Identification of a serine proteinase homolog (Sp-SPH) involved in immune defense in the mud crab Scylla paramamosain
Clip domain serine proteinase homologs are involved in many biological processes including immune response. To identify the immune function of a serine proteinase homolog (Sp-SPH), originally isolated from hemocytes of the mud crab, Scylla paramamosain, the Sp-SPH was expressed recombinantly and pur...
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| Veröffentlicht in: | PloS one 2013-05, Vol.8 (5), p.e63787-e63787 |
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| creator | Zhang, Qiu-xia Liu, Hai-peng Chen, Rong-yuan Shen, Kai-li Wang, Ke-jian |
| description | Clip domain serine proteinase homologs are involved in many biological processes including immune response. To identify the immune function of a serine proteinase homolog (Sp-SPH), originally isolated from hemocytes of the mud crab, Scylla paramamosain, the Sp-SPH was expressed recombinantly and purified for further studies. It was found that the Sp-SPH protein could bind to a number of bacteria (including Aeromonas hydrophila, Escherichia coli, Staphylococcus aureus, Vibrio fluvialis, Vibrio harveyi and Vibrio parahemolyticus), bacterial cell wall components such as lipopolysaccharide or peptidoglycan (PGN), and β-1, 3-glucan of fungus. But no direct antibacterial activity of Sp-SPH protein was shown by using minimum inhibitory concentration or minimum bactericidal concentration assays. Nevertheless, the Sp-SPH protein was found to significantly enhance the crab hemocyte adhesion activity (paired t-test, P |
| doi_str_mv | 10.1371/journal.pone.0063787 |
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To identify the immune function of a serine proteinase homolog (Sp-SPH), originally isolated from hemocytes of the mud crab, Scylla paramamosain, the Sp-SPH was expressed recombinantly and purified for further studies. It was found that the Sp-SPH protein could bind to a number of bacteria (including Aeromonas hydrophila, Escherichia coli, Staphylococcus aureus, Vibrio fluvialis, Vibrio harveyi and Vibrio parahemolyticus), bacterial cell wall components such as lipopolysaccharide or peptidoglycan (PGN), and β-1, 3-glucan of fungus. But no direct antibacterial activity of Sp-SPH protein was shown by using minimum inhibitory concentration or minimum bactericidal concentration assays. Nevertheless, the Sp-SPH protein was found to significantly enhance the crab hemocyte adhesion activity (paired t-test, P<0.05), and increase phenoloxidase activity if triggered by PGN in vitro (paired t-test, P<0.05). Importantly, the Sp-SPH protein was demonstrated to promote the survival rate of the animals after challenge with A. hydrophila or V. parahemolyticus which were both recognized by Sp-SPH protein, if pre-incubated with Sp-SPH protein, respectively. Whereas, the crabs died much faster when challenged with Vibrio alginolyiicus, a pathogenic bacterium not recognized by Sp-SPH protein, compared to those of crabs challenged with A. hydrophila or V. parahemolyticus when pre-coated with Sp-SPH protein. Taken together, these data suggested that Sp-SPH molecule might play an important role in immune defense against bacterial infection in the mud crab S. paramamosain.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0063787</identifier><identifier>PMID: 23724001</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Adhesion tests ; Aeromonas hydrophila ; Agriculture ; Animals ; Antibacterial activity ; Bacteria ; Bacteria - drug effects ; Bacteria - metabolism ; Bacterial infections ; Biochemistry ; Biological activity ; Biology ; Brachyura - drug effects ; Brachyura - enzymology ; Brachyura - immunology ; Brachyura - microbiology ; Cell Adhesion - drug effects ; Cell Extracts ; Cell walls ; Cloning ; Crabs ; Crustaceans ; Decapoda ; Drosophila ; E coli ; Earth science ; Electrophoresis, Polyacrylamide Gel ; Environmental science ; Escherichia coli ; Fungi - drug effects ; Fungi - metabolism ; Glucan ; Hemocytes ; Hemocytes - cytology ; Hemocytes - drug effects ; Hemocytes - enzymology ; Homology ; Immune response ; Immune system ; Immunity - drug effects ; Immunology ; In vitro methods and tests ; Insects ; Laboratories ; Lipopolysaccharides ; Manduca sexta ; Minimum inhibitory concentration ; Molecular biology ; Monophenol Monooxygenase - metabolism ; Mud ; Pacifastacus leniusculus ; Pattern recognition ; Peptidoglycans ; Phenoloxidase ; Protein Binding - drug effects ; Proteinase ; Proteins ; Recombinant Proteins - pharmacology ; Scylla ; Scylla paramamosain ; Sequence Homology, Amino Acid ; Serine ; Serine Proteases - metabolism ; Serine proteinase ; Signal transduction ; Staphylococcus aureus ; Tenebrio molitor ; Veterinary Science ; Vibrio ; Vibrio fluvialis ; Vibrio harveyi ; Waterborne diseases</subject><ispartof>PloS one, 2013-05, Vol.8 (5), p.e63787-e63787</ispartof><rights>2013 Zhang et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://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>2013 Zhang et al 2013 Zhang et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c559t-38b50126c7b1bcb7fc633f0e227dd71b8f785ea2852b991d73197eda1452bae23</citedby><cites>FETCH-LOGICAL-c559t-38b50126c7b1bcb7fc633f0e227dd71b8f785ea2852b991d73197eda1452bae23</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/PMC3665817/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3665817/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2100,2926,23865,27923,27924,53790,53792,79371,79372</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23724001$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Allodi, Silvana</contributor><creatorcontrib>Zhang, Qiu-xia</creatorcontrib><creatorcontrib>Liu, Hai-peng</creatorcontrib><creatorcontrib>Chen, Rong-yuan</creatorcontrib><creatorcontrib>Shen, Kai-li</creatorcontrib><creatorcontrib>Wang, Ke-jian</creatorcontrib><title>Identification of a serine proteinase homolog (Sp-SPH) involved in immune defense in the mud crab Scylla paramamosain</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Clip domain serine proteinase homologs are involved in many biological processes including immune response. To identify the immune function of a serine proteinase homolog (Sp-SPH), originally isolated from hemocytes of the mud crab, Scylla paramamosain, the Sp-SPH was expressed recombinantly and purified for further studies. It was found that the Sp-SPH protein could bind to a number of bacteria (including Aeromonas hydrophila, Escherichia coli, Staphylococcus aureus, Vibrio fluvialis, Vibrio harveyi and Vibrio parahemolyticus), bacterial cell wall components such as lipopolysaccharide or peptidoglycan (PGN), and β-1, 3-glucan of fungus. But no direct antibacterial activity of Sp-SPH protein was shown by using minimum inhibitory concentration or minimum bactericidal concentration assays. Nevertheless, the Sp-SPH protein was found to significantly enhance the crab hemocyte adhesion activity (paired t-test, P<0.05), and increase phenoloxidase activity if triggered by PGN in vitro (paired t-test, P<0.05). Importantly, the Sp-SPH protein was demonstrated to promote the survival rate of the animals after challenge with A. hydrophila or V. parahemolyticus which were both recognized by Sp-SPH protein, if pre-incubated with Sp-SPH protein, respectively. Whereas, the crabs died much faster when challenged with Vibrio alginolyiicus, a pathogenic bacterium not recognized by Sp-SPH protein, compared to those of crabs challenged with A. hydrophila or V. parahemolyticus when pre-coated with Sp-SPH protein. Taken together, these data suggested that Sp-SPH molecule might play an important role in immune defense against bacterial infection in the mud crab S. paramamosain.</description><subject>Adhesion tests</subject><subject>Aeromonas hydrophila</subject><subject>Agriculture</subject><subject>Animals</subject><subject>Antibacterial activity</subject><subject>Bacteria</subject><subject>Bacteria - drug effects</subject><subject>Bacteria - metabolism</subject><subject>Bacterial infections</subject><subject>Biochemistry</subject><subject>Biological activity</subject><subject>Biology</subject><subject>Brachyura - drug effects</subject><subject>Brachyura - enzymology</subject><subject>Brachyura - immunology</subject><subject>Brachyura - microbiology</subject><subject>Cell Adhesion - drug effects</subject><subject>Cell Extracts</subject><subject>Cell walls</subject><subject>Cloning</subject><subject>Crabs</subject><subject>Crustaceans</subject><subject>Decapoda</subject><subject>Drosophila</subject><subject>E coli</subject><subject>Earth science</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Environmental science</subject><subject>Escherichia coli</subject><subject>Fungi - drug effects</subject><subject>Fungi - metabolism</subject><subject>Glucan</subject><subject>Hemocytes</subject><subject>Hemocytes - cytology</subject><subject>Hemocytes - drug effects</subject><subject>Hemocytes - enzymology</subject><subject>Homology</subject><subject>Immune response</subject><subject>Immune system</subject><subject>Immunity - drug effects</subject><subject>Immunology</subject><subject>In vitro methods and tests</subject><subject>Insects</subject><subject>Laboratories</subject><subject>Lipopolysaccharides</subject><subject>Manduca sexta</subject><subject>Minimum inhibitory concentration</subject><subject>Molecular biology</subject><subject>Monophenol Monooxygenase - metabolism</subject><subject>Mud</subject><subject>Pacifastacus leniusculus</subject><subject>Pattern recognition</subject><subject>Peptidoglycans</subject><subject>Phenoloxidase</subject><subject>Protein Binding - drug effects</subject><subject>Proteinase</subject><subject>Proteins</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Scylla</subject><subject>Scylla paramamosain</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serine</subject><subject>Serine Proteases - metabolism</subject><subject>Serine proteinase</subject><subject>Signal transduction</subject><subject>Staphylococcus aureus</subject><subject>Tenebrio molitor</subject><subject>Veterinary Science</subject><subject>Vibrio</subject><subject>Vibrio fluvialis</subject><subject>Vibrio harveyi</subject><subject>Waterborne diseases</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</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><sourceid>DOA</sourceid><recordid>eNqNkk9v1DAQxSMEoqXwDRBY4lIOu_hPYscXJFQBXakSSAtna-JMdr1K7GAnK_Xb42W3VYs4cPJo_Jvn8dMriteMLplQ7MMuzNFDvxyDxyWlUqhaPSnOmRZ8ITkVTx_UZ8WLlHaUVqKW8nlxxoXiJaXsvJhXLfrJdc7C5IInoSNAEkbnkYwxTOg8JCTbMIQ-bMjlelysv1-_J87vQ7_HNhfEDcOc8RY79JnNnWmLZJhbYiM0ZG1v-x7ICBEGGEIC518WzzroE746nRfFzy-ff1xdL26-fV1dfbpZ2KrS00LUTUUZl1Y1rLGN6qwUoqPIuWpbxZq6U3WFwOuKN1qzVgmmFbbAytwA5OKieHvUHfuQzMmxZJjI8lRJXmZidSTaADszRjdAvDUBnPnTCHFjIE7O9mjqbJ_mVnEoZckaDSVKaEGyvGStLM1aH0-vzc2Arc3GRugfiT6-8W5rNmFvhJRVzVQWuDwJxPBrxjSZwSWL2T2PYT7srXXeWwn9H2ilSq1LUWX03V_ov40oj5SNIaWI3f3ejJpD4O6mzCFw5hS4PPbm4Z_vh-4SJn4DyQTTrg</recordid><startdate>20130528</startdate><enddate>20130528</enddate><creator>Zhang, Qiu-xia</creator><creator>Liu, Hai-peng</creator><creator>Chen, Rong-yuan</creator><creator>Shen, Kai-li</creator><creator>Wang, Ke-jian</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>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20130528</creationdate><title>Identification of a serine proteinase homolog (Sp-SPH) involved in immune defense in the mud crab Scylla paramamosain</title><author>Zhang, Qiu-xia ; Liu, Hai-peng ; Chen, Rong-yuan ; Shen, Kai-li ; Wang, Ke-jian</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c559t-38b50126c7b1bcb7fc633f0e227dd71b8f785ea2852b991d73197eda1452bae23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Adhesion tests</topic><topic>Aeromonas hydrophila</topic><topic>Agriculture</topic><topic>Animals</topic><topic>Antibacterial activity</topic><topic>Bacteria</topic><topic>Bacteria - drug effects</topic><topic>Bacteria - metabolism</topic><topic>Bacterial infections</topic><topic>Biochemistry</topic><topic>Biological activity</topic><topic>Biology</topic><topic>Brachyura - drug effects</topic><topic>Brachyura - enzymology</topic><topic>Brachyura - immunology</topic><topic>Brachyura - microbiology</topic><topic>Cell Adhesion - drug effects</topic><topic>Cell Extracts</topic><topic>Cell walls</topic><topic>Cloning</topic><topic>Crabs</topic><topic>Crustaceans</topic><topic>Decapoda</topic><topic>Drosophila</topic><topic>E coli</topic><topic>Earth science</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Environmental science</topic><topic>Escherichia coli</topic><topic>Fungi - drug effects</topic><topic>Fungi - metabolism</topic><topic>Glucan</topic><topic>Hemocytes</topic><topic>Hemocytes - cytology</topic><topic>Hemocytes - drug effects</topic><topic>Hemocytes - enzymology</topic><topic>Homology</topic><topic>Immune response</topic><topic>Immune system</topic><topic>Immunity - 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Academic</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Qiu-xia</au><au>Liu, Hai-peng</au><au>Chen, Rong-yuan</au><au>Shen, Kai-li</au><au>Wang, Ke-jian</au><au>Allodi, Silvana</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of a serine proteinase homolog (Sp-SPH) involved in immune defense in the mud crab Scylla