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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Online Access: | https://hal.science/hal-04499032 https://doi.org/10.1016/j.fsi.2011.07.016 |
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ftunivpolynesief:oai:HAL:hal-04499032v1 2024-05-19T07:39:14+00:00 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 Ecosystèmes Insulaires Océaniens (UMR 241) (EIO) Institut de Recherche pour le Développement (IRD)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Université de la Polynésie Française (UPF)-Institut Louis Malardé Papeete (ILM) Institut de Recherche pour le Développement (IRD) Unité Amélioration génétique, Santé animale et Environnement (AGSAE) Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER) Centre Océanologique du Pacifique (COP) 2011-12 https://hal.science/hal-04499032 https://doi.org/10.1016/j.fsi.2011.07.016 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.fsi.2011.07.016 hal-04499032 https://hal.science/hal-04499032 doi:10.1016/j.fsi.2011.07.016 ISSN: 1050-4648 EISSN: 1095-9947 Fish and Shellfish Immunology https://hal.science/hal-04499032 Fish and Shellfish Immunology, 2011, 31 (6), pp.795-800. ⟨10.1016/j.fsi.2011.07.016⟩ [SDV]Life Sciences [q-bio] info:eu-repo/semantics/article Journal articles 2011 ftunivpolynesief https://doi.org/10.1016/j.fsi.2011.07.016 2024-05-01T00:14:57Z 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 Université de la Polynésie française (upf): HAL Fish & Shellfish Immunology 31 6 795 800 |
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Open Polar |
collection |
Université de la Polynésie française (upf): HAL |
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ftunivpolynesief |
language |
English |
topic |
[SDV]Life Sciences [q-bio] |
spellingShingle |
[SDV]Life Sciences [q-bio] 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 |
[SDV]Life Sciences [q-bio] |
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. |
author2 |
Ecosystèmes Insulaires Océaniens (UMR 241) (EIO) Institut de Recherche pour le Développement (IRD)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Université de la Polynésie Française (UPF)-Institut Louis Malardé Papeete (ILM) Institut de Recherche pour le Développement (IRD) Unité Amélioration génétique, Santé animale et Environnement (AGSAE) Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER) Centre Océanologique du Pacifique (COP) |
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 |
HAL CCSD |
publishDate |
2011 |
url |
https://hal.science/hal-04499032 https://doi.org/10.1016/j.fsi.2011.07.016 |
genre |
Crassostrea gigas Pacific oyster |
genre_facet |
Crassostrea gigas Pacific oyster |
op_source |
ISSN: 1050-4648 EISSN: 1095-9947 Fish and Shellfish Immunology https://hal.science/hal-04499032 Fish and Shellfish Immunology, 2011, 31 (6), pp.795-800. ⟨10.1016/j.fsi.2011.07.016⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.fsi.2011.07.016 hal-04499032 https://hal.science/hal-04499032 doi:10.1016/j.fsi.2011.07.016 |
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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1799478787127115776 |