Characterization and functional analysis of serpin-1 like gene from oak silkworm Antheraea pernyi
Serpins are a broadly distributed family of proteases found in various organisms that play an important role in regulating the immune response. Here, we identified a serpin-1 gene from Antheraea pernyi that encodes a 279 amino acid protein with a molecular weight of 30.8 kDa. We expressed the recomb...
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| Veröffentlicht in: | Bulletin of entomological research 2017-10, Vol.107 (5), p.620-626 |
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| creator | Yu, H.M. Zhu, B.J. Sun, Y. Wei, G.Q. Wang, L. Qian, C. Nadeem Abbas, M. Liu, C.L. |
| description | Serpins are a broadly distributed family of proteases found in various organisms that play an important role in regulating the immune response. Here, we identified a serpin-1 gene from Antheraea pernyi that encodes a 279 amino acid protein with a molecular weight of 30.8 kDa. We expressed the recombinant Ap-serpin-1 protein in Escherichia coli and used the purified protein to prepare rabbit anti-Ap-serpin-1 polyclonal antibodies. We calculated the enzyme-linked immunosorbent assay titer of the antibody as 1:128000. Quantitative real-time polymerase chain reaction analysis revealed that Ap-serpin-1 was expressed in all examined tissues, including hemolymph, malpighian tubules, midgut, silk gland, integument and the fat body; the highest Ap-serpin-1 expression levels was detected in the fat body. We next investigated the expression patterns of Ap-serpin-1 in both fat body and hemolymph samples, following treatment with E. coli, Beauveria bassiana, Micrococcus luteus and nuclear polyhedrosis virus (NPV). We reported that NPV and M. luteus significantly enhanced Ap-serpin-1 expression in the fat body. While, in the hemolymph samples, treatment with B. bassiana and M. luteus was shown to upregulate Ap-serpin-1 expression at 24 h induction. Altogether, our results suggest that Ap-serpin-1 is involved in the innate immunity of A. pernyi. |
| doi_str_mv | 10.1017/S000748531700013X |
| format | Article |
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Here, we identified a serpin-1 gene from Antheraea pernyi that encodes a 279 amino acid protein with a molecular weight of 30.8 kDa. We expressed the recombinant Ap-serpin-1 protein in Escherichia coli and used the purified protein to prepare rabbit anti-Ap-serpin-1 polyclonal antibodies. We calculated the enzyme-linked immunosorbent assay titer of the antibody as 1:128000. Quantitative real-time polymerase chain reaction analysis revealed that Ap-serpin-1 was expressed in all examined tissues, including hemolymph, malpighian tubules, midgut, silk gland, integument and the fat body; the highest Ap-serpin-1 expression levels was detected in the fat body. We next investigated the expression patterns of Ap-serpin-1 in both fat body and hemolymph samples, following treatment with E. coli, Beauveria bassiana, Micrococcus luteus and nuclear polyhedrosis virus (NPV). We reported that NPV and M. luteus significantly enhanced Ap-serpin-1 expression in the fat body. While, in the hemolymph samples, treatment with B. bassiana and M. luteus was shown to upregulate Ap-serpin-1 expression at 24 h induction. Altogether, our results suggest that Ap-serpin-1 is involved in the innate immunity of A. pernyi.