No Cover Image

Journal article 1294 views 353 downloads

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

Check full text

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...

Full description

Published in: Developmental & Comparative Immunology
ISSN: 0145305X
Published: 2018
Online Access: Check full text

URI: https://cronfa.swan.ac.uk/Record/cronfa39536
Tags: Add Tag
No Tags, Be the first to tag this record!
first_indexed 2018-04-22T04:39:25Z
last_indexed 2018-06-25T13:34:28Z
id cronfa39536
recordtype SURis
fullrecord <?xml version="1.0"?><rfc1807><datestamp>2018-06-25T11:31:37.1096725</datestamp><bib-version>v2</bib-version><id>39536</id><entry>2018-04-21</entry><title>Hemocyanin-derived phenoloxidase reaction products display anti-infective properties</title><swanseaauthors><author><sid>af160934b75bea5b8ba83d68b3d1a003</sid><firstname>Christopher</firstname><surname>Coates</surname><name>Christopher Coates</name><active>true</active><ethesisStudent>false</ethesisStudent></author></swanseaauthors><date>2018-04-21</date><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 (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.</abstract><type>Journal Article</type><journal>Developmental &amp; Comparative Immunology</journal><volume>86</volume><paginationStart>47</paginationStart><paginationEnd>51</paginationEnd><publisher/><issnPrint>0145305X</issnPrint><keywords/><publishedDay>30</publishedDay><publishedMonth>9</publishedMonth><publishedYear>2018</publishedYear><publishedDate>2018-09-30</publishedDate><doi>10.1016/j.dci.2018.04.017</doi><url/><notes/><college>COLLEGE NANME</college><CollegeCode>COLLEGE CODE</CollegeCode><institution>Swansea University</institution><apcterm/><lastEdited>2018-06-25T11:31:37.1096725</lastEdited><Created>2018-04-21T19:57:19.5574526</Created><path><level id="1">Faculty of Science and Engineering</level><level id="2">School of Biosciences, Geography and Physics - Biosciences</level></path><authors><author><firstname>Christopher</firstname><surname>Coates</surname><order>1</order></author><author><firstname>James</firstname><surname>Talbot</surname><order>2</order></author></authors><documents><document><filename>0039536-01052018141027.pdf</filename><originalFilename>39536.pdf</originalFilename><uploaded>2018-05-01T14:10:27.6700000</uploaded><type>Output</type><contentLength>1330622</contentLength><contentType>application/pdf</contentType><version>Accepted Manuscript</version><cronfaStatus>true</cronfaStatus><embargoDate>2019-04-25T00:00:00.0000000</embargoDate><documentNotes>12 month embargo.</documentNotes><copyrightCorrect>true</copyrightCorrect><language>eng</language></document></documents><OutputDurs/></rfc1807>
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
_version_ 1763752451601596416
score 11.013148

Similar Items