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...

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Published in:Fish & Shellfish Immunology
Main Authors: Luna-Acosta, Andrea, Saulnier, Denis, Pommier, Mylene, Haffner, Philippe, de Decker, Sophie, Renault, Tristan, Thomas-Guyon, Helene
Other Authors: 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
Language:English
Published: HAL CCSD 2011
Subjects:
Online Access:https://hal.science/hal-04499032
https://doi.org/10.1016/j.fsi.2011.07.016
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spelling 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
institution Open Polar
collection Université de la Polynésie française (upf): HAL
op_collection_id 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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