Molecular characterization and serological reactivity of a vacuolar ATP synthase subunit ε-like protein from Clonorchis sinensis
The vacuolar ATPase enzyme complex (V-ATPase) pumps protons across membranes, energized by hydrolysis of ATP. Extensive investigations on structural and biochemical features of these molecules have implied their importance in the physiological process. In this study, a full-length sequence encoding...
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| Veröffentlicht in: | Parasitology research (1987) 2014-04, Vol.113 (4), p.1545-1554 |
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| creator | Lv, Xiaoli Huang, Lisi Chen, Wenjun Wang, Xiaoyun Huang, Yan Deng, Chuanhuan Sun, Jiufeng Tian, Yanli Mao, Qiang Lei, Huali Yu, Xinbing |
| description | The vacuolar ATPase enzyme complex (V-ATPase) pumps protons across membranes, energized by hydrolysis of ATP. Extensive investigations on structural and biochemical features of these molecules have implied their importance in the physiological process. In this study, a full-length sequence encoding a vacuolar ATP synthase subunit ε-like protein of
Clonorchis sinensis
(
Cs
ATP-ε) was isolated from our cDNA library. The hypothetical 226 amino acid sequence shared 76 % identity with ATP-ε proteins of
Schistosoma japonicum
and above 55 % identity with ATP-ε proteins from human and other eukaryotes. Characteristic Asp
140
amino acid residues and seven B-cell epitopes were predicted in this sequence. The complete coding sequence of the gene was expressed in
Escherichia coli
. Recombinant
Cs
ATP-ε (r
Cs
ATP-ε) protein could be probed by anti-r
Cs
ATP-ε rat serum and
C.sinensis
-infected human serum in Western blotting experiment, indicating that it is an antigen of strong antigenicity. The high level of antibody titers (1:204,800) showed that
Cs
ATP-ε has a powerful immunogenicity. Both the increased level and the change trend of IgG1/IgG2a subtypes in serum showed that the r
Cs
ATP-ε can induce strong combined Th1/Th2 immune responses in rats and stimulate the immune response changes to the dominant Th2 from Th1 along with long time infection. The results of immunoblot and immunolocalization demonstrated that
Cs
ATP-ε was consecutively expressed at various developmental stages of the parasite, which was supported by real-time PCR analysis. In immunohistochemistry,
Cs
ATP-ε was localized on the intestine, vitellarium, and testicle of an adult worm and excretory bladder of metacercaria, implying that
Cs
ATP-ε may relate to energy intake and metabolism. This fundamental study would contribute to further researches that are related to growth and development and immunomodulation of
C. sinensis
. |
| doi_str_mv | 10.1007/s00436-014-3799-7 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1753461910</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1507795241</sourcerecordid><originalsourceid>FETCH-LOGICAL-c377t-8d7880d4caba07d73a9cba44461d1a494f6213f7bc94afd25882bd65d2fd45e03</originalsourceid><addsrcrecordid>eNqNkc2OFCEURonROO3oA7gxLN2UQgFFsZx0_EvG6GJck1tATTPSMHKrJml3PpSv4TNJp0eXxtUluef7csMh5Dlnrzhj-jUyJsXQMS47oY3p9AOy4VL0HTdKPSQbZtqbcS7OyBPEG8a4HqR8TM56qYTSQmzIj48lBbcmqNTtoIJbQo3fYYklU8ieYqgllevoINEa2jrexeVAy0yB3oFbyzF5cfWZ4iEvO8BAcZ3WHBf662eX4tdAb2tZQsx0rmVPt6nkUt0uIsWYQ8aIT8mjGRKGZ_fznHx5--Zq-767_PTuw_bisnNC66UbvR5H5qWDCZj2WoBxE0gpB-45SCPnoedi1pMzEmbfq3HsJz8o389eqsDEOXl56m0HfVsDLnYf0YWUIIeyouVaiVZm-H-gimltVC95Q_kJdbUg1jDb2xr3UA-WM3uUZE-SbJNkj5KsbpkX9_XrtA_-b-KPlQb0JwDbKl-Ham_KWnP7nX-0_gYaqZ_1</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1507795241</pqid></control><display><type>article</type><title>Molecular characterization and serological reactivity of a vacuolar ATP synthase subunit ε-like protein from Clonorchis sinensis</title><source>MEDLINE</source><source>SpringerLink Journals - AutoHoldings</source><creator>Lv, Xiaoli ; Huang, Lisi ; Chen, Wenjun ; Wang, Xiaoyun ; Huang, Yan ; Deng, Chuanhuan ; Sun, Jiufeng ; Tian, Yanli ; Mao, Qiang ; Lei, Huali ; Yu, Xinbing</creator><creatorcontrib>Lv, Xiaoli ; Huang, Lisi ; Chen, Wenjun ; Wang, Xiaoyun ; Huang, Yan ; Deng, Chuanhuan ; Sun, Jiufeng ; Tian, Yanli ; Mao, Qiang ; Lei, Huali ; Yu, Xinbing</creatorcontrib><description>The vacuolar ATPase enzyme complex (V-ATPase) pumps protons across membranes, energized by hydrolysis of ATP. Extensive investigations on structural and biochemical features of these molecules have implied their importance in the physiological process. In this study, a full-length sequence encoding a vacuolar ATP synthase subunit ε-like protein of
