Proteomic analysis of cattle tick Rhipicephalus (Boophilus) microplus saliva: a comparison between partially and fully engorged females
The cattle tick Rhipicephalus (Boophilus) microplus is one of the most harmful parasites affecting bovines. Similarly to other hematophagous ectoparasites, R. microplus saliva contains a collection of bioactive compounds that inhibit host defenses against tick feeding activity. Thus, the study of ti...
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creator | Tirloni, Lucas Reck, José Terra, Renata Maria Soares Martins, João Ricardo Mulenga, Albert Sherman, Nicholas E Fox, Jay W Yates, 3rd, John R Termignoni, Carlos Pinto, Antônio F M Vaz, Jr, Itabajara da Silva |
description | The cattle tick Rhipicephalus (Boophilus) microplus is one of the most harmful parasites affecting bovines. Similarly to other hematophagous ectoparasites, R. microplus saliva contains a collection of bioactive compounds that inhibit host defenses against tick feeding activity. Thus, the study of tick salivary components offers opportunities for the development of immunological based tick control methods and medicinal applications. So far, only a few proteins have been identified in cattle tick saliva. The aim of this work was to identify proteins present in R. microplus female tick saliva at different feeding stages. Proteomic analysis of R. microplus saliva allowed identifying peptides corresponding to 187 and 68 tick and bovine proteins, respectively. Our data confirm that (i) R. microplus saliva is complex, and (ii) that there are remarkable differences in saliva composition between partially engorged and fully engorged female ticks. R. microplus saliva is rich mainly in (i) hemelipoproteins and other transporter proteins, (ii) secreted cross-tick species conserved proteins, (iii) lipocalins, (iv) peptidase inhibitors, (v) antimicrobial peptides, (vii) glycine-rich proteins, (viii) housekeeping proteins and (ix) host proteins. This investigation represents the first proteomic study about R. microplus saliva, and reports the most comprehensive Ixodidae tick saliva proteome published to date. Our results improve the understanding of tick salivary modulators of host defense to tick feeding, and provide novel information on the tick-host relationship. |
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Similarly to other hematophagous ectoparasites, R. microplus saliva contains a collection of bioactive compounds that inhibit host defenses against tick feeding activity. Thus, the study of tick salivary components offers opportunities for the development of immunological based tick control methods and medicinal applications. So far, only a few proteins have been identified in cattle tick saliva. The aim of this work was to identify proteins present in R. microplus female tick saliva at different feeding stages. Proteomic analysis of R. microplus saliva allowed identifying peptides corresponding to 187 and 68 tick and bovine proteins, respectively. Our data confirm that (i) R. microplus saliva is complex, and (ii) that there are remarkable differences in saliva composition between partially engorged and fully engorged female ticks. R. microplus saliva is rich mainly in (i) hemelipoproteins and other transporter proteins, (ii) secreted cross-tick species conserved proteins, (iii) lipocalins, (iv) peptidase inhibitors, (v) antimicrobial peptides, (vii) glycine-rich proteins, (viii) housekeeping proteins and (ix) host proteins. This investigation represents the first proteomic study about R. microplus saliva, and reports the most comprehensive Ixodidae tick saliva proteome published to date. Our results improve the understanding of tick salivary modulators of host defense to tick feeding, and provide novel information on the tick-host relationship.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0094831</identifier><identifier>PMID: 24762651</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Acari ; Analysis ; Anaplasma ; Animals ; Antimicrobial agents ; Antimicrobial Cationic Peptides - metabolism ; Antimicrobial peptides ; Arachnids ; Arthropod Proteins - metabolism ; Babesia ; Bioactive compounds ; Biology and Life Sciences ; Boophilus ; Boophilus microplus ; Cattle ; Control methods ; Cystatins - metabolism ; Distribution ; Ectoparasites ; Feeding ; Female ; Females ; Genes, Essential ; Glycine ; Immunology ; Immunomodulation ; Lipocalin ; Lipocalins - metabolism ; Lipoproteins - metabolism ; Medicine and Health Sciences ; Modulators ; Parasites ; Peptidase ; Peptides ; Physiological aspects ; Postprandial Period ; Proteinase Inhibitory Proteins, Secretory - metabolism ; Proteins ; Proteome - metabolism ; Proteomics ; Rhipicephalus ; Rhipicephalus - metabolism ; Saliva ; Saliva - metabolism ; Ticks</subject><ispartof>PloS one, 