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Characterisation of tropomyosin and paramyosin as vaccine candidate molecules for the poultry red mite, Dermanyssus gallinae
Dermanyssus gallinae is the most economically important haematophagous ectoparasite in commercial egg laying flocks worldwide. It infests the hens during the night where it causes irritation leading to restlessness, pecking and in extreme cases anaemia and increased cannibalism. Due to an increase i...
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Published in: | Parasites & vectors 2016-10, Vol.9 (1), p.544-544, Article 544 |
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description | Dermanyssus gallinae is the most economically important haematophagous ectoparasite in commercial egg laying flocks worldwide. It infests the hens during the night where it causes irritation leading to restlessness, pecking and in extreme cases anaemia and increased cannibalism. Due to an increase in the occurrence of acaricide-resistant D. gallinae populations, new control strategies are required and vaccination may offer a sustainable alternative to acaricides. In this study, recombinant forms of D. gallinae tropomyosin (Der g 10) and paramyosin (Der g 11) were produced, characterised and tested as vaccine candidate molecules.
The D. gallinae paramyosin (Der g 11) coding sequence was characterised and recombinant versions of Der g 11 and D. gallinae tropomyosin (Der g 10) were produced. Hens were immunised with the recombinant proteins and the resulting antibodies were fed to D. gallinae and mite mortality evaluated. Sections of mites were probed with anti- Der g 11 and Der g 10 antibodies to identify the tissue distribution of these protein in D. gallinae.
The entire coding sequence of Der g 11 was 2,622 bp encoding 874 amino acid residues. Immunohistochemical staining of mite sections revealed that Der g 10 and Der g 11 were located throughout D. gallinae tissues. In phylogenetic analyses of these proteins both clustered with orthologues from tick species rather than with orthologues from astigmatid mites. Antibodies raised in hens against recombinant forms of these proteins significantly increased D. gallinae mortality, by 19 % for Der g 10 (P |
doi_str_mv | 10.1186/s13071-016-1831-8 |
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The D. gallinae paramyosin (Der g 11) coding sequence was characterised and recombinant versions of Der g 11 and D. gallinae tropomyosin (Der g 10) were produced. Hens were immunised with the recombinant proteins and the resulting antibodies were fed to D. gallinae and mite mortality evaluated. Sections of mites were probed with anti- Der g 11 and Der g 10 antibodies to identify the tissue distribution of these protein in D. gallinae.
The entire coding sequence of Der g 11 was 2,622 bp encoding 874 amino acid residues. Immunohistochemical staining of mite sections revealed that Der g 10 and Der g 11 were located throughout D. gallinae tissues. In phylogenetic analyses of these proteins both clustered with orthologues from tick species rather than with orthologues from astigmatid mites. Antibodies raised in hens against recombinant forms of these proteins significantly increased D. gallinae mortality, by 19 % for Der g 10 (P < 0.001) and by 23 % for Der g 11 (P = 0.009) when fed to the mites using an in vitro feeding device.
This study has shown that Der g 10 and Der g 11 were located ubiquitously throughout D. gallinae and that antibodies raised against recombinant versions of these proteins can be used to significantly increase D. gallinae mortality in an in vitro feeding assay. When comparing archived data for all recombinant and native proteins assessed as vaccines using this in vitro feeding assay, Der g 10 and Der g 11 ranked highly and performed better than some of the pools of native proteins.</description><identifier>ISSN: 1756-3305</identifier><identifier>EISSN: 1756-3305</identifier><identifier>DOI: 10.1186/s13071-016-1831-8</identifier><identifier>PMID: 27733192</identifier><language>eng</language><publisher>England: BioMed Central Ltd</publisher><subject>Animals ; Antibodies - immunology ; Chickens - immunology ; Chickens - parasitology ; Composition ; Female ; Genetic aspects ; Mite Infestations - prevention & control ; Mite Infestations - veterinary ; Myosin ; Poultry Diseases - immunology ; Poultry Diseases - prevention & control ; Recombinant molecules ; Recombinant Proteins - administration & dosage ; Recombinant Proteins - immunology ; Testing ; Tropomyosin - genetics ; Tropomyosin - immunology ; Tropomyosin - isolation & purification ; Vaccines ; Vaccines - administration & dosage ; Vaccines - chemistry ; Vaccines - immunology</subject><ispartof>Parasites & vectors, 2016-10, Vol.9 (1), p.544-544, Article 544</ispartof><rights>COPYRIGHT 2016 BioMed Central Ltd.