First evidence of a potential antibacterial activity involving a laccase-type enzyme of the phenoloxidase system in Pacific oyster Crassostrea gigas haemocytes
Phenoloxidases (POs) are a group of copper proteins including tyrosinase, catecholase and laccase. In several insects and crustaceans, antibacterial substances are produced through the PO cascade, participating in the direct killing of invading microorganisms. However, although POs are widely recogn...
Published in: | Fish & Shellfish Immunology |
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Language: | English |
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Academic Press Ltd- Elsevier Science Ltd
2011
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Online Access: | https://archimer.ifremer.fr/doc/00045/15598/13001.pdf https://doi.org/10.1016/j.fsi.2011.07.016 https://archimer.ifremer.fr/doc/00045/15598/ |
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ftarchimer:oai:archimer.ifremer.fr:15598 2023-05-15T15:57:50+02:00 First evidence of a potential antibacterial activity involving a laccase-type enzyme of the phenoloxidase system in Pacific oyster Crassostrea gigas haemocytes Luna-acosta, Andrea Saulnier, Denis Pommier, Mylene Haffner, Philippe De Decker, Sophie Renault, Tristan Thomas-guyon, Helene 2011-12 application/pdf https://archimer.ifremer.fr/doc/00045/15598/13001.pdf https://doi.org/10.1016/j.fsi.2011.07.016 https://archimer.ifremer.fr/doc/00045/15598/ eng eng Academic Press Ltd- Elsevier Science Ltd https://archimer.ifremer.fr/doc/00045/15598/13001.pdf doi:10.1016/j.fsi.2011.07.016 https://archimer.ifremer.fr/doc/00045/15598/ 2011 Elsevier Ltd. All rights reserved. info:eu-repo/semantics/openAccess restricted use Fish & Shellfish Immunology (1050-4648) (Academic Press Ltd- Elsevier Science Ltd), 2011-12 , Vol. 31 , N. 6 , P. 795-800 Phenoloxidases Antibacterial activity Vibrio Bivalve Immunity text Publication info:eu-repo/semantics/article 2011 ftarchimer https://doi.org/10.1016/j.fsi.2011.07.016 2021-09-23T20:19:48Z Phenoloxidases (POs) are a group of copper proteins including tyrosinase, catecholase and laccase. In several insects and crustaceans, antibacterial substances are produced through the PO cascade, participating in the direct killing of invading microorganisms. However, although POs are widely recognised as an integral part of the invertebrate immune defence system, experimental evidence is lacking that these properties are conserved in molluscs, and more particularly in the Pacific oyster Crassostrea gigas. In the present study, Vibrio splendidus LGP32 and Vibrio aestuarianus 02/041 growths were affected, after being treated with C. gigas haemocyte lysate supernatant (HLS), and either a common substrate of POs, l-3,4-dihydroxyphenylalanine (l-DOPA), to detect catecholase-type PO activity, or a specific substrate of laccase, p-phenylenediamine (PPD), to detect laccase-type PO activity. Interestingly, a higher bacterial growth inhibition was observed in the presence of PPD than in the presence of l-DOPA. These effects were suppressed when the specific PO inhibitor, phenylthiourea (PTU), was added to the medium. Results of the present study suggest, for the first time in a mollusc species, that antibacterial activities of HLS from C. gigas potentially involve POs, and more particularly laccase catalysed reactions. Highlights ► Bacterial growth inhibition was studied in two Vibrio oyster bacterial pathogens. ► Different Crassostrea gigas tissues, haemolymph fractions, and PO substrates, were tested. ► The inhibition occurred only in the presence of C. gigas HLS and PO substrates. ► Bacterial growth inhibition was suppressed with a PO inhibitor. ► Results suggest that HLS antibacterial activities involve laccase-type PO-catalysed reactions. Article in Journal/Newspaper Crassostrea gigas Pacific oyster Archimer (Archive Institutionnelle de l'Ifremer - Institut français de recherche pour l'exploitation de la mer) Pacific Fish & Shellfish Immunology 31 6 795 800 |
institution |
Open Polar |
collection |
Archimer (Archive Institutionnelle de l'Ifremer - Institut français de recherche pour l'exploitation de la mer) |
op_collection_id |
ftarchimer |
language |
English |
topic |
Phenoloxidases Antibacterial activity Vibrio Bivalve Immunity |
spellingShingle |