Clonorchis sinensis
(
Cs
ATP-ε) was isolated from our cDNA library. The hypothetical 226 amino acid sequence shared 76 % identity with ATP-ε proteins of
Schistosoma japonicum
and above 55 % identity with ATP-ε proteins from human and other eukaryotes. Characteristic Asp
140
amino acid residues and seven B-cell epitopes were predicted in this sequence. The complete coding sequence of the gene was expressed in
Escherichia coli
. Recombinant
Cs
ATP-ε (r
Cs
ATP-ε) protein could be probed by anti-r
Cs
ATP-ε rat serum and
C.sinensis
-infected human serum in Western blotting experiment, indicating that it is an antigen of strong antigenicity. The high level of antibody titers (1:204,800) showed that
Cs
ATP-ε has a powerful immunogenicity. Both the increased level and the change trend of IgG1/IgG2a subtypes in serum showed that the r
Cs
ATP-ε can induce strong combined Th1/Th2 immune responses in rats and stimulate the immune response changes to the dominant Th2 from Th1 along with long time infection. The results of immunoblot and immunolocalization demonstrated that
Cs
ATP-ε was consecutively expressed at various developmental stages of the parasite, which was supported by real-time PCR analysis. In immunohistochemistry,
Cs
ATP-ε was localized on the intestine, vitellarium, and testicle of an adult worm and excretory bladder of metacercaria, implying that
Cs
ATP-ε may relate to energy intake and metabolism. This fundamental study would contribute to further researches that are related to growth and development and immunomodulation of
C. sinensis
.</description><identifier>ISSN: 0932-0113</identifier><identifier>EISSN: 1432-1955</identifier><identifier>DOI: 10.1007/s00436-014-3799-7</identifier><identifier>PMID: 24535733</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Amino Acid Sequence ; Animals ; Antibodies, Helminth - blood ; Biomedical and Life Sciences ; Biomedicine ; Cloning, Molecular ; Clonorchis sinensis ; Clonorchis sinensis - enzymology ; Clonorchis sinensis - genetics ; Clonorchis sinensis - immunology ; Epitopes, B-Lymphocyte - immunology ; Escherichia coli ; Ethenoadenosine Triphosphate - immunology ; Humans ; Immunity, Cellular ; Immunoglobulin G - blood ; Immunology ; Medical Microbiology ; Microbiology ; Molecular Sequence Data ; Original Paper ; Rats ; Rats, Sprague-Dawley ; Recombinant Proteins - genetics ; Recombinant Proteins - immunology ; Schistosoma japonicum ; Vacuolar Proton-Translocating ATPases - immunology</subject><ispartof>Parasitology research (1987), 2014-04, Vol.113 (4), p.1545-1554</ispartof><rights>Springer-Verlag Berlin Heidelberg 2014</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c377t-8d7880d4caba07d73a9cba44461d1a494f6213f7bc94afd25882bd65d2fd45e03</citedby><cites>FETCH-LOGICAL-c377t-8d7880d4caba07d73a9cba44461d1a494f6213f7bc94afd25882bd65d2fd45e03</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/s00436-014-3799-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00436-014-3799-7$$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/24535733$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lv, Xiaoli</creatorcontrib><creatorcontrib>Huang, Lisi</creatorcontrib><creatorcontrib>Chen, Wenjun</creatorcontrib><creatorcontrib>Wang, Xiaoyun</creatorcontrib><creatorcontrib>Huang, Yan</creatorcontrib><creatorcontrib>Deng, Chuanhuan</creatorcontrib><creatorcontrib>Sun, Jiufeng</creatorcontrib><creatorcontrib>Tian, Yanli</creatorcontrib><creatorcontrib>Mao, Qiang</creatorcontrib><creatorcontrib>Lei, Huali</creatorcontrib><creatorcontrib>Yu, Xinbing</creatorcontrib><title>Molecular characterization and serological reactivity of a vacuolar ATP synthase subunit ε-like protein from Clonorchis sinensis</title><title>Parasitology research (1987)</title><addtitle>Parasitol Res</addtitle><addtitle>Parasitol Res</addtitle><description>The vacuolar ATPase enzyme complex (V-ATPase) pumps protons across membranes, energized by hydrolysis of ATP. Extensive investigations on structural and biochemical features of these molecules have implied their importance in the physiological process. In this study, a full-length sequence encoding a vacuolar ATP synthase subunit ε-like protein of
