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Hemocyanin-derived phenoloxidase reaction products display anti-infective properties

Christopher Coates, James Talbot

Developmental & Comparative Immunology, Volume: 86, Pages: 47 - 51

Swansea University Author: Christopher Coates

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DOI (Published version): 10.1016/j.dci.2018.04.017

Abstract

Hemocyanin is a multi-functional protein located in the hemolymph (blood) of certain arthropods and molluscs. In addition to its well-defined role in oxygen transport, hemocyanin can be converted into a phenoloxidase-like enzyme. Herein, we tested the antimicrobial properties of horseshoe crab (Limu...

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Published in: Developmental & Comparative Immunology
ISSN: 0145305X
Published: 2018
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URI: https://cronfa.swan.ac.uk/Record/cronfa39536
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first_indexed 2018-04-22T04:39:25Z
last_indexed 2018-06-25T13:34:28Z
id cronfa39536
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spelling 2018-06-25T11:31:37.1096725 v2 39536 2018-04-21 Hemocyanin-derived phenoloxidase reaction products display anti-infective properties af160934b75bea5b8ba83d68b3d1a003 Christopher Coates Christopher Coates true false 2018-04-21 Hemocyanin is a multi-functional protein located in the hemolymph (blood) of certain arthropods and molluscs. In addition to its well-defined role in oxygen transport, hemocyanin can be converted into a phenoloxidase-like enzyme. Herein, we tested the antimicrobial properties of horseshoe crab (Limulus polyphemus) hemocyanin-derived phenoloxidase reaction products using broad ranges of phenolic substrates (e.g. L-DOPA) and microbial targets (Gram-positive/negative bacteria, yeast). The enzyme-catalysed turnover of several substrates generated (by)products that reduced significantly the number of colony forming units. Microbicidal effects of hemocyanin-derived phenoloxidase were thwarted by the inhibitor phenylthiourea. Data presentedhere further support a role for hemocyanin in invertebrate innate immunity. Journal Article Developmental & Comparative Immunology 86 47 51 0145305X 30 9 2018 2018-09-30 10.1016/j.dci.2018.04.017 COLLEGE NANME COLLEGE CODE Swansea University 2018-06-25T11:31:37.1096725 2018-04-21T19:57:19.5574526 Faculty of Science and Engineering School of Biosciences, Geography and Physics - Biosciences Christopher Coates 1 James Talbot 2 0039536-01052018141027.pdf 39536.pdf 2018-05-01T14:10:27.6700000 Output 1330622 application/pdf Accepted Manuscript true 2019-04-25T00:00:00.0000000 12 month embargo. true eng
title Hemocyanin-derived phenoloxidase reaction products display anti-infective properties
spellingShingle Hemocyanin-derived phenoloxidase reaction products display anti-infective properties
Christopher Coates
title_short Hemocyanin-derived phenoloxidase reaction products display anti-infective properties
title_full Hemocyanin-derived phenoloxidase reaction products display anti-infective properties
title_fullStr Hemocyanin-derived phenoloxidase reaction products display anti-infective properties
title_full_unstemmed Hemocyanin-derived phenoloxidase reaction products display anti-infective properties
title_sort Hemocyanin-derived phenoloxidase reaction products display anti-infective properties
author_id_str_mv af160934b75bea5b8ba83d68b3d1a003
author_id_fullname_str_mv af160934b75bea5b8ba83d68b3d1a003_***_Christopher Coates
author Christopher Coates
author2 Christopher Coates
James Talbot
format Journal article
container_title Developmental & Comparative Immunology
container_volume 86
container_start_page 47
publishDate 2018
institution Swansea University
issn 0145305X
doi_str_mv 10.1016/j.dci.2018.04.017
college_str Faculty of Science and Engineering
hierarchytype
hierarchy_top_id facultyofscienceandengineering
hierarchy_top_title Faculty of Science and Engineering
hierarchy_parent_id facultyofscienceandengineering
hierarchy_parent_title Faculty of Science and Engineering
department_str School of Biosciences, Geography and Physics - Biosciences{{{_:::_}}}Faculty of Science and Engineering{{{_:::_}}}School of Biosciences, Geography and Physics - Biosciences
document_store_str 1
active_str 0
description Hemocyanin is a multi-functional protein located in the hemolymph (blood) of certain arthropods and molluscs. In addition to its well-defined role in oxygen transport, hemocyanin can be converted into a phenoloxidase-like enzyme. Herein, we tested the antimicrobial properties of horseshoe crab (Limulus polyphemus) hemocyanin-derived phenoloxidase reaction products using broad ranges of phenolic substrates (e.g. L-DOPA) and microbial targets (Gram-positive/negative bacteria, yeast). The enzyme-catalysed turnover of several substrates generated (by)products that reduced significantly the number of colony forming units. Microbicidal effects of hemocyanin-derived phenoloxidase were thwarted by the inhibitor phenylthiourea. Data presentedhere further support a role for hemocyanin in invertebrate innate immunity.
published_date 2018-09-30T03:50:13Z
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