Proteomics of larval hemolymph in Bombyx mori reveals various nutrient-storage and immunity-related proteins
The silkworm, Bombyx mori, is an important economic insect for its production of silk. The larvae of many lepidopteran insects are major agricultural pests and often silkworm is explored as a model organism for other lepidopteran pest species. The hemolymph of caterpillars contains a lot of nutrient...
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creator | Zhang, Yan Dong, Zhaoming Wang, Dandan Wu, Yong Song, Qianru Gu, Peiming Zhao, Ping Xia, Qingyou |
description | The silkworm, Bombyx mori, is an important economic insect for its production of silk. The larvae of many lepidopteran insects are major agricultural pests and often silkworm is explored as a model organism for other lepidopteran pest species. The hemolymph of caterpillars contains a lot of nutrient and immune components. In this study, we applied liquid chromatography–tandem mass spectrometry to gain a better understanding of the larval hemolymph proteomics in B. mori. We identified 752 proteins in hemolymph collected from day-4 fourth instar and day-7 fifth instar. Nearly half the identified proteins (49 %) were predicted to function as binding proteins and 46 % were predicted to have catalytic activities. Apolipophorins, storage proteins, and 30K proteins constituted the most abundant groups of nutrient-storage proteins. Of them, 30K proteins showed large differences between fourth instar larvae and fifth instar larvae. Besides nutrient-storage proteins, protease inhibitors are also expressed very highly in hemolymph. The analysis also revealed lots of immunity-related proteins, including recognition, signaling, effectors and other proteins, comprising multiple immunity pathways in hemolymph. Our data provide an exhaustive research of nutrient-storage proteins and immunity-related proteins in larval hemolymph, and will pave the way for future physiological and pathological studies of caterpillars. |
doi_str_mv | 10.1007/s00726-014-1665-7 |
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The larvae of many lepidopteran insects are major agricultural pests and often silkworm is explored as a model organism for other lepidopteran pest species. The hemolymph of caterpillars contains a lot of nutrient and immune components. In this study, we applied liquid chromatography–tandem mass spectrometry to gain a better understanding of the larval hemolymph proteomics in B. mori. We identified 752 proteins in hemolymph collected from day-4 fourth instar and day-7 fifth instar. Nearly half the identified proteins (49 %) were predicted to function as binding proteins and 46 % were predicted to have catalytic activities. Apolipophorins, storage proteins, and 30K proteins constituted the most abundant groups of nutrient-storage proteins. Of them, 30K proteins showed large differences between fourth instar larvae and fifth instar larvae. Besides nutrient-storage proteins, protease inhibitors are also expressed very highly in hemolymph. The analysis also revealed lots of immunity-related proteins, including recognition, signaling, effectors and other proteins, comprising multiple immunity pathways in hemolymph. Our data provide an exhaustive research of nutrient-storage proteins and immunity-related proteins in larval hemolymph, and will pave the way for future physiological and pathological studies of caterpillars.</description><identifier>ISSN: 0939-4451</identifier><identifier>EISSN: 1438-2199</identifier><identifier>DOI: 10.1007/s00726-014-1665-7</identifier><identifier>PMID: 24402669</identifier><language>eng</language><publisher>Vienna: Springer-Verlag</publisher><subject>Analytical Chemistry ; Animals ; binding proteins ; Biochemical Engineering ; Biochemistry ; Biomedical and Life Sciences ; Bombyx - chemistry ; Bombyx - genetics ; Bombyx - growth & development ; Bombyx - immunology ; Bombyx mori ; catalytic activity ; Caterpillars ; Economics ; hemolymph ; Hemolymph - chemistry ; Hemolymph - immunology ; immunity ; insect larvae ; Insect Proteins - chemistry ; Insect Proteins - genetics ; Insect Proteins - immunology ; Insects ; instars ; Larva - chemistry ; Larva - genetics ; Larva - growth & development ; Larva - immunology ; Larvae ; Life Sciences ; liquid chromatography ; Mass Spectrometry ; Molecular Sequence Data ; Neurobiology ; Original Article ; Pests ; proteinase inhibitors ; Proteins ; Proteomics ; silk ; Silkworms ; storage proteins ; tandem mass spectrometry</subject><ispartof>Amino acids, 2014-04, Vol.46 (4), p.1021-1031</ispartof><rights>Springer-Verlag Wien 2014</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c495t-50901ba8413174f3f12d9447a7d74d8bbcb25c5e54e9a74c08a2180ea0968c663</citedby><cites>FETCH-LOGICAL-c495t-50901ba8413174f3f12d9447a7d74d8bbcb25c5e54e9a74c08a2180ea0968c663</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00726-014-1665-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00726-014-1665-7$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24402669$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Yan</creatorcontrib><creatorcontrib>Dong, Zhaoming</creatorcontrib><creatorcontrib>Wang, Dandan</creatorcontrib><creatorcontrib>Wu, Yong</creatorcontrib><creatorcontrib>Song, Qianru</creatorcontrib><creatorcontrib>Gu, Peiming</creatorcontrib><creatorcontrib>Zhao, Ping</creatorcontrib><creatorcontrib>Xia, Qingyou</creatorcontrib><title>Proteomics