Inducible ASABF-Type Antimicrobial Peptide from the Sponge Suberites domuncula: Microbicidal and Hemolytic Activity in Vitro and Toxic Effect on Molluscs in Vivo
Since sponges, as typical filter-feeders, are exposed to a high load of attacking prokaryotic and eukaryotic organisms, they are armed with a wide arsenal of antimicrobial/cytostatic low-molecular-weight, non-proteinaceous bioactive compounds. Here we present the first sponge agent belonging to the...
| Main Authors: | , , , , , |
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| Format: | Article |
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MDPI AG
2011-10-01
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| Series: | Marine Drugs |
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| Online Access: | http://www.mdpi.com/1660-3397/9/10/1969/ |
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| author | Werner E. G. Müller Renato Batel Heinz C. Schröder Xiao-Hong Wang Michael Korzhev Matthias Wiens |
| author_facet | Werner E. G. Müller Renato Batel Heinz C. Schröder Xiao-Hong Wang Michael Korzhev Matthias Wiens |
| author_sort | Werner E. G. Müller |
| collection | DOAJ |
| description | Since sponges, as typical filter-feeders, are exposed to a high load of attacking prokaryotic and eukaryotic organisms, they are armed with a wide arsenal of antimicrobial/cytostatic low-molecular-weight, non-proteinaceous bioactive compounds. Here we present the first sponge agent belonging to the group of ASABF-type antimicrobial peptides. The ASABF gene was identified and cloned from the demospongeSuberites domuncula. The mature peptide, with a length of 64 aa residues has a predicted pI of 9.24, and comprises the characteristic CSαβ structural motif. Consequently, the S. domuncula ASABF shares high similarity with the nematode ASABFs; it is distantly related to the defensins. The recombinant peptide was found to display besides microbicidal activity, anti-fungal activity. In addition, the peptide lyses human erythrocytes. The expression ofASABF is upregulated after exposure to the apoptosis-inducing agent 2,2'-dipyridyl. During the process of apoptosis of surface tissue of S. domuncula, grazing gastropods (Bittium sp.) are attracted by quinolinic acid which is synthesized through the kynurenine pathway by the enzyme 3-hydroxyanthranilate 3,4-dioxygenase (HAD). Finally, the gastropods are repelled from the sponge tissue by the ASABF. It is shown that the effector peptide ASABF is sequentially expressed after the induction of the HAD gene and a caspase, as a central enzyme executing apoptosis. |
| first_indexed | 2024-04-11T18:03:49Z |
| format | Article |
| id | doaj.art-1d31a378cced4f65afff63ed697ee8da |
| institution | Directory Open Access Journal |
| issn | 1660-3397 |
| language | English |
| last_indexed | 2024-04-11T18:03:49Z |
| publishDate | 2011-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Marine Drugs |
| spelling | doaj.art-1d31a378cced4f65afff63ed697ee8da2022-12-22T04:10:22ZengMDPI AGMarine Drugs1660-33972011-10-019101969199410.3390/md9101969Inducible ASABF-Type Antimicrobial Peptide from the Sponge Suberites domuncula: Microbicidal and Hemolytic Activity in Vitro and Toxic Effect on Molluscs in VivoWerner E. G. MüllerRenato BatelHeinz C. SchröderXiao-Hong WangMichael KorzhevMatthias WiensSince sponges, as typical filter-feeders, are exposed to a high load of attacking prokaryotic and eukaryotic organisms, they are armed with a wide arsenal of antimicrobial/cytostatic low-molecular-weight, non-proteinaceous bioactive compounds. Here we present the first sponge agent belonging to the group of ASABF-type antimicrobial peptides. The ASABF gene was identified and cloned from the demospongeSuberites domuncula. The mature peptide, with a length of 64 aa residues has a predicted pI of 9.24, and comprises the characteristic CSαβ structural motif. Consequently, the S. domuncula ASABF shares high similarity with the nematode ASABFs; it is distantly related to the defensins. The recombinant peptide was found to display besides microbicidal activity, anti-fungal activity. In addition, the peptide lyses human erythrocytes. The expression ofASABF is upregulated after exposure to the apoptosis-inducing agent 2,2'-dipyridyl. During the process of apoptosis of surface tissue of S. domuncula, grazing gastropods (Bittium sp.) are attracted by quinolinic acid which is synthesized through the kynurenine pathway by the enzyme 3-hydroxyanthranilate 3,4-dioxygenase (HAD). Finally, the gastropods are repelled from the sponge tissue by the ASABF. It is shown that the effector peptide ASABF is sequentially expressed after the induction of the HAD gene and a caspase, as a central enzyme executing apoptosis.http://www.mdpi.com/1660-3397/9/10/1969/spongesSuberites domunculaASABFantimicrobial peptidesapoptosisBittium sp. |
| spellingShingle | Werner E. G. Müller Renato Batel Heinz C. Schröder Xiao-Hong Wang Michael Korzhev Matthias Wiens Inducible ASABF-Type Antimicrobial Peptide from the Sponge Suberites domuncula: Microbicidal and Hemolytic Activity in Vitro and Toxic Effect on Molluscs in Vivo Marine Drugs sponges Suberites domuncula ASABF antimicrobial peptides apoptosis Bittium sp. |
| title | Inducible ASABF-Type Antimicrobial Peptide from the Sponge Suberites domuncula: Microbicidal and Hemolytic Activity in Vitro and Toxic Effect on Molluscs in Vivo |
| title_full | Inducible ASABF-Type Antimicrobial Peptide from the Sponge Suberites domuncula: Microbicidal and Hemolytic Activity in Vitro and Toxic Effect on Molluscs in Vivo |
| title_fullStr | Inducible ASABF-Type Antimicrobial Peptide from the Sponge Suberites domuncula: Microbicidal and Hemolytic Activity in Vitro and Toxic Effect on Molluscs in Vivo |
| title_full_unstemmed | Inducible ASABF-Type Antimicrobial Peptide from the Sponge Suberites domuncula: Microbicidal and Hemolytic Activity in Vitro and Toxic Effect on Molluscs in Vivo |
| title_short | Inducible ASABF-Type Antimicrobial Peptide from the Sponge Suberites domuncula: Microbicidal and Hemolytic Activity in Vitro and Toxic Effect on Molluscs in Vivo |
| title_sort | inducible asabf type antimicrobial peptide from the sponge suberites domuncula microbicidal and hemolytic activity in vitro and toxic effect on molluscs in vivo |
| topic | sponges Suberites domuncula ASABF antimicrobial peptides apoptosis Bittium sp. |
| url | http://www.mdpi.com/1660-3397/9/10/1969/ |
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