2014-04, Vol.9 (4), p.e94831</ispartof><rights>COPYRIGHT 2014 Public Library of Science</rights><rights>2014 Tirloni et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2014 Tirloni et al 2014 Tirloni et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c651t-7c56e3f5b2b827d8d5f3f4bb4e8d8116cd841b4f76dfe3814dabeb1e37eb17183</citedby><cites>FETCH-LOGICAL-c651t-7c56e3f5b2b827d8d5f3f4bb4e8d8116cd841b4f76dfe3814dabeb1e37eb17183</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/PMC3998978/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3998978/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79569,79570</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24762651$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tirloni, Lucas</creatorcontrib><creatorcontrib>Reck, José</creatorcontrib><creatorcontrib>Terra, Renata Maria Soares</creatorcontrib><creatorcontrib>Martins, João Ricardo</creatorcontrib><creatorcontrib>Mulenga, Albert</creatorcontrib><creatorcontrib>Sherman, Nicholas E</creatorcontrib><creatorcontrib>Fox, Jay W</creatorcontrib><creatorcontrib>Yates, 3rd, John R</creatorcontrib><creatorcontrib>Termignoni, Carlos</creatorcontrib><creatorcontrib>Pinto, Antônio F M</creatorcontrib><creatorcontrib>Vaz, Jr, Itabajara da Silva</creatorcontrib><title>Proteomic analysis of cattle tick Rhipicephalus (Boophilus) microplus saliva: a comparison between partially and fully engorged females</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The cattle tick Rhipicephalus (Boophilus) microplus is one of the most harmful parasites affecting bovines. 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R. microplus saliva is rich mainly in (i) hemelipoproteins and other transporter proteins, (ii) secreted cross-tick species conserved proteins, (iii) lipocalins, (iv) peptidase inhibitors, (v) antimicrobial peptides, (vii) glycine-rich proteins, (viii) housekeeping proteins and (ix) host proteins. This investigation represents the first proteomic study about R. microplus saliva, and reports the most comprehensive Ixodidae tick saliva proteome published to date. Our results improve the understanding of tick salivary modulators of host defense to tick feeding, and provide novel information on the tick-host relationship.</description><subject>Acari</subject><subject>Analysis</subject><subject>Anaplasma</subject><subject>Animals</subject><subject>Antimicrobial agents</subject><subject>Antimicrobial Cationic Peptides - metabolism</subject><subject>Antimicrobial peptides</subject><subject>Arachnids</subject><subject>Arthropod Proteins - metabolism</subject><subject>Babesia</subject><subject>Bioactive compounds</subject><subject>Biology and Life Sciences</subject><subject>Boophilus</subject><subject>Boophilus microplus</subject><subject>Cattle</subject><subject>Control methods</subject><subject>Cystatins - metabolism</subject><subject>Distribution</subject><subject>Ectoparasites</subject><subject>Feeding</subject><subject>Female</subject><subject>Females</subject><subject>Genes, Essential</subject><subject>Glycine</subject><subject>Immunology</subject><subject>Immunomodulation</subject><subject>Lipocalin</subject><subject>Lipocalins - metabolism</subject><subject>Lipoproteins - metabolism</subject><subject>Medicine and Health Sciences</subject><subject>Modulators</subject><subject>Parasites</subject><subject>Peptidase</subject><subject>Peptides</subject><subject>Physiological aspects</subject><subject>Postprandial Period</subject><subject>Proteinase Inhibitory Proteins, Secretory - metabolism</subject><subject>Proteins</subject><subject>Proteome - metabolism</subject><subject>Proteomics</subject><subject>Rhipicephalus</subject><subject>Rhipicephalus - metabolism</subject><subject>Saliva</subject><subject>Saliva - metabolism</subject><subject>Ticks</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNptUttu1DAQjRCIlsIfILCEhMrDLrEdJw4PSKXiUqkSCMGzZTvjjRcnTmOnaL-A38bpptUW8WLP2GfOnBmdLHuO8zWmFX679dPYS7cefA_rPK8LTvGD7BjXlKxKktOHB_FR9iSEbZ4zysvycXZEiqokJcPH2Z9vo4_gO6uRTGy7YAPyBmkZowMUrf6Fvrd2sBqGVropoNMP3g-tTeEblKpGP8yvQTp7Ld8hibTvBjna4HukIP4G6FHKo5XO7VKLBplpjqDf-HEDKYVOOghPs0dGugDPlvsk-_np44_zL6vLr58vzs8uVzrJjatKsxKoYYooTqqGN8xQUyhVAG84xqVueIFVYaqyMUA5LhqpQGGgVTorzOlJ9nLPOzgfxLLDIDDDnKeV0BlxsUc0Xm7FMNpOjjvhpRU3D0m1mOfRDoQpSkpqRrFhUNSslqCIxIQRzUvTKJm43i_dJtVBo6GPo3T3SO__9LYVG38taF3zuprFnC4Eo7-aIETR2aDBOdmDn25010k1IVWCvvoH-v_pFtQmbV3Y3vjUV8-k4oxWjHFaVyyhXh-gWpAutsG7KVrfh_vAYg9MRghhBHM3G87FbNNbEWK2qVhsmspeHO7lrujWl_Qvs57nxw</recordid><startdate>20140424</startdate><enddate>20140424</enddate><creator>Tirloni, Lucas</creator><creator>Reck, José</creator><creator>Terra, Renata Maria Soares</creator><creator>Martins, João Ricardo</creator><creator>Mulenga, Albert</creator><creator>Sherman, Nicholas E</creator><creator>Fox, Jay W</creator><creator>Yates, 