</description><identifier>ISSN: 0007-4853</identifier><identifier>EISSN: 1475-2670</identifier><identifier>DOI: 10.1017/S000748531700013X</identifier><identifier>PMID: 28228181</identifier><language>eng</language><publisher>Cambridge, UK: Cambridge University Press</publisher><subject>Amino acids ; Animals ; Antibodies ; Beauveria bassiana ; Biochemistry ; Cloning ; Defence mechanisms ; E coli ; ELISA ; Enzyme-linked immunosorbent assay ; Enzymes ; Escherichia coli ; Fat body ; Fat Body - metabolism ; Functional analysis ; Genes ; Genomes ; Hemolymph ; Hemolymph - metabolism ; Immune response ; Immune system ; Immunity ; Innate immunity ; Insect Proteins - genetics ; Insect Proteins - isolation & purification ; Insect Proteins - metabolism ; Integument ; Life Cycle Stages ; Male ; Malpighian tubules ; Microorganisms ; Midgut ; Molecular biology ; Molecular weight ; Moths - physiology ; Nucleotide sequence ; Oak ; PCR ; Physiology ; Polyclonal antibodies ; Polymerase chain reaction ; Proteins ; Rabbits ; Recombinants ; Research Papers ; Serine proteinase inhibitors ; Serpins - genetics ; Serpins - isolation & purification ; Serpins - metabolism ; Silk ; Silk gland ; Tissue ; Viruses</subject><ispartof>Bulletin of entomological research, 2017-10, Vol.107 (5), p.620-626</ispartof><rights>Copyright © Cambridge University Press 2017</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c373t-4448107b5e6d945554f23c7e53cf6f717712bb75fa6cf91ee03859c5b571070a3</citedby><cites>FETCH-LOGICAL-c373t-4448107b5e6d945554f23c7e53cf6f717712bb75fa6cf91ee03859c5b571070a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.cambridge.org/core/product/identifier/S000748531700013X/type/journal_article$$EHTML$$P50$$Gcambridge$$H</linktohtml><link.rule.ids>164,314,780,784,27923,27924,55627</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28228181$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yu, H.M.</creatorcontrib><creatorcontrib>Zhu, B.J.</creatorcontrib><creatorcontrib>Sun, Y.</creatorcontrib><creatorcontrib>Wei, G.Q.</creatorcontrib><creatorcontrib>Wang, L.</creatorcontrib><creatorcontrib>Qian, C.</creatorcontrib><creatorcontrib>Nadeem Abbas, M.</creatorcontrib><creatorcontrib>Liu, C.L.</creatorcontrib><title>Characterization and functional analysis of serpin-1 like gene from oak silkworm Antheraea pernyi</title><title>Bulletin of entomological research</title><addtitle>Bull. Entomol. Res</addtitle><description>Serpins are a broadly distributed family of proteases found in various organisms that play an important role in regulating the immune response. Here, we identified a serpin-1 gene from Antheraea pernyi that encodes a 279 amino acid protein with a molecular weight of 30.8 kDa. We expressed the recombinant Ap-serpin-1 protein in Escherichia coli and used the purified protein to prepare rabbit anti-Ap-serpin-1 polyclonal antibodies. We calculated the enzyme-linked immunosorbent assay titer of the antibody as 1:128000. Quantitative real-time polymerase chain reaction analysis revealed that Ap-serpin-1 was expressed in all examined tissues, including hemolymph, malpighian tubules, midgut, silk gland, integument and the fat body; the highest Ap-serpin-1 expression levels was detected in the fat body. We next investigated the expression patterns of Ap-serpin-1 in both fat body and hemolymph samples, following treatment with E. coli, Beauveria bassiana, Micrococcus luteus and nuclear polyhedrosis virus (NPV). We reported that NPV and M. luteus significantly enhanced Ap-serpin-1 expression in the fat body. While, in the hemolymph samples, treatment with B. bassiana and M. luteus was shown to upregulate Ap-serpin-1 expression at 24 h induction. Altogether, our results suggest that Ap-serpin-1 is involved in the innate immunity of A. pernyi.