</rights><rights>Copyright BioMed Central 2016</rights><rights>The Author(s). 2016</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c528t-384f68d5bd1a9db1edf1155794168482676be7a3fac1b0e8df485421c29cfef93</citedby><cites>FETCH-LOGICAL-c528t-384f68d5bd1a9db1edf1155794168482676be7a3fac1b0e8df485421c29cfef93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5059928/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1837611557?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27733192$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wright, Harry W</creatorcontrib><creatorcontrib>Bartley, Kathryn</creatorcontrib><creatorcontrib>Huntley, John F</creatorcontrib><creatorcontrib>Nisbet, Alasdair J</creatorcontrib><title>Characterisation of tropomyosin and paramyosin as vaccine candidate molecules for the poultry red mite, Dermanyssus gallinae</title><title>Parasites & vectors</title><addtitle>Parasit Vectors</addtitle><description>Dermanyssus gallinae is the most economically important haematophagous ectoparasite in commercial egg laying flocks worldwide. It infests the hens during the night where it causes irritation leading to restlessness, pecking and in extreme cases anaemia and increased cannibalism. Due to an increase in the occurrence of acaricide-resistant D. gallinae populations, new control strategies are required and vaccination may offer a sustainable alternative to acaricides. In this study, recombinant forms of D. gallinae tropomyosin (Der g 10) and paramyosin (Der g 11) were produced, characterised and tested as vaccine candidate molecules.
The D. gallinae paramyosin (Der g 11) coding sequence was characterised and recombinant versions of Der g 11 and D. gallinae tropomyosin (Der g 10) were produced. Hens were immunised with the recombinant proteins and the resulting antibodies were fed to D. gallinae and mite mortality evaluated. Sections of mites were probed with anti- Der g 11 and Der g 10 antibodies to identify the tissue distribution of these protein in D. gallinae.
The entire coding sequence of Der g 11 was 2,622 bp encoding 874 amino acid residues. Immunohistochemical staining of mite sections revealed that Der g 10 and Der g 11 were located throughout D. gallinae tissues. In phylogenetic analyses of these proteins both clustered with orthologues from tick species rather than with orthologues from astigmatid mites. Antibodies raised in hens against recombinant forms of these proteins significantly increased D. gallinae mortality, by 19 % for Der g 10 (P < 0.001) and by 23 % for Der g 11 (P = 0.009) when fed to the mites using an in vitro feeding device.
This study has shown that Der g 10 and Der g 11 were located ubiquitously throughout D. gallinae and that antibodies raised against recombinant versions of these proteins can be used to significantly increase D. gallinae mortality in an in vitro feeding assay. When comparing archived data for all recombinant and native proteins assessed as vaccines using this in vitro feeding assay, Der g 10 and Der g 11 ranked highly and performed better than some of the pools of native proteins.</description><subject>Animals</subject><subject>Antibodies - immunology</subject><subject>Chickens - immunology</subject><subject>Chickens - parasitology</subject><subject>Composition</subject><subject>Female</subject><subject>Genetic aspects</subject><subject>Mite Infestations - prevention & control</subject><subject>Mite Infestations - veterinary</subject><subject>Myosin</subject><subject>Poultry Diseases - immunology</subject><subject>Poultry Diseases - prevention & control</subject><subject>Recombinant molecules</subject><subject>Recombinant Proteins - administration & dosage</subject><subject>Recombinant Proteins - immunology</subject><subject>Testing</subject><subject>Tropomyosin - genetics</subject><subject>Tropomyosin - immunology</subject><subject>Tropomyosin - isolation & purification</subject><subject>Vaccines</subject><subject>Vaccines - administration & dosage</subject><subject>Vaccines - chemistry</subject><subject>Vaccines - immunology</subject><issn>1756-3305</issn><issn>1756-3305</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><recordid>eNptkltrFDEYhgdRbK3-AG8k4I2CU3OYZDI3hbKeCgXBw3XIZL7spswka5IpLvjjzbht7YrkIqfne_Pl5a2q5wSfEiLF20QYbkmNiaiJZKSWD6pj0nJRM4b5w3vro-pJSlcYC9xx8bg6om3LGOnocfVrtdFRmwzRJZ1d8ChYlGPYhmkXkvNI-wFtC3K7TehaG-M8IFOu3KAzoCmMYOYRErIhorwBtA3zmOMORRjQ5DK8Qe8gTtrvUpoTWutxdF7D0-qR1WOCZzfzSfX9w_tvq0_15eePF6vzy9pwKnPNZGOFHHg_EN0NPYHBEsJ52zVEyEZS0YoeWs2sNqTHIAfbSN5QYmhnLNiOnVRne93t3E8wGPA56lFto5t03KmgnTq88W6j1uFaccy7jsoi8OpGIIYfM6SsJpcMjKP2EOakivu8IZR1uKAv_0Gvwhx9-d5CteJP53-pYgUo520o75pFVJ03QjQNpXzROv0PVcYAkzPBg3Xl_KDg9UFBYTL8zGs9p6Quvn45ZMmeNTGkFMHe-UGwWuKl9vFSJV5L60QtPry4b-RdxW2e2G_ZMsvM</recordid><startdate>20161012</startdate><enddate>20161012</enddate><creator>Wright, Harry W</creator><creator>Bartley, Kathryn</creator><creator>Huntley, John F</creator><creator>Nisbet, Alasdair J</creator><general>BioMed Central Ltd</general><general>BioMed Central</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ISR</scope><scope>3V.</scope><scope>7SN</scope><scope>7SS</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F1W</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>H95</scope><scope>K9.</scope><scope>L.G</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20161012</creationdate><title>Characterisation of tropomyosin and paramyosin as vaccine candidate molecules for the poultry red mite, Dermanyssus gallinae</title><author>Wright, Harry W ; 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It infests the hens during the night where it causes irritation leading to restlessness, pecking and in extreme cases anaemia and increased cannibalism. Due to an increase in the occurrence of acaricide-resistant D. gallinae populations, new control strategies are required and vaccination may offer a sustainable alternative to acaricides. In this study, recombinant forms of D. gallinae tropomyosin (Der g 10) and paramyosin (Der g 11) were produced, characterised and tested as vaccine candidate molecules.
The D. gallinae paramyosin (Der g 11) coding sequence was characterised and recombinant versions of Der g 11 and D. gallinae tropomyosin (Der g 10) were produced. Hens were immunised with the recombinant proteins and the resulting antibodies were fed to D. gallinae and mite mortality evaluated. Sections of mites were probed with anti- Der g 11 and Der g 10 antibodies to identify the tissue distribution of these protein in D. gallinae.
The entire coding sequence of Der g 11 was 2,622 bp encoding 874 amino acid residues. Immunohistochemical staining of mite sections revealed that Der g 10 and Der g 11 were located throughout D. gallinae tissues. In phylogenetic analyses of these proteins both clustered with orthologues from tick species rather than with orthologues from astigmatid mites. Antibodies raised in hens against recombinant forms of these proteins significantly increased D. gallinae mortality, by 19 % for Der g 10 (P < 0.001) and by 23 % for Der g 11 (P = 0.009) when fed to the mites using an in vitro feeding device.
This study has shown that Der g 10 and Der g 11 were located ubiquitously throughout D. gallinae and that antibodies raised against recombinant versions of these proteins can be used to significantly increase D. gallinae mortality in an in vitro feeding assay. When comparing archived data for all recombinant and native proteins assessed as vaccines using this in vitro feeding assay, Der g 10 and Der g 11 ranked highly and performed better than some of the pools of native proteins.</abstract><cop>England</cop><pub>BioMed Central Ltd</pub><pmid>27733192</pmid><doi>10.1186/s13071-016-1831-8</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Antibodies - immunology Chickens - immunology Chickens - parasitology Composition Female Genetic aspects Mite Infestations - prevention & control Mite Infestations - veterinary Myosin Poultry Diseases - immunology Poultry Diseases - prevention & control Recombinant molecules Recombinant Proteins - administration & dosage Recombinant Proteins - immunology Testing Tropomyosin - genetics Tropomyosin - immunology Tropomyosin - isolation & purification Vaccines Vaccines - administration & dosage Vaccines - chemistry Vaccines - immunology |
title | Characterisation of tropomyosin and paramyosin as vaccine candidate molecules for the poultry red mite, Dermanyssus gallinae |
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