Molecular characteristics of three thymosin-repeat proteins from Marsupenaeus japonicus and their responses to WSSV infection
β-thymosins, a family of highly conserved peptides, play a vital role in wound-healing, angiogenesis,antimicrobial process and antiviral immunity. Three novel β-thymosin-repeat proteins, named mjthm4, mjthm3 and mjthm2, were cloned from Marsupenaeus japonicus using expressed sequence tags（EST） from...
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| Veröffentlicht in: | Acta oceanologica Sinica 2016-04, Vol.35 (4), p.44-50 |
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| creator | Ma, Jinyou Ruan, Lingwei Xu, Xun Gao, Zhaoming |
| description | β-thymosins, a family of highly conserved peptides, play a vital role in wound-healing, angiogenesis,antimicrobial process and antiviral immunity. Three novel β-thymosin-repeat proteins, named mjthm4, mjthm3 and mjthm2, were cloned from Marsupenaeus japonicus using expressed sequence tags（EST） from suppression subtractive hybridization. The mjthm4, mjthm3 and mjthm2 c DNAs possessed open reading frames that encoded166, 128 and 90 amino acid residue polypeptides and contained four, three and two β-thymosin actin binding modules, respectively. Blast analysis demonstrated that mjthm4, mjthm3 and mjthm2 shared high homology with known invertebrate multi-repeat β-thymosins. These proteins are ubiquitously expressed in all of the examined tissues, and the transcriptional levels were highest in the intestine. Further investigation revealed that mjthm4,mjthm3 and mjthm2 were remarkably up-regulated 6 h after WSSV infection. Moreover, while mjthm4 transcriptional levels displayed no changes, mjthm3 and mjthm2 levels decreased in the virus-resistant shrimps.The results indicate that mjthm4, mjthm3 and mjthm2 are novel multi-repeat β-thymosin homologues, have a close relationship with WSSV infection, and might contribute to a better understanding of host defense and/or virus invasion interactions in shrimps. |
| doi_str_mv | 10.1007/s13131-016-0835-8 |
| format | Article |
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Three novel β-thymosin-repeat proteins, named mjthm4, mjthm3 and mjthm2, were cloned from Marsupenaeus japonicus using expressed sequence tags（EST） from suppression subtractive hybridization. The mjthm4, mjthm3 and mjthm2 c DNAs possessed open reading frames that encoded166, 128 and 90 amino acid residue polypeptides and contained four, three and two β-thymosin actin binding modules, respectively. Blast analysis demonstrated that mjthm4, mjthm3 and mjthm2 shared high homology with known invertebrate multi-repeat β-thymosins. These proteins are ubiquitously expressed in all of the examined tissues, and the transcriptional levels were highest in the intestine. Further investigation revealed that mjthm4,mjthm3 and mjthm2 were remarkably up-regulated 6 h after WSSV infection. Moreover, while mjthm4 transcriptional levels displayed no changes, mjthm3 and mjthm2 levels decreased in the virus-resistant shrimps.The results indicate that mjthm4, mjthm3 and mjthm2 are novel multi-repeat β-thymosin homologues, have a close relationship with WSSV infection, and might contribute to a better understanding of host defense and/or virus invasion interactions in shrimps.</description><identifier>ISSN: 0253-505X</identifier><identifier>EISSN: 1869-1099</identifier><identifier>DOI: 10.1007/s13131-016-0835-8</identifier><language>eng</language><publisher>Beijing: The Chinese Society of Oceanography</publisher><subject>Actin ; Amino acids ; Angiogenesis ; Antiviral agents ; Climatology ; Decapoda ; Earth and Environmental Science ; Earth Sciences ; Ecology ; Engineering Fluid Dynamics ; Environmental Chemistry ; Expressed sequence tags ; Homology ; Hybridization ; Immunity ; Infections ; Intestine ; Intestines ; Marine ; Marine & Freshwater Sciences ; Marsupenaeus japonicus ; Nucleotide sequence ; Oceanography ; Open reading frames ; Peptides ; Polypeptides ; Proteins ; Shrimps ; Viruses ; White spot syndrome virus ; Wound healing ; WSSV感染 ; 分子特征 ; 反应 ; 抑制消减杂交 ; 日本囊对虾 ; 肌动蛋白 ; 胸腺肽 ; 表达序列标签</subject><ispartof>Acta oceanologica Sinica, 2016-04, Vol.35 (4), p.44-50</ispartof><rights>The Chinese Society of Oceanography and Springer-Verlag Berlin Heidelberg 2016</rights><rights>The Chinese Society of Oceanography and Springer-Verlag Berlin Heidelberg 2016.