of larval hemolymph in Bombyx mori reveals various nutrient-storage and immunity-related proteins</title><title>Amino acids</title><addtitle>Amino Acids</addtitle><addtitle>Amino Acids</addtitle><description>The silkworm, Bombyx mori, is an important economic insect for its production of silk. The larvae of many lepidopteran insects are major agricultural pests and often silkworm is explored as a model organism for other lepidopteran pest species. The hemolymph of caterpillars contains a lot of nutrient and immune components. In this study, we applied liquid chromatography–tandem mass spectrometry to gain a better understanding of the larval hemolymph proteomics in B. mori. We identified 752 proteins in hemolymph collected from day-4 fourth instar and day-7 fifth instar. Nearly half the identified proteins (49 %) were predicted to function as binding proteins and 46 % were predicted to have catalytic activities. Apolipophorins, storage proteins, and 30K proteins constituted the most abundant groups of nutrient-storage proteins. Of them, 30K proteins showed large differences between fourth instar larvae and fifth instar larvae. Besides nutrient-storage proteins, protease inhibitors are also expressed very highly in hemolymph. The analysis also revealed lots of immunity-related proteins, including recognition, signaling, effectors and other proteins, comprising multiple immunity pathways in hemolymph. Our data provide an exhaustive research of nutrient-storage proteins and immunity-related proteins in larval hemolymph, and will pave the way for future physiological and pathological studies of caterpillars.</description><subject>Analytical Chemistry</subject><subject>Animals</subject><subject>binding proteins</subject><subject>Biochemical Engineering</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Bombyx - chemistry</subject><subject>Bombyx - genetics</subject><subject>Bombyx - growth & development</subject><subject>Bombyx - immunology</subject><subject>Bombyx mori</subject><subject>catalytic activity</subject><subject>Caterpillars</subject><subject>Economics</subject><subject>hemolymph</subject><subject>Hemolymph - chemistry</subject><subject>Hemolymph - immunology</subject><subject>immunity</subject><subject>insect larvae</subject><subject>Insect Proteins - chemistry</subject><subject>Insect Proteins - genetics</subject><subject>Insect Proteins - immunology</subject><subject>Insects</subject><subject>instars</subject><subject>Larva - chemistry</subject><subject>Larva - genetics</subject><subject>Larva - growth & development</subject><subject>Larva - immunology</subject><subject>Larvae</subject><subject>Life Sciences</subject><subject>liquid chromatography</subject><subject>Mass Spectrometry</subject><subject>Molecular Sequence Data</subject><subject>Neurobiology</subject><subject>Original Article</subject><subject>Pests</subject><subject>proteinase inhibitors</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>silk</subject><subject>Silkworms</subject><subject>storage proteins</subject><subject>tandem mass spectrometry</subject><issn>0939-4451</issn><issn>1438-2199</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkU1vFSEYhYnR2Gv1B7hREjduqLwMw8fSNn4lTTTRrgkzw9zSDHCFmRvvvy_XqcZ00cgCFjznnBcOQi-BngGl8l2pGxOEAicgREvkI7QB3ijCQOvHaEN1ownnLZygZ6XcUApMgXiKThjnlAmhN2j6ltPsUvB9wWnEk817O-FrF9J0CLtr7CM-T6E7_MIhZY-z2zs7Fby32ael4LjM2bs4kzKnbLcO2zhgH8IS_Xwg2U12dgPeHTN8LM_Rk7Gq3Yu78xRdffzw4-Izufz66cvF-0vSc93OpKWaQmcVhwYkH5sR2KA5l1YOkg-q6_qOtX3rWu60lbynyjJQ1FmqheqFaE7R29W3Bv9cXJlN8KV302Sjq1MbaBnVkinB_gOtP60Zg6aib-6hN2nJsT6kUlSDFOp3NqxUn1Mp2Y1ml32w-WCAmmNrZm3N1NbMsTUjq-bVnfPSBTf8VfypqQJsBUq9iluX_4l-wPX1KhptMnabfTFX3xkFQY9LKdbcAm52q3g</recordid><startdate>20140401</startdate><enddate>20140401</enddate><creator>Zhang, Yan</creator><creator>Dong, Zhaoming</creator><creator>Wang, Dandan</creator><creator>Wu, Yong</creator><creator>Song, Qianru</creator><creator>Gu, Peiming</creator><creator>Zhao, Ping</creator><creator>Xia, Qingyou</creator><general>Springer-Verlag</general><general>Springer Vienna</general><general>Springer Nature B.V</general><scope>FBQ</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>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</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>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>7U5</scope><scope>8FD</scope><scope>L7M</scope></search><sort><creationdate>20140401</creationdate><title>Proteomics of larval hemolymph in Bombyx mori reveals various nutrient-storage and immunity-related proteins</title><author>Zhang, Yan ; Dong, Zhaoming ; Wang, Dandan ; Wu, Yong ; Song, Qianru ; Gu, Peiming ; Zhao, Ping ; Xia, Qingyou</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c495t-50901ba8413174f3f12d9447a7d74d8bbcb25c5e54e9a74c08a2180ea0968c663</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Analytical Chemistry</topic><topic>Animals</topic><topic>binding proteins</topic><topic>Biochemical Engineering</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Bombyx - chemistry</topic><topic>Bombyx - genetics</topic><topic>Bombyx - growth & development</topic><topic>Bombyx - immunology</topic><topic>Bombyx mori</topic><topic>catalytic activity</topic><topic>Caterpillars</topic><topic>Economics</topic><topic>hemolymph</topic><topic>Hemolymph - chemistry</topic><topic>Hemolymph - immunology</topic><topic>immunity</topic><topic>insect larvae</topic><topic>Insect Proteins - chemistry</topic><topic>Insect Proteins - genetics</topic><topic>Insect Proteins - immunology</topic><topic>Insects</topic><topic>instars</topic><topic>Larva - chemistry</topic><topic>Larva - genetics</topic><topic>Larva - growth & development</topic><topic>Larva - immunology</topic><topic>Larvae</topic><topic>Life Sciences</topic><topic>liquid chromatography</topic><topic>Mass Spectrometry</topic><topic>Molecular Sequence Data</topic><topic>Neurobiology</topic><topic>Original Article</topic><topic>Pests</topic><topic>proteinase inhibitors</topic><topic>Proteins</topic><topic>Proteomics</topic><topic>silk</topic><topic>Silkworms</topic><topic>storage proteins</topic><topic>tandem mass spectrometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Yan</creatorcontrib><creatorcontrib>Dong, Zhaoming</creatorcontrib><creatorcontrib>Wang, Dandan</creatorcontrib><creatorcontrib>Wu, Yong</creatorcontrib><creatorcontrib>Song, Qianru</creatorcontrib><creatorcontrib>Gu, Peiming</creatorcontrib><creatorcontrib>Zhao, Ping</creatorcontrib><creatorcontrib>Xia, Qingyou</creatorcontrib><collection>AGRIS</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>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology 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>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection (ProQuest)</collection><collection>Natural Science Collection (ProQuest)</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</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>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Materials Science Collection</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>MEDLINE - Academic</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Amino acids</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Yan</au><au>Dong, Zhaoming</au><au>Wang, Dandan</au><au>Wu, Yong</au><au>Song, Qianru</au><au>Gu, Peiming</au><au>Zhao, Ping</au><au>Xia, Qingyou</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteomics of larval hemolymph in Bombyx mori reveals various nutrient-storage and immunity-related proteins</atitle><jtitle>Amino acids</jtitle><stitle>Amino Acids</stitle><addtitle>Amino Acids</addtitle><date>2014-04-01</date><risdate>2014</risdate><volume>46</volume><issue>4</issue><spage>1021</spage><epage>1031</epage><pages>1021-1031</pages><issn>0939-4451</issn><eissn>1438-2199</eissn><abstract>The silkworm, Bombyx mori, is an important economic insect for its production of silk. The larvae of many lepidopteran insects are major agricultural pests and often silkworm is explored as a model organism for other lepidopteran pest species. The hemolymph of caterpillars contains a lot of nutrient and immune components. In this study, we applied liquid chromatography–tandem mass spectrometry to gain a better understanding of the larval hemolymph proteomics in B. mori. We identified 752 proteins in hemolymph collected from day-4 fourth instar and day-7 fifth instar. Nearly half the identified proteins (49 %) were predicted to function as binding proteins and 46 % were predicted to have catalytic activities. Apolipophorins, storage proteins, and 30K proteins constituted the most abundant groups of nutrient-storage proteins. Of them, 30K proteins showed large differences between fourth instar larvae and fifth instar larvae. Besides nutrient-storage proteins, protease inhibitors are also expressed very highly in hemolymph. The analysis also revealed lots of immunity-related proteins, including recognition, signaling, effectors and other proteins, comprising multiple immunity pathways in hemolymph. Our data provide an exhaustive research of nutrient-storage proteins and immunity-related proteins in larval hemolymph, and will pave the way for future physiological and pathological studies of caterpillars.</abstract><cop>Vienna</cop><pub>Springer-Verlag</pub><pmid>24402669</pmid><doi>10.1007/s00726-014-1665-7</doi><tpages>11</tpages></addata></record> |
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subjects | Analytical Chemistry Animals binding proteins Biochemical Engineering Biochemistry Biomedical and Life Sciences Bombyx - chemistry Bombyx - genetics Bombyx - growth & development Bombyx - immunology Bombyx mori catalytic activity Caterpillars Economics hemolymph Hemolymph - chemistry Hemolymph - immunology immunity insect larvae Insect Proteins - chemistry Insect Proteins - genetics Insect Proteins - immunology Insects instars Larva - chemistry Larva - genetics Larva - growth & development Larva - immunology Larvae Life Sciences liquid chromatography Mass Spectrometry Molecular Sequence Data Neurobiology Original Article Pests proteinase inhibitors Proteins Proteomics silk Silkworms storage proteins tandem mass spectrometry |
title | Proteomics of larval hemolymph in Bombyx mori reveals various nutrient-storage and immunity-related proteins |
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