3rd, John R</creator><creator>Termignoni, Carlos</creator><creator>Pinto, Antônio F M</creator><creator>Vaz, Jr, Itabajara da Silva</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PIMPY</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20140424</creationdate><title>Proteomic analysis of cattle tick Rhipicephalus (Boophilus) microplus saliva: a comparison between partially and fully engorged females</title><author>Tirloni, Lucas ; Reck, José ; Terra, Renata Maria Soares ; Martins, João Ricardo ; Mulenga, Albert ; Sherman, Nicholas E ; Fox, Jay W ; Yates, 3rd, John R ; Termignoni, Carlos ; Pinto, Antônio F M ; Vaz, Jr, Itabajara da Silva</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c651t-7c56e3f5b2b827d8d5f3f4bb4e8d8116cd841b4f76dfe3814dabeb1e37eb17183</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Acari</topic><topic>Analysis</topic><topic>Anaplasma</topic><topic>Animals</topic><topic>Antimicrobial agents</topic><topic>Antimicrobial Cationic Peptides - metabolism</topic><topic>Antimicrobial peptides</topic><topic>Arachnids</topic><topic>Arthropod Proteins - metabolism</topic><topic>Babesia</topic><topic>Bioactive compounds</topic><topic>Biology and Life Sciences</topic><topic>Boophilus</topic><topic>Boophilus microplus</topic><topic>Cattle</topic><topic>Control methods</topic><topic>Cystatins - metabolism</topic><topic>Distribution</topic><topic>Ectoparasites</topic><topic>Feeding</topic><topic>Female</topic><topic>Females</topic><topic>Genes, Essential</topic><topic>Glycine</topic><topic>Immunology</topic><topic>Immunomodulation</topic><topic>Lipocalin</topic><topic>Lipocalins - metabolism</topic><topic>Lipoproteins - metabolism</topic><topic>Medicine and Health Sciences</topic><topic>Modulators</topic><topic>Parasites</topic><topic>Peptidase</topic><topic>Peptides</topic><topic>Physiological aspects</topic><topic>Postprandial Period</topic><topic>Proteinase Inhibitory Proteins, Secretory - metabolism</topic><topic>Proteins</topic><topic>Proteome - 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Similarly to other hematophagous ectoparasites, R. microplus saliva contains a collection of bioactive compounds that inhibit host defenses against tick feeding activity. Thus, the study of tick salivary components offers opportunities for the development of immunological based tick control methods and medicinal applications. So far, only a few proteins have been identified in cattle tick saliva. The aim of this work was to identify proteins present in R. microplus female tick saliva at different feeding stages. Proteomic analysis of R. microplus saliva allowed identifying peptides corresponding to 187 and 68 tick and bovine proteins, respectively. Our data confirm that (i) R. microplus saliva is complex, and (ii) that there are remarkable differences in saliva composition between partially engorged and fully engorged female ticks. R. microplus saliva is rich mainly in (i) hemelipoproteins and other transporter proteins, (ii) secreted cross-tick species conserved proteins, (iii) lipocalins, (iv) peptidase inhibitors, (v) antimicrobial peptides, (vii) glycine-rich proteins, (viii) housekeeping proteins and (ix) host proteins. This investigation represents the first proteomic study about R. microplus saliva, and reports the most comprehensive Ixodidae tick saliva proteome published to date. Our results improve the understanding of tick salivary modulators of host defense to tick feeding, and provide novel information on the tick-host relationship.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24762651</pmid><doi>10.1371/journal.pone.0094831</doi><oa>free_for_read</oa></addata></record> |
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source | Public Library of Science (PLoS) Journals Open Access; MEDLINE; DOAJ Directory of Open Access Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
subjects | Acari Analysis Anaplasma Animals Antimicrobial agents Antimicrobial Cationic Peptides - metabolism Antimicrobial peptides Arachnids Arthropod Proteins - metabolism Babesia Bioactive compounds Biology and Life Sciences Boophilus Boophilus microplus Cattle Control methods Cystatins - metabolism Distribution Ectoparasites Feeding Female Females Genes, Essential Glycine Immunology Immunomodulation Lipocalin Lipocalins - metabolism Lipoproteins - metabolism Medicine and Health Sciences Modulators Parasites Peptidase Peptides Physiological aspects Postprandial Period Proteinase Inhibitory Proteins, Secretory - metabolism Proteins Proteome - metabolism Proteomics Rhipicephalus Rhipicephalus - metabolism Saliva Saliva - metabolism Ticks |
title | Proteomic analysis of cattle tick Rhipicephalus (Boophilus) microplus saliva: a comparison between partially and fully engorged females |
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