In-depth proteomic analysis of Varroa destructor: Detection of DWV-complex, ABPV, VdMLV and honeybee proteins in the mite
We investigated pathogens in the parasitic honeybee mite Varroa destructor using nanoLC-MS/MS (TripleTOF) and 2D-E-MS/MS proteomics approaches supplemented with affinity-chromatography to concentrate trace target proteins. Peptides were detected from the currently uncharacterized Varroa destructor M...
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| Veröffentlicht in: | Scientific reports 2015-09, Vol.5 (1), p.13907-13907, Article 13907 |
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| creator | Erban, Tomas Harant, Karel Hubalek, Martin Vitamvas, Pavel Kamler, Martin Poltronieri, Palmiro Tyl, Jan Markovic, Martin Titera, Dalibor |
| description | We investigated pathogens in the parasitic honeybee mite
Varroa destructor
using nanoLC-MS/MS (TripleTOF) and 2D-E-MS/MS proteomics approaches supplemented with affinity-chromatography to concentrate trace target proteins. Peptides were detected from the currently uncharacterized
Varroa destructor
Macula-like virus (VdMLV), the deformed wing virus (DWV)-complex and the acute bee paralysis virus (ABPV). Peptide alignments revealed detection of complete structural DWV-complex block VP2-VP1-VP3, VDV-1 helicase and single-amino-acid substitution A/K/Q in VP1, the ABPV structural block VP1-VP4-VP2-VP3 including uncleaved VP4/VP2 and VdMLV coat protein. Isoforms of viral structural proteins of highest abundance were localized via 2D-E. The presence of all types of capsid/coat proteins of a particular virus suggested the presence of virions in
Varroa
. Also, matches between the MWs of viral structural proteins on 2D-E and their theoretical MWs indicated that viruses were not digested. The absence/scarce detection of non-structural proteins compared with high-abundance structural proteins suggest that the viruses did not replicate in the mite; hence, virions accumulate in the
Varroa
gut via hemolymph feeding. Hemolymph feeding also resulted in the detection of a variety of honeybee proteins. The advantages of MS-based proteomics for pathogen detection, false-positive pathogen detection, virus replication, posttranslational modifications and the presence of honeybee proteins in
Varroa
are discussed. |
| doi_str_mv | 10.1038/srep13907 |
| format | Article |
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Varroa destructor
using nanoLC-MS/MS (TripleTOF) and 2D-E-MS/MS proteomics approaches supplemented with affinity-chromatography to concentrate trace target proteins. Peptides were detected from the currently uncharacterized
Varroa destructor
Macula-like virus (VdMLV), the deformed wing virus (DWV)-complex and the acute bee paralysis virus (ABPV). Peptide alignments revealed detection of complete structural DWV-complex block VP2-VP1-VP3, VDV-1 helicase and single-amino-acid substitution A/K/Q in VP1, the ABPV structural block VP1-VP4-VP2-VP3 including uncleaved VP4/VP2 and VdMLV coat protein. Isoforms of viral structural proteins of highest abundance were localized via 2D-E. The presence of all types of capsid/coat proteins of a particular virus suggested the presence of virions in
Varroa
. Also, matches between the MWs of viral structural proteins on 2D-E and their theoretical MWs indicated that viruses were not digested. The absence/scarce detection of non-structural proteins compared with high-abundance structural proteins suggest that the viruses did not replicate in the mite; hence, virions accumulate in the
Varroa
gut via hemolymph feeding. Hemolymph feeding also resulted in the detection of a variety of honeybee proteins. The advantages of MS-based proteomics for pathogen detection, false-positive pathogen detection, virus replication, posttranslational modifications and the presence of honeybee proteins in
Varroa
are discussed.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep13907</identifier><identifier>PMID: 26358842</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/1647/2067 ; 631/326/417/1716 ; 631/326/596/2561 ; Amino acid substitution ; Animals ; Bees ; Chromatography, Liquid ; Coat protein ; Databases, Genetic ; DNA helicase ; Feeding ; Gastrointestinal tract ; Hemolymph ; Host-Pathogen Interactions ; Humanities and Social Sciences ; Isoforms ; Mites ; multidisciplinary ; Paralysis ; Pathogens ; Peptides ; Proteins ; Proteome ; Proteomics ; Proteomics - methods ; Science ; Structural proteins ; Tandem Mass Spectrometry ; Varroidae - virology ; Virions ; Viruses ; VP1 protein ; VP3 protein</subject><ispartof>Scientific reports, 2015-09, Vol.5 (1), p.13907-13907, Article 13907</ispartof><rights>The Author(s) 2015</rights><rights>Copyright Nature Publishing Group Sep 2015</rights><rights>Copyright © 2015, Macmillan Publishers Limited 2015 Macmillan