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...

Full description

Bibliographic Details
Published in:Fish & Shellfish Immunology
Main Authors: Luna-acosta, Andrea, Saulnier, Denis, Pommier, Mylene, Haffner, Philippe, De Decker, Sophie, Renault, Tristan, Thomas-guyon, Helene
Format: Article in Journal/Newspaper
Language:English
Published: Academic Press Ltd- Elsevier Science Ltd 2011
Subjects:
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/
id ftarchimer:oai:archimer.ifremer.fr:15598
record_format openpolar
spelling 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
_version_ 1766393534936514560