</description><subject>Amino acids</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Beauveria bassiana</subject><subject>Biochemistry</subject><subject>Cloning</subject><subject>Defence mechanisms</subject><subject>E coli</subject><subject>ELISA</subject><subject>Enzyme-linked immunosorbent assay</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Fat body</subject><subject>Fat Body - metabolism</subject><subject>Functional analysis</subject><subject>Genes</subject><subject>Genomes</subject><subject>Hemolymph</subject><subject>Hemolymph - metabolism</subject><subject>Immune response</subject><subject>Immune system</subject><subject>Immunity</subject><subject>Innate immunity</subject><subject>Insect Proteins - genetics</subject><subject>Insect Proteins - isolation & purification</subject><subject>Insect Proteins - metabolism</subject><subject>Integument</subject><subject>Life Cycle Stages</subject><subject>Male</subject><subject>Malpighian tubules</subject><subject>Microorganisms</subject><subject>Midgut</subject><subject>Molecular biology</subject><subject>Molecular weight</subject><subject>Moths - physiology</subject><subject>Nucleotide sequence</subject><subject>Oak</subject><subject>PCR</subject><subject>Physiology</subject><subject>Polyclonal antibodies</subject><subject>Polymerase chain reaction</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>Recombinants</subject><subject>Research Papers</subject><subject>Serine proteinase inhibitors</subject><subject>Serpins - genetics</subject><subject>Serpins - isolation & purification</subject><subject>Serpins - metabolism</subject><subject>Silk</subject><subject>Silk gland</subject><subject>Tissue</subject><subject>Viruses</subject><issn>0007-4853</issn><issn>1475-2670</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp1kEFr3DAQhUVpaTZJf0AvQdBLLk41lmTJx7AkbWChhySQm5G1o42ytrWVbMLm11fLbktIyWnmMd97Qo-Qr8AugIH6fssYU0JLDipvwB8-kBkIJYuyUuwjme3Oxe5-RI5TespS1KL-TI5KXZYaNMyImT-aaOyI0b-Y0YeBmmFJ3TTYnTBdlqbbJp9ocDRh3PihANr5NdIVDkhdDD0NZk2T79bPIfb0chgfMRo0dINx2PpT8smZLuGXwzwh99dXd_OfxeLXj5v55aKwXPGxEEJoYKqVWC1rIaUUruRWoeTWVU6BUlC2rZLOVNbVgMi4lrWVrVTZxgw_Ief73E0MvydMY9P7ZLHrzIBhSg1oBVKCFjyj396gT2GK-aOZqgWXqhSVzhTsKRtDShFds4m-N3HbAGt2_Tf_9Z89Z4fkqe1x-c_xt_AM8EOo6dvolyt89fa7sX8Arz-OlQ</recordid><startdate>20171001</startdate><enddate>20171001</enddate><creator>Yu, H.M.</creator><creator>Zhu, B.J.</creator><creator>Sun, Y.</creator><creator>Wei, G.Q.</creator><creator>Wang, L.</creator><creator>Qian, C.</creator><creator>Nadeem Abbas, M.</creator><creator>Liu, C.L.</creator><general>Cambridge University Press</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>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T7</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F1W</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H95</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L.G</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20171001</creationdate><title>Characterization and functional analysis of serpin-1 like gene from oak silkworm Antheraea pernyi</title><author>Yu, H.M. ; Zhu, B.J. ; Sun, Y. ; Wei, G.Q. ; Wang, L. ; Qian, C. ; Nadeem Abbas, M. ; Liu, C.L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c373t-4448107b5e6d945554f23c7e53cf6f717712bb75fa6cf91ee03859c5b571070a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Amino acids</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Beauveria bassiana</topic><topic>Biochemistry</topic><topic>Cloning</topic><topic>Defence mechanisms</topic><topic>E coli</topic><topic>ELISA</topic><topic>Enzyme-linked immunosorbent assay</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Fat body</topic><topic>Fat Body - metabolism</topic><topic>Functional analysis</topic><topic>Genes</topic><topic>Genomes</topic><topic>Hemolymph</topic><topic>Hemolymph - metabolism</topic><topic>Immune response</topic><topic>Immune system</topic><topic>Immunity</topic><topic>Innate immunity</topic><topic>Insect Proteins - genetics</topic><topic>Insect Proteins - isolation & purification</topic><topic>Insect Proteins - metabolism</topic><topic>Integument</topic><topic>Life Cycle Stages</topic><topic>Male</topic><topic>Malpighian