Phenoloxidases Antibacterial activity Vibrio Bivalve Immunity Luna-acosta, Andrea Saulnier, Denis Pommier, Mylene Haffner, Philippe De Decker, Sophie Renault, Tristan Thomas-guyon, Helene First evidence of a potential antibacterial activity involving a laccase-type enzyme of the phenoloxidase system in Pacific oyster Crassostrea gigas haemocytes |
topic_facet |
Phenoloxidases Antibacterial activity Vibrio Bivalve Immunity |
description |
Phenoloxidases (POs) are a group of copper proteins including tyrosinase, catecholase and laccase. In several insects and crustaceans, antibacterial substances are produced through the PO cascade, participating in the direct killing of invading microorganisms. However, although POs are widely recognised as an integral part of the invertebrate immune defence system, experimental evidence is lacking that these properties are conserved in molluscs, and more particularly in the Pacific oyster Crassostrea gigas. In the present study, Vibrio splendidus LGP32 and Vibrio aestuarianus 02/041 growths were affected, after being treated with C. gigas haemocyte lysate supernatant (HLS), and either a common substrate of POs, l-3,4-dihydroxyphenylalanine (l-DOPA), to detect catecholase-type PO activity, or a specific substrate of laccase, p-phenylenediamine (PPD), to detect laccase-type PO activity. Interestingly, a higher bacterial growth inhibition was observed in the presence of PPD than in the presence of l-DOPA. These effects were suppressed when the specific PO inhibitor, phenylthiourea (PTU), was added to the medium. Results of the present study suggest, for the first time in a mollusc species, that antibacterial activities of HLS from C. gigas potentially involve POs, and more particularly laccase catalysed reactions. Highlights ► Bacterial growth inhibition was studied in two Vibrio oyster bacterial pathogens. ► Different Crassostrea gigas tissues, haemolymph fractions, and PO substrates, were tested. ► The inhibition occurred only in the presence of C. gigas HLS and PO substrates. ► Bacterial growth inhibition was suppressed with a PO inhibitor. ► Results suggest that HLS antibacterial activities involve laccase-type PO-catalysed reactions. |
format |
Article in Journal/Newspaper |
author |
Luna-acosta, Andrea Saulnier, Denis Pommier, Mylene Haffner, Philippe De Decker, Sophie Renault, Tristan Thomas-guyon, Helene |
author_facet |
Luna-acosta, Andrea Saulnier, Denis Pommier, Mylene Haffner, Philippe De Decker, Sophie Renault, Tristan Thomas-guyon, Helene |
author_sort |
Luna-acosta, Andrea |
title |
First evidence of a potential antibacterial activity involving a laccase-type enzyme of the phenoloxidase system in Pacific oyster Crassostrea gigas haemocytes |
title_short |
First evidence of a potential antibacterial activity involving a laccase-type enzyme of the phenoloxidase system in Pacific oyster Crassostrea gigas haemocytes |
title_full |
First evidence of a potential antibacterial activity involving a laccase-type enzyme of the phenoloxidase system in Pacific oyster Crassostrea gigas haemocytes |
title_fullStr |
First evidence of a potential antibacterial activity involving a laccase-type enzyme of the phenoloxidase system in Pacific oyster Crassostrea gigas haemocytes |
title_full_unstemmed |
First evidence of a potential antibacterial activity involving a laccase-type enzyme of the phenoloxidase system in Pacific oyster Crassostrea gigas haemocytes |
title_sort |
first evidence of a potential antibacterial activity involving a laccase-type enzyme of the phenoloxidase system in pacific oyster crassostrea gigas haemocytes |
publisher |
Academic Press Ltd- Elsevier Science Ltd |
publishDate |
2011 |
url |
https://archimer.ifremer.fr/doc/00045/15598/13001.pdf https://doi.org/10.1016/j.fsi.2011.07.016 https://archimer.ifremer.fr/doc/00045/15598/ |
geographic |
Pacific |
geographic_facet |
Pacific |
genre |
Crassostrea gigas Pacific oyster |
genre_facet |
Crassostrea gigas Pacific oyster |
op_source |
Fish & Shellfish Immunology (1050-4648) (Academic Press Ltd- Elsevier Science Ltd), 2011-12 , Vol. 31 , N. 6 , P. 795-800 |
op_relation |
https://archimer.ifremer.fr/doc/00045/15598/13001.pdf doi:10.1016/j.fsi.2011.07.016 https://archimer.ifremer.fr/doc/00045/15598/ |
op_rights |
2011 Elsevier Ltd. All rights reserved. info:eu-repo/semantics/openAccess restricted use |
op_doi |
https://doi.org/10.1016/j.fsi.2011.07.016 |
container_title |
Fish & Shellfish Immunology |
container_volume |
31 |
container_issue |
6 |
container_start_page |
795 |
op_container_end_page |
800 |
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1766393534936514560 |