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c404t-c3979242b56409ba7e10e76c498d67df0d7545e470d5ece9acaff8083c868e323</citedby><cites>FETCH-LOGICAL-c404t-c3979242b56409ba7e10e76c498d67df0d7545e470d5ece9acaff8083c868e323</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://image.cqvip.com/vip1000/qk/86790X/86790X.jpg</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s13131-016-0835-8$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1780747685?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>314,776,780,21369,27903,27904,33723,33724,41467,42536,43784,51297</link.rule.ids></links><search><creatorcontrib>Ma, Jinyou</creatorcontrib><creatorcontrib>Ruan, Lingwei</creatorcontrib><creatorcontrib>Xu, Xun</creatorcontrib><creatorcontrib>Gao, Zhaoming</creatorcontrib><title>Molecular characteristics of three thymosin-repeat proteins from Marsupenaeus japonicus and their responses to WSSV infection</title><title>Acta oceanologica Sinica</title><addtitle>Acta Oceanol. Sin</addtitle><addtitle>Acta Oceanologica Sinica</addtitle><description>β-thymosins, a family of highly conserved peptides, play a vital role in wound-healing, angiogenesis,antimicrobial process and antiviral immunity. Three novel β-thymosin-repeat proteins, named mjthm4, mjthm3 and mjthm2, were cloned from Marsupenaeus japonicus using expressed sequence tags（EST） from suppression subtractive hybridization. The mjthm4, mjthm3 and mjthm2 c DNAs possessed open reading frames that encoded166, 128 and 90 amino acid residue polypeptides and contained four, three and two β-thymosin actin binding modules, respectively. Blast analysis demonstrated that mjthm4, mjthm3 and mjthm2 shared high homology with known invertebrate multi-repeat β-thymosins. These proteins are ubiquitously expressed in all of the examined tissues, and the transcriptional levels were highest in the intestine. Further investigation revealed that mjthm4,mjthm3 and mjthm2 were remarkably up-regulated 6 h after WSSV infection. Moreover, while mjthm4 transcriptional levels displayed no changes, mjthm3 and mjthm2 levels decreased in the virus-resistant shrimps.The results indicate that mjthm4, mjthm3 and mjthm2 are novel multi-repeat β-thymosin homologues, have a close relationship with WSSV infection, and might contribute to a better understanding of host defense and/or virus invasion interactions in shrimps.</description><subject>Actin</subject><subject>Amino acids</subject><subject>Angiogenesis</subject><subject>Antiviral agents</subject><subject>Climatology</subject><subject>Decapoda</subject><subject>Earth and Environmental Science</subject><subject>Earth Sciences</subject><subject>Ecology</subject><subject>Engineering Fluid Dynamics</subject><subject>Environmental Chemistry</subject><subject>Expressed sequence tags</subject><subject>Homology</subject><subject>Hybridization</subject><subject>Immunity</subject><subject>Infections</subject><subject>Intestine</subject><subject>Intestines</subject><subject>Marine</subject><subject>Marine & Freshwater Sciences</subject><subject>Marsupenaeus japonicus</subject><subject>Nucleotide sequence</subject><subject>Oceanography</subject><subject>Open reading frames</subject><subject>Peptides</subject><subject>Polypeptides</subject><subject>Proteins</subject><subject>Shrimps</subject><subject>Viruses</subject><subject>White spot syndrome virus</subject><subject>Wound