together with their aglycone desmamide C (3), from the nostocalean cyanobacterium Desmonostoc muscorum LEGE 12446 isolated from a cycad (Cycas revoluta) coralloid root. The chemical structures of the compounds were elucidated using a combination of 1D and 2D NMR spectroscopy and mass spectrometry. The desmamides are decapeptides featuring O-glycosylation of tyrosine (in 1 and 2) and an unusual 3,5-dihydroxy-2-methyldecanoic acid residue. The biosynthesis of the desmamides was studied by substrate incubation experiments and bioinformatics. We describe herein the dsm biosynthetic gene cluster and propose it to be associated with desmamide production. The discovery of this class of very abundant (>1.5% d.w.) bacterial lipoglycopeptides paves the way for exploration of their potential role in root endosymbiosis.

  structure, NMR spectroscopy, mass spectrometry, cyanobacteria, marine, lipoglycopeptides, Desmonostoc muscorum

  NCBI PubMed ID: 35793792
  Publication DOI: 10.1021/acs.jnatprod.2c00162
  Journal NLM ID: 7906882
  Publisher: American Society of Pharmacognosy
  Correspondence: P.N. Leão
  Institutions: Interdisciplinary Centre of Marine and Environmental Research (CIIMAR/CIMAR), University of Porto, Avenida General Norton de Matos, s/n, 4450-208 Matosinhos, Portugal, Department of Biology, Faculty of Sciences, University of Porto Rua do Campo Alegre, Porto, Portugal, GEOMAR Centre for Marine Biotechnology (GEOMAR-Biotech), Research Unit Marine Natural Product Chemistry, GEOMAR Helmholtz Centre for Ocean Research Kiel, Am Kiel Kanal 44, 24106 Kiel, Germany, Kiel University, Christian-Albrechts-Platz 4, 24118 Kiel, Germany
  Methods: 13C NMR, 1H NMR, NMR-2D, FTIR, HPLC, extraction, optical rotation measurement, bioinformatic analysis, HR-ESI-MS, antibacterial assay, cell viability assay, flash chromatography, genome sequencing, Marfey’s method, LC-HR-ESI-MS
  
   
  
  Desmonostoc muscorum LEGE 12446
  CSDB ID 8455 (all data & tools)

Show legend Show as text

Structure type: cyclic polymer repeating unit ; 1430.7666 [M+H]+
C₆₈H₁₀₈N₁₁O₂₂
Trivial name: desmamides B
Compound class: lipoglycopeptide
Contained glycoepitopes: IEDB_114701,IEDB_150900

• Article ID: 6224
  Freitas S, Castelo-Branco R, Wenzel-Storjohann A, Vasconcelos VM, Tasdemir D, Leão PN "Structure and Biosynthesis of Desmamides A-C, Lipoglycopeptides from the Endophytic Cyanobacterium Desmonostoc muscorum LEGE 12446" - Journal of Natural Products 85(7) (2022) 1704-1714
  

  Certain cyanobacteria of the secondary metabolite-rich order Nostocales can establish permanent symbioses with a large number of cycads, by accumulating in their coralloid roots and shifting their metabolism to dinitrogen fixation. Here, we report the discovery of two new lipoglycopeptides, desmamides A (1) and B (2), together with their aglycone desmamide C (3), from the nostocalean cyanobacterium Desmonostoc muscorum LEGE 12446 isolated from a cycad (Cycas revoluta) coralloid root. The chemical structures of the compounds were elucidated using a combination of 1D and 2D NMR spectroscopy and mass spectrometry. The desmamides are decapeptides featuring O-glycosylation of tyrosine (in 1 and 2) and an unusual 3,5-dihydroxy-2-methyldecanoic acid residue. The biosynthesis of the desmamides was studied by substrate incubation experiments and bioinformatics. We describe herein the dsm biosynthetic gene cluster and propose it to be associated with desmamide production. The discovery of this class of very abundant (>1.5% d.w.) bacterial lipoglycopeptides paves the way for exploration of their potential role in root endosymbiosis.

  structure, NMR spectroscopy, mass spectrometry, cyanobacteria, marine, lipoglycopeptides, Desmonostoc muscorum

  NCBI PubMed ID: 35793792
  Publication DOI: 10.1021/acs.jnatprod.2c00162
  Journal NLM ID: 7906882
  Publisher: American Society of Pharmacognosy
  Correspondence: P.N. Leão
  Institutions: Interdisciplinary Centre of Marine and Environmental Research (CIIMAR/CIMAR), University of Porto, Avenida General Norton de Matos, s/n, 4450-208 Matosinhos, Portugal, Department of Biology, Faculty of Sciences, University of Porto Rua do Campo Alegre, Porto, Portugal, GEOMAR Centre for Marine Biotechnology (GEOMAR-Biotech), Research Unit Marine Natural Product Chemistry, GEOMAR Helmholtz Centre for Ocean Research Kiel, Am Kiel Kanal 44, 24106 Kiel, Germany, Kiel University, Christian-Albrechts-Platz 4, 24118 Kiel, Germany
  Methods: 13C NMR, 1H NMR, NMR-2D, FTIR, HPLC, extraction, optical rotation measurement, bioinformatic analysis, HR-ESI-MS, antibacterial assay, cell viability assay, flash chromatography, genome sequencing, Marfey’s method, LC-HR-ESI-MS
  
   
  
  Desmonostoc muscorum LEGE 12446
  CSDB ID 20935 (all data & tools)