tubules</topic><topic>Microorganisms</topic><topic>Midgut</topic><topic>Molecular biology</topic><topic>Molecular weight</topic><topic>Moths - physiology</topic><topic>Nucleotide sequence</topic><topic>Oak</topic><topic>PCR</topic><topic>Physiology</topic><topic>Polyclonal antibodies</topic><topic>Polymerase chain reaction</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>Recombinants</topic><topic>Research Papers</topic><topic>Serine proteinase inhibitors</topic><topic>Serpins - genetics</topic><topic>Serpins - 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Academic</collection><jtitle>Bulletin of entomological research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yu, H.M.</au><au>Zhu, B.J.</au><au>Sun, Y.</au><au>Wei, G.Q.</au><au>Wang, L.</au><au>Qian, C.</au><au>Nadeem Abbas, M.</au><au>Liu, C.L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization and functional analysis of serpin-1 like gene from oak silkworm Antheraea pernyi</atitle><jtitle>Bulletin of entomological research</jtitle><addtitle>Bull. Entomol. Res</addtitle><date>2017-10-01</date><risdate>2017</risdate><volume>107</volume><issue>5</issue><spage>620</spage><epage>626</epage><pages>620-626</pages><issn>0007-4853</issn><eissn>1475-2670</eissn><abstract>Serpins are a broadly distributed family of proteases found in various organisms that play an important role in regulating the immune response. Here, we identified a serpin-1 gene from Antheraea pernyi that encodes a 279 amino acid protein with a molecular weight of 30.8 kDa. We expressed the recombinant Ap-serpin-1 protein in Escherichia coli and used the purified protein to prepare rabbit anti-Ap-serpin-1 polyclonal antibodies. We calculated the enzyme-linked immunosorbent assay titer of the antibody as 1:128000. Quantitative real-time polymerase chain reaction analysis revealed that Ap-serpin-1 was expressed in all examined tissues, including hemolymph, malpighian tubules, midgut, silk gland, integument and the fat body; the highest Ap-serpin-1 expression levels was detected in the fat body. We next investigated the expression patterns of Ap-serpin-1 in both fat body and hemolymph samples, following treatment with E. coli, Beauveria bassiana, Micrococcus luteus and nuclear polyhedrosis virus (NPV). We reported that NPV and M. luteus significantly enhanced Ap-serpin-1 expression in the fat body. While, in the hemolymph samples, treatment with B. bassiana and M. luteus was shown to upregulate Ap-serpin-1 expression at 24 h induction. Altogether, our results suggest that Ap-serpin-1 is involved in the innate immunity of A. pernyi.</abstract><cop>Cambridge, UK</cop><pub>Cambridge University Press</pub><pmid>28228181</pmid><doi>10.1017/S000748531700013X</doi><tpages>7</tpages></addata></record> |
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| subjects | Amino acids Animals Antibodies Beauveria bassiana Biochemistry Cloning Defence mechanisms E coli ELISA Enzyme-linked immunosorbent assay Enzymes Escherichia coli Fat body Fat Body - metabolism Functional analysis Genes Genomes Hemolymph Hemolymph - metabolism Immune response Immune system Immunity Innate immunity Insect Proteins - genetics Insect Proteins - isolation & purification Insect Proteins - metabolism Integument Life Cycle Stages Male Malpighian tubules Microorganisms Midgut Molecular biology Molecular weight Moths - physiology Nucleotide sequence Oak PCR Physiology Polyclonal antibodies Polymerase chain reaction Proteins Rabbits Recombinants Research Papers Serine proteinase inhibitors Serpins - genetics Serpins - isolation & purification Serpins - metabolism Silk Silk gland Tissue Viruses |
| title | Characterization and functional analysis of serpin-1 like gene from oak silkworm Antheraea pernyi |
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