healing</subject><subject>WSSV感染</subject><subject>分子特征</subject><subject>反应</subject><subject>抑制消减杂交</subject><subject>日本囊对虾</subject><subject>肌动蛋白</subject><subject>胸腺肽</subject><subject>表达序列标签</subject><issn>0253-505X</issn><issn>1869-1099</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNp9kU2LFDEQhoMoOI7-AG9BL15aK-nO11EWv2AXD-vXLWTT1TsZZpLeVPdhD_53s8wi4mEJJEV4n6qXehl7KeCtADDvSPTtdCB0B7ZXnX3ENsJq1wlw7jHbgFR9p0D9esqeEe0BlFC92bDfF-WAcT2EyuMu1BAXrImWFImXiS-7itju22OhlLuKM4aFz7UsmDLxqZYjvwiV1hlzwJX4Pswlp9iqkMcGYqq8IrVPQuJL4T8vL3_wlCeMSyr5OXsyhQPhi_t3y75__PDt7HN3_vXTl7P3510cYFi62Dvj5CCvlB7AXQWDAtDoODg7ajNOMBo1KBwMjAojuhDDNNm2h2i1xV72W_bm1LdZv1mRFn9MFPFwCBnLSl4YB87Ioe1wy17_J92XtebmzksnnOq1FPIhlTAWzGC0VU0lTqpYC1HFyc81HUO99QL8XWz-FJtvsfm72LxtjDwx1LT5Gus_nR-AXt0P2pV8fdO4v5N0MyK1kND_ASgipxo</recordid><startdate>20160401</startdate><enddate>20160401</enddate><creator>Ma, Jinyou</creator><creator>Ruan, Lingwei</creator><creator>Xu, Xun</creator><creator>Gao, Zhaoming</creator><general>The Chinese Society of Oceanography</general><general>Springer Nature B.V</general><scope>2RA</scope><scope>92L</scope><scope>CQIGP</scope><scope>W94</scope><scope>~WA</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7ST</scope><scope>7TG</scope><scope>7TN</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F1W</scope><scope>GNUQQ</scope><scope>H96</scope><scope>HCIFZ</scope><scope>KL.</scope><scope>L.G</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PYCSY</scope><scope>SOI</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>BBNVY</scope><scope>FR3</scope><scope>H95</scope><scope>H97</scope><scope>H98</scope><scope>H99</scope><scope>L.F</scope><scope>LK8</scope><scope>M7P</scope><scope>P64</scope></search><sort><creationdate>20160401</creationdate><title>Molecular characteristics of three thymosin-repeat proteins from Marsupenaeus japonicus and their responses to WSSV infection</title><author>Ma, Jinyou ; 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Sin</stitle><addtitle>Acta Oceanologica Sinica</addtitle><date>2016-04-01</date><risdate>2016</risdate><volume>35</volume><issue>4</issue><spage>44</spage><epage>50</epage><pages>44-50</pages><issn>0253-505X</issn><eissn>1869-1099</eissn><abstract>β-thymosins, a family of highly conserved peptides, play a vital role in wound-healing, angiogenesis,antimicrobial process and antiviral immunity. Three novel β-thymosin-repeat proteins, named mjthm4, mjthm3 and mjthm2, were cloned from Marsupenaeus japonicus using expressed sequence tags（EST） from suppression subtractive hybridization. The mjthm4, mjthm3 and mjthm2 c DNAs possessed open reading frames that encoded166, 128 and 90 amino acid residue polypeptides and contained four, three and two β-thymosin actin binding modules, respectively. Blast analysis demonstrated that mjthm4, mjthm3 and mjthm2 shared high homology with known invertebrate multi-repeat β-thymosins. These proteins are ubiquitously expressed in all of the examined tissues, and the transcriptional levels were highest in the intestine. Further investigation revealed that mjthm4,mjthm3 and mjthm2 were remarkably up-regulated 6 h after WSSV infection. Moreover, while mjthm4 transcriptional levels displayed no changes, mjthm3 and mjthm2 levels decreased in the virus-resistant shrimps.The results indicate that mjthm4, mjthm3 and mjthm2 are novel multi-repeat β-thymosin homologues, have a close relationship with WSSV infection, and might contribute to a better understanding of host defense and/or virus invasion interactions in shrimps.</abstract><cop>Beijing</cop><pub>The Chinese Society of Oceanography</pub><doi>10.1007/s13131-016-0835-8</doi><tpages>7</tpages></addata></record> |
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| subjects | Actin Amino acids Angiogenesis Antiviral agents Climatology Decapoda Earth and Environmental Science Earth Sciences Ecology Engineering Fluid Dynamics Environmental Chemistry Expressed sequence tags Homology Hybridization Immunity Infections Intestine Intestines Marine Marine & Freshwater Sciences Marsupenaeus japonicus Nucleotide sequence Oceanography Open reading frames Peptides Polypeptides Proteins Shrimps Viruses White spot syndrome virus Wound healing WSSV感染 分子特征 反应 抑制消减杂交 日本囊对虾 肌动蛋白 胸腺肽 表达序列标签 |
| title | Molecular characteristics of three thymosin-repeat proteins from Marsupenaeus japonicus and their responses to WSSV infection |
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