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Exploring the Antagonistic Producer Streptomyces MSI051: Implications of Polyketide Synthase Gene Type II and a Ubiquitous Defense Enzyme Phospholipase A2 in the Host Sponge Dendrilla nigra

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Abstract

To explore the functional role of the antagonistic producer strain Streptomyces dendra sp. nov. MSI051 in the host sponge Dendrilla nigra, hypothetical factors including the antagonistic potential of MSI051 against biofilm bacteria and a ubiquitous defense enzyme phospholipase A2 (PLA2) in host sponge as well as in bacterial symbiont MSI051 were determined. The host sponge D. nigra and associated bacterial symbiont MSI051 contained high levels of PLA2. The host sponge showed PLA2 activity to the extent of 1032 U/L, with a specific activity of 2021 U/g, and strain MSI051 showed similar activity. The findings of the present study suggest that PLA2 in the sponge-associated bacteria might have an integrated functional role in the host defense system of marine sponges. This report may be the first on the role of PLA2 activity in sponge-associated bacteria. Isolate MSI051 was a potential antagonistic producer which showed a broad spectrum of antibacterial activity. Polyketide synthase gene type II in MSI051 ultimately evidenced the antagonistic potential. Antimicrobial activity was found to be positively skewed toward biofilm bacteria. This implies a functional role of MSI051 in the protection of host sponge against fouling processes.

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References

  1. Ayuso-Sacido A, Genilloud O (2005) New PCR primers for the screening of NRPS and PKS-I systems in actinomycetes: detection and distribution of these biosynthetic gene sequences in major taxonomic groups. Microb Ecol 49:10–24

    Article  PubMed  CAS  Google Scholar 

  2. Chuck JA, Dunn C, Facultad FECD, Nakazono C, Nikodinovic J, Barrow KD (2006) Amplification of DNA encoding entire type I polyketide synthase domains and linkers from Streptomyces species. Curr Microbiol 53:89–94

    Article  PubMed  CAS  Google Scholar 

  3. Davis AR, Targett NM, McConnel OJ, Young CM (1989) Epibiosis of marine algae and benthic invertebrates: natural products chemistry and other mechanisms inhibiting settlement and overgrowth. Bioorg Mar Chem 3:85–114

    CAS  Google Scholar 

  4. Finking R, Marahiel AM (2004) Biosynthesis of nonribosomal peptides. Annu Rev Microbiol 28:453–488

    Article  CAS  Google Scholar 

  5. Flowers AE, Garson MJ, Webb RI, Dumdei EJ, Charan RD (1998) Cellular origin of chlorinated diketopiperazines in the dictyoceratid sponge Dysidea herbacea (Keller). Cell Tissue Res 292:597–607

    Article  PubMed  CAS  Google Scholar 

  6. Gramzow M, Schröder HC, Fritsche U, Kurelec B, Robitzki A, Zimmermann H, Friese K, Kreuter MH, Müller WE (1989) Role of phospholipase A2 in the stimulation of sponge cell proliferation by homologous lectin. Cell 5:939–948

    Article  Google Scholar 

  7. Hadas E, Shpigel M, Ilan M (2005) Sea ranching of the marine sponge Negombata magnifica (Demospongiae, Latrunculiidae) as a first step for latrunculin B mass production. Aquaculture 244:159–169

    Article  CAS  Google Scholar 

  8. Hoffmann GE, Schmidt D, Bastian B, Guder WG (1986) Photometric determination of phospholipase. Am J Clin Chem Clin Biochem 24:871–875

    CAS  Google Scholar 

  9. Laine VJO, Grass DS, Nevalainen TJ (1999) Protection by group II phospholipase 2 against Staphylococcus aureus. J Immunol 162:7402–7408

    PubMed  CAS  Google Scholar 

  10. Lechevalier (1989) The Actinomycetes III, a practical guide to generic identification of Actinomycetes. In: Bergey’s manual of systematic bacteriology, vol 4. Williams & Wilkins, Baltimore, pp 2344–2347

  11. Metsa-Ketela M, Salo V, Halo L, Hautala A, Hakala J, Mantsala P, Ylihonko K (1999) An efficient approach for screening minimal PKS genes from Streptomyces. FEMS Microbiol Lett 180:1–6

    Article  PubMed  CAS  Google Scholar 

  12. Nevalainen TJ, Peuravuori HJ, Quinn RJ, Llewellyn LE, Benzie JAH, Fenner PJ, Winkel KD (2004) Phospholipase A2 in Cnidaria. Comp Biochem Physiol Part B 139:731–735

    Article  CAS  Google Scholar 

  13. Nevalainen TJ, Quinn RJ, Hooper JNA (2004) Phospholipase A2 in porifera. Comp Biochem Physiol Part B 137:413–420

    Article  CAS  Google Scholar 

  14. Selvin J, Lipton AP (2004) Biopotentials of secondary metabolites isolated from marine sponges. Hydrobiologia 513:231–238

    Article  CAS  Google Scholar 

  15. Selvin J, Lipton AP (2004) Dendrilla nigra, a marine sponge, as potential source of antibacterial substances for managing shrimp diseases. Aquaculture 236:277–283

    Article  Google Scholar 

  16. Selvin J, Soniya J, Asha KRT, Manjusha WA, Sangeetha VS, Jayaseema DM, Antony MC, Vinitha DAJ (2004) Antibacterial potential of antagonistic Streptomyces sp. isolated from the marine sponge Dendrilla nigra. FEMS Microbiol Ecol 50:117–122

    Article  CAS  PubMed  Google Scholar 

  17. Stahl U, Lee M, Sjodahl S et al (1999) Plant low-molecular-weight phospholipase A2s (PLA2s) are structurally related to the animal secretory PLA2s and are present as a family of isoformas in rice (Oryza sativa). Plant Mol Biol 41:481–490

    Article  PubMed  CAS  Google Scholar 

  18. Tamura K, Dudley J, Nei M, Kumar S (2007) MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software, version 4.0. Mol Biol Evol 24:1596–1599

    Article  PubMed  CAS  Google Scholar 

  19. Uriz MJ, Turon X, Galera J, Tur JM (1996) New light on the cell location of avarol within the sponge Dysidea avara (Dendroceratida). Cell Tissue Res 285:519–527

    Article  Google Scholar 

  20. Weinrauch Y, Elsbach P, Madsen LM, Foreman A, Weiss J (1996) The potent anti-Staphylococcus aureus activity of a sterile rabbit inflammatory fluid is due to a 14-kD phospholipase A2. J Clin Invest 97:250–257

    Article  PubMed  CAS  Google Scholar 

  21. Bradford M (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254

    Article  PubMed  CAS  Google Scholar 

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Acknowledgments

J.S. is thankful to the DST-Young Scientist Scheme (SR/FT/L-19/2004), Delhi, India, and the International Foundation for Science (RGA No. F/3776-1), Sweden, for financial support.

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  1. Marine Bioprospecting Laboratory, Department of Microbiology, Bharathidasan University, Tiruchirappalli, 620 024, India

    Joseph Selvin

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  1. Joseph Selvin
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Correspondence to Joseph Selvin.

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Selvin, J. Exploring the Antagonistic Producer Streptomyces MSI051: Implications of Polyketide Synthase Gene Type II and a Ubiquitous Defense Enzyme Phospholipase A2 in the Host Sponge Dendrilla nigra . Curr Microbiol 58, 459–463 (2009). https://doi.org/10.1007/s00284-008-9343-1

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  • DOI: https://doi.org/10.1007/s00284-008-9343-1

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