Publishers Limited</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c438t-2a4db37bdd5d54fb325d17a124af94577bd79f69c31b5e69bae4bf4876b6be5f3</citedby><cites>FETCH-LOGICAL-c438t-2a4db37bdd5d54fb325d17a124af94577bd79f69c31b5e69bae4bf4876b6be5f3</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/PMC4566121/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4566121/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26358842$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Erban, Tomas</creatorcontrib><creatorcontrib>Harant, Karel</creatorcontrib><creatorcontrib>Hubalek, Martin</creatorcontrib><creatorcontrib>Vitamvas, Pavel</creatorcontrib><creatorcontrib>Kamler, Martin</creatorcontrib><creatorcontrib>Poltronieri, Palmiro</creatorcontrib><creatorcontrib>Tyl, Jan</creatorcontrib><creatorcontrib>Markovic, Martin</creatorcontrib><creatorcontrib>Titera, Dalibor</creatorcontrib><title>In-depth proteomic analysis of Varroa destructor: Detection of DWV-complex, ABPV, VdMLV and honeybee proteins in the mite</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>We investigated pathogens in the parasitic honeybee mite
Varroa destructor
using nanoLC-MS/MS (TripleTOF) and 2D-E-MS/MS proteomics approaches supplemented with affinity-chromatography to concentrate trace target proteins. Peptides were detected from the currently uncharacterized
Varroa destructor
Macula-like virus (VdMLV), the deformed wing virus (DWV)-complex and the acute bee paralysis virus (ABPV). Peptide alignments revealed detection of complete structural DWV-complex block VP2-VP1-VP3, VDV-1 helicase and single-amino-acid substitution A/K/Q in VP1, the ABPV structural block VP1-VP4-VP2-VP3 including uncleaved VP4/VP2 and VdMLV coat protein. Isoforms of viral structural proteins of highest abundance were localized via 2D-E. The presence of all types of capsid/coat proteins of a particular virus suggested the presence of virions in
Varroa
. Also, matches between the MWs of viral structural proteins on 2D-E and their theoretical MWs indicated that viruses were not digested. The absence/scarce detection of non-structural proteins compared with high-abundance structural proteins suggest that the viruses did not replicate in the mite; hence, virions accumulate in the
Varroa
gut via hemolymph feeding. Hemolymph feeding also resulted in the detection of a variety of honeybee proteins. The advantages of MS-based proteomics for pathogen detection, false-positive pathogen detection, virus replication, posttranslational modifications and the presence of honeybee proteins in
Varroa
are discussed.</description><subject>631/1647/2067</subject><subject>631/326/417/1716</subject><subject>631/326/596/2561</subject><subject>Amino acid substitution</subject><subject>Animals</subject><subject>Bees</subject><subject>Chromatography, Liquid</subject><subject>Coat protein</subject><subject>Databases, Genetic</subject><subject>DNA helicase</subject><subject>Feeding</subject><subject>Gastrointestinal tract</subject><subject>Hemolymph</subject><subject>Host-Pathogen Interactions</subject><subject>Humanities and Social Sciences</subject><subject>Isoforms</subject><subject>Mites</subject><subject>multidisciplinary</subject><subject>Paralysis</subject><subject>Pathogens</subject><subject>Peptides</subject><subject>Proteins</subject><subject>Proteome</subject><subject>Proteomics</subject><subject>Proteomics - methods</subject><subject>Science</subject><subject>Structural proteins</subject><subject>Tandem Mass Spectrometry</subject><subject>Varroidae - virology</subject><subject>Virions</subject><subject>Viruses</subject><subject>VP1 protein</subject><subject>VP3 protein</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNplkc1u1DAURiMEolXpghdAlthQ1JT4L45ZVCot0EqDYAFhGdnxTcdVYgfbQczb42rKaABvbOk7Or66X1E8x9UZrmjzJgaYMZWVeFQckorxklBCHu-9D4rjGO-qfDiRDMunxQGpKW8aRg6LzY0rDcxpjebgE_jJ9kg5NW6ijcgPqFUheIUMxBSWPvnwFl1Bgj5Z7-7zq-9t2ftpHuHXKbp496U9Ra35tGqzxKC1d7DRAFu3dRFZh9Ia0GQTPCueDGqMcPxwHxXfPrz_enldrj5_vLm8WJU9o00qiWJGU6GN4YazQVPCDRYKE6YGybjIiZBDLXuKNYdaagVMD6wRta418IEeFedb77zoCUwPLgU1dnOwkwqbzivb_Z04u-5u_c-O8brGBGfBqwdB8D-WvIhusrGHcVQO_BI7LDDmVGDJMvryH_TOLyGvM1ONlKLmkjWZOtlSffAx1zfshsFVd99pt-s0sy_2p9-RfxrMwOstEHPkbiHsffmf7TcHJawr</recordid><startdate>20150911</startdate><enddate>20150911</enddate><creator>Erban, Tomas</creator><creator>Harant, Karel</creator><creator>Hubalek, Martin</creator><creator>Vitamvas, Pavel</creator><creator>Kamler, Martin</creator><creator>Poltronieri, Palmiro</creator><creator>Tyl, Jan</creator><creator>Markovic, Martin</creator><creator>Titera, Dalibor</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</scope><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>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20150911</creationdate><title>In-depth proteomic analysis