paramamosain</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2013-05-28</date><risdate>2013</risdate><volume>8</volume><issue>5</issue><spage>e63787</spage><epage>e63787</epage><pages>e63787-e63787</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Clip domain serine proteinase homologs are involved in many biological processes including immune response. To identify the immune function of a serine proteinase homolog (Sp-SPH), originally isolated from hemocytes of the mud crab, Scylla paramamosain, the Sp-SPH was expressed recombinantly and purified for further studies. It was found that the Sp-SPH protein could bind to a number of bacteria (including Aeromonas hydrophila, Escherichia coli, Staphylococcus aureus, Vibrio fluvialis, Vibrio harveyi and Vibrio parahemolyticus), bacterial cell wall components such as lipopolysaccharide or peptidoglycan (PGN), and β-1, 3-glucan of fungus. But no direct antibacterial activity of Sp-SPH protein was shown by using minimum inhibitory concentration or minimum bactericidal concentration assays. Nevertheless, the Sp-SPH protein was found to significantly enhance the crab hemocyte adhesion activity (paired t-test, P<0.05), and increase phenoloxidase activity if triggered by PGN in vitro (paired t-test, P<0.05). Importantly, the Sp-SPH protein was demonstrated to promote the survival rate of the animals after challenge with A. hydrophila or V. parahemolyticus which were both recognized by Sp-SPH protein, if pre-incubated with Sp-SPH protein, respectively. Whereas, the crabs died much faster when challenged with Vibrio alginolyiicus, a pathogenic bacterium not recognized by Sp-SPH protein, compared to those of crabs challenged with A. hydrophila or V. parahemolyticus when pre-coated with Sp-SPH protein. Taken together, these data suggested that Sp-SPH molecule might play an important role in immune defense against bacterial infection in the mud crab S. paramamosain.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23724001</pmid><doi>10.1371/journal.pone.0063787</doi><oa>free_for_read</oa></addata></record> |
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| recordid | cdi_plos_journals_1355907624 |
| source | PLoS; MEDLINE; Full-Text Journals in Chemistry (Open access); DOAJ Directory of Open Access Journals; PubMed Central; EZB Electronic Journals Library |
| subjects | Adhesion tests Aeromonas hydrophila Agriculture Animals Antibacterial activity Bacteria Bacteria - drug effects Bacteria - metabolism Bacterial infections Biochemistry Biological activity Biology Brachyura - drug effects Brachyura - enzymology Brachyura - immunology Brachyura - microbiology Cell Adhesion - drug effects Cell Extracts Cell walls Cloning Crabs Crustaceans Decapoda Drosophila E coli Earth science Electrophoresis, Polyacrylamide Gel Environmental science Escherichia coli Fungi - drug effects Fungi - metabolism Glucan Hemocytes Hemocytes - cytology Hemocytes - drug effects Hemocytes - enzymology Homology Immune response Immune system Immunity - drug effects Immunology In vitro methods and tests Insects Laboratories Lipopolysaccharides Manduca sexta Minimum inhibitory concentration Molecular biology Monophenol Monooxygenase - metabolism Mud Pacifastacus leniusculus Pattern recognition Peptidoglycans Phenoloxidase Protein Binding - drug effects Proteinase Proteins Recombinant Proteins - pharmacology Scylla Scylla paramamosain Sequence Homology, Amino Acid Serine Serine Proteases - metabolism Serine proteinase Signal transduction Staphylococcus aureus Tenebrio molitor Veterinary Science Vibrio Vibrio fluvialis Vibrio harveyi Waterborne diseases |
| title | Identification of a serine proteinase homolog (Sp-SPH) involved in immune defense in the mud crab Scylla paramamosain |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-10T15%3A51%3A32IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Identification%20of%20a%20serine%20proteinase%20homolog%20(Sp-SPH)%20involved%20in%20immune%20defense%20in%20the%20mud%20crab%20Scylla%20paramamosain&rft.jtitle=PloS%20one&rft.au=Zhang,%20Qiu-xia&rft.date=2013-05-28&rft.volume=8&rft.issue=5&rft.spage=e63787&rft.epage=e63787&rft.pages=e63787-e63787&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0063787&rft_dat=%3Cproquest_plos_%3E1357499435%3C/proquest_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1355907624&rft_id=info:pmid/23724001&rft_doaj_id=oai_doaj_org_article_805392c72a4641b9a4e6ada61b5087c0&rfr_iscdi=true |