of Varroa destructor: Detection of DWV-complex, ABPV, VdMLV and honeybee proteins in the mite</title><author>Erban, Tomas ; Harant, Karel ; Hubalek, Martin ; Vitamvas, Pavel ; Kamler, Martin ; Poltronieri, Palmiro ; Tyl, Jan ; Markovic, Martin ; Titera, Dalibor</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c438t-2a4db37bdd5d54fb325d17a124af94577bd79f69c31b5e69bae4bf4876b6be5f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>631/1647/2067</topic><topic>631/326/417/1716</topic><topic>631/326/596/2561</topic><topic>Amino acid substitution</topic><topic>Animals</topic><topic>Bees</topic><topic>Chromatography, Liquid</topic><topic>Coat protein</topic><topic>Databases, Genetic</topic><topic>DNA helicase</topic><topic>Feeding</topic><topic>Gastrointestinal tract</topic><topic>Hemolymph</topic><topic>Host-Pathogen Interactions</topic><topic>Humanities and Social Sciences</topic><topic>Isoforms</topic><topic>Mites</topic><topic>multidisciplinary</topic><topic>Paralysis</topic><topic>Pathogens</topic><topic>Peptides</topic><topic>Proteins</topic><topic>Proteome</topic><topic>Proteomics</topic><topic>Proteomics - methods</topic><topic>Science</topic><topic>Structural proteins</topic><topic>Tandem Mass Spectrometry</topic><topic>Varroidae - virology</topic><topic>Virions</topic><topic>Viruses</topic><topic>VP1 protein</topic><topic>VP3 protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Erban, Tomas</creatorcontrib><creatorcontrib>Harant, Karel</creatorcontrib><creatorcontrib>Hubalek, Martin</creatorcontrib><creatorcontrib>Vitamvas, Pavel</creatorcontrib><creatorcontrib>Kamler, Martin</creatorcontrib><creatorcontrib>Poltronieri, Palmiro</creatorcontrib><creatorcontrib>Tyl, Jan</creatorcontrib><creatorcontrib>Markovic, Martin</creatorcontrib><creatorcontrib>Titera, Dalibor</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Erban, Tomas</au><au>Harant, Karel</au><au>Hubalek, Martin</au><au>Vitamvas, Pavel</au><au>Kamler, Martin</au><au>Poltronieri, Palmiro</au><au>Tyl, Jan</au><au>Markovic, Martin</au><au>Titera, Dalibor</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>In-depth proteomic analysis of Varroa destructor: Detection of DWV-complex, ABPV, VdMLV and honeybee proteins in the mite</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2015-09-11</date><risdate>2015</risdate><volume>5</volume><issue>1</issue><spage>13907</spage><epage>13907</epage><pages>13907-13907</pages><artnum>13907</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>We investigated pathogens in the parasitic honeybee mite
Varroa destructor
using nanoLC-MS/MS (TripleTOF) and 2D-E-MS/MS proteomics approaches supplemented with affinity-chromatography to concentrate trace target proteins. Peptides were detected from the currently uncharacterized
Varroa destructor
Macula-like virus (VdMLV), the deformed wing virus (DWV)-complex and the acute bee paralysis virus (ABPV). Peptide alignments revealed detection of complete structural DWV-complex block VP2-VP1-VP3, VDV-1 helicase and single-amino-acid substitution A/K/Q in VP1, the ABPV structural block VP1-VP4-VP2-VP3 including uncleaved VP4/VP2 and VdMLV coat protein. Isoforms of viral structural proteins of highest abundance were localized via 2D-E. The presence of all types of capsid/coat proteins of a particular virus suggested the presence of virions in
Varroa
. Also, matches between the MWs of viral structural proteins on 2D-E and their theoretical MWs indicated that viruses were not digested. The absence/scarce detection of non-structural proteins compared with high-abundance structural proteins suggest that the viruses did not replicate in the mite; hence, virions accumulate in the
Varroa
gut via hemolymph feeding. Hemolymph feeding also resulted in the detection of a variety of honeybee proteins. The advantages of MS-based proteomics for pathogen detection, false-positive pathogen detection, virus replication, posttranslational modifications and the presence of honeybee proteins in
Varroa
are discussed.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>26358842</pmid><doi>10.1038/srep13907</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/1647/2067 631/326/417/1716 631/326/596/2561 Amino acid substitution Animals Bees Chromatography, Liquid Coat protein Databases, Genetic DNA helicase Feeding Gastrointestinal tract Hemolymph Host-Pathogen Interactions Humanities and Social Sciences Isoforms Mites multidisciplinary Paralysis Pathogens Peptides Proteins Proteome Proteomics Proteomics - methods Science Structural proteins Tandem Mass Spectrometry Varroidae - virology Virions Viruses VP1 protein VP3 protein |
| title | In-depth proteomic analysis of Varroa destructor: Detection of DWV-complex, ABPV, VdMLV and honeybee proteins in the mite |
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