Clonorchis sinensis
(
Cs
ATP-ε) was isolated from our cDNA library. The hypothetical 226 amino acid sequence shared 76 % identity with ATP-ε proteins of
Schistosoma japonicum
and above 55 % identity with ATP-ε proteins from human and other eukaryotes. Characteristic Asp
140
amino acid residues and seven B-cell epitopes were predicted in this sequence. The complete coding sequence of the gene was expressed in
Escherichia coli
. Recombinant
Cs
ATP-ε (r
Cs
ATP-ε) protein could be probed by anti-r
Cs
ATP-ε rat serum and
C.sinensis
-infected human serum in Western blotting experiment, indicating that it is an antigen of strong antigenicity. The high level of antibody titers (1:204,800) showed that
Cs
ATP-ε has a powerful immunogenicity. Both the increased level and the change trend of IgG1/IgG2a subtypes in serum showed that the r
Cs
ATP-ε can induce strong combined Th1/Th2 immune responses in rats and stimulate the immune response changes to the dominant Th2 from Th1 along with long time infection. The results of immunoblot and immunolocalization demonstrated that
Cs
ATP-ε was consecutively expressed at various developmental stages of the parasite, which was supported by real-time PCR analysis. In immunohistochemistry,
Cs
ATP-ε was localized on the intestine, vitellarium, and testicle of an adult worm and excretory bladder of metacercaria, implying that
Cs
ATP-ε may relate to energy intake and metabolism. This fundamental study would contribute to further researches that are related to growth and development and immunomodulation of
C. sinensis
.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies, Helminth - blood</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cloning, Molecular</subject><subject>Clonorchis sinensis</subject><subject>Clonorchis sinensis - enzymology</subject><subject>Clonorchis sinensis - genetics</subject><subject>Clonorchis sinensis - immunology</subject><subject>Epitopes, B-Lymphocyte - immunology</subject><subject>Escherichia coli</subject><subject>Ethenoadenosine Triphosphate - immunology</subject><subject>Humans</subject><subject>Immunity, Cellular</subject><subject>Immunoglobulin G - blood</subject><subject>Immunology</subject><subject>Medical Microbiology</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Original Paper</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - immunology</subject><subject>Schistosoma japonicum</subject><subject>Vacuolar Proton-Translocating ATPases - immunology</subject><issn>0932-0113</issn><issn>1432-1955</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc2OFCEURonROO3oA7gxLN2UQgFFsZx0_EvG6GJck1tATTPSMHKrJml3PpSv4TNJp0eXxtUluef7csMh5Dlnrzhj-jUyJsXQMS47oY3p9AOy4VL0HTdKPSQbZtqbcS7OyBPEG8a4HqR8TM56qYTSQmzIj48lBbcmqNTtoIJbQo3fYYklU8ieYqgllevoINEa2jrexeVAy0yB3oFbyzF5cfWZ4iEvO8BAcZ3WHBf662eX4tdAb2tZQsx0rmVPt6nkUt0uIsWYQ8aIT8mjGRKGZ_fznHx5--Zq-767_PTuw_bisnNC66UbvR5H5qWDCZj2WoBxE0gpB-45SCPnoedi1pMzEmbfq3HsJz8o389eqsDEOXl56m0HfVsDLnYf0YWUIIeyouVaiVZm-H-gimltVC95Q_kJdbUg1jDb2xr3UA-WM3uUZE-SbJNkj5KsbpkX9_XrtA_-b-KPlQb0JwDbKl-Ham_KWnP7nX-0_gYaqZ_1</recordid><startdate>20140401</startdate><enddate>20140401</enddate><creator>Lv, Xiaoli</creator><creator>Huang, Lisi</creator><creator>Chen, Wenjun</creator><creator>Wang, Xiaoyun</creator><creator>Huang, Yan</creator><creator>Deng, Chuanhuan</creator><creator>Sun, Jiufeng</creator><creator>Tian, Yanli</creator><creator>Mao, Qiang</creator><creator>Lei, Huali</creator><creator>Yu, Xinbing</creator><general>Springer Berlin Heidelberg</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>7X8</scope><scope>M7N</scope></search><sort><creationdate>20140401</creationdate><title>Molecular characterization and serological reactivity of a vacuolar ATP synthase subunit ε-like protein from Clonorchis sinensis</title><author>Lv, Xiaoli ; Huang, Lisi ; Chen, Wenjun ; Wang, Xiaoyun ; Huang, Yan ; Deng, Chuanhuan ; Sun, Jiufeng ; Tian, Yanli ; Mao, Qiang ; Lei, Huali ; Yu, Xinbing</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c377t-8d7880d4caba07d73a9cba44461d1a494f6213f7bc94afd25882bd65d2fd45e03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies, Helminth - blood</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Cloning, Molecular</topic><topic>Clonorchis sinensis</topic><topic>Clonorchis sinensis - enzymology</topic><topic>Clonorchis sinensis - genetics</topic><topic>Clonorchis sinensis - immunology</topic><topic>Epitopes, B-Lymphocyte - immunology</topic><topic>Escherichia coli</topic><topic>Ethenoadenosine Triphosphate - immunology</topic><topic>Humans</topic><topic>Immunity, Cellular</topic><topic>Immunoglobulin G - blood</topic><topic>Immunology</topic><topic>Medical Microbiology</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Original Paper</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - immunology</topic><topic>Schistosoma japonicum</topic><topic>Vacuolar Proton-Translocating ATPases - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lv, Xiaoli</creatorcontrib><creatorcontrib>Huang, Lisi</creatorcontrib><creatorcontrib>Chen, Wenjun</creatorcontrib><creatorcontrib>Wang, Xiaoyun</creatorcontrib><creatorcontrib>Huang, Yan</creatorcontrib><creatorcontrib>Deng, Chuanhuan</creatorcontrib><creatorcontrib>Sun, Jiufeng</creatorcontrib><creatorcontrib>Tian, Yanli</creatorcontrib><creatorcontrib>Mao, Qiang</creatorcontrib><creatorcontrib>Lei, Huali</creatorcontrib><creatorcontrib>Yu, Xinbing</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>Parasitology research (1987)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lv, Xiaoli</au><au>Huang, Lisi</au><au>Chen, Wenjun</au><au>Wang, Xiaoyun</au><au>Huang, Yan</au><au>Deng, Chuanhuan</au><au>Sun, Jiufeng</au><au>Tian, Yanli</au><au>Mao, Qiang</au><au>Lei, Huali</au><au>Yu, Xinbing</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular characterization and serological reactivity of a vacuolar ATP synthase subunit ε-like protein from Clonorchis sinensis</atitle><jtitle>Parasitology research (1987)</jtitle><stitle>Parasitol Res</stitle><addtitle>Parasitol Res</addtitle><date>2014-04-01</date><risdate>2014</risdate><volume>113</volume><issue>4</issue><spage>1545</spage><epage>1554</epage><pages>1545-1554</pages><issn>0932-0113</issn><eissn>1432-1955</eissn><abstract>The vacuolar ATPase enzyme complex (V-ATPase) pumps protons across membranes, energized by hydrolysis of ATP. Extensive investigations on structural and biochemical features of these molecules have implied their importance in the physiological process. In this study, a full-length sequence encoding a vacuolar ATP synthase subunit ε-like protein of
Clonorchis sinensis
(
Cs
ATP-ε) was isolated from our cDNA library. The hypothetical 226 amino acid sequence shared 76 % identity with ATP-ε proteins of
Schistosoma japonicum
and above 55 % identity with ATP-ε proteins from human and other eukaryotes. Characteristic Asp
140
amino acid residues and seven B-cell epitopes were predicted in this sequence. The complete coding sequence of the gene was expressed in
Escherichia coli
. Recombinant
Cs
ATP-ε (r
Cs
ATP-ε) protein could be probed by anti-r
Cs
ATP-ε rat serum and
C.sinensis
-infected human serum in Western blotting experiment, indicating that it is an antigen of strong antigenicity. The high level of antibody titers (1:204,800) showed that
Cs
ATP-ε has a powerful immunogenicity. Both the increased level and the change trend of IgG1/IgG2a subtypes in serum showed that the r
Cs
ATP-ε can induce strong combined Th1/Th2 immune responses in rats and stimulate the immune response changes to the dominant Th2 from Th1 along with long time infection. The results of immunoblot and immunolocalization demonstrated that
Cs
ATP-ε was consecutively expressed at various developmental stages of the parasite, which was supported by real-time PCR analysis. In immunohistochemistry,
Cs
ATP-ε was localized on the intestine, vitellarium, and testicle of an adult worm and excretory bladder of metacercaria, implying that
Cs
ATP-ε may relate to energy intake and metabolism. This fundamental study would contribute to further researches that are related to growth and development and immunomodulation of
C. sinensis
.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>24535733</pmid><doi>10.1007/s00436-014-3799-7</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0932-0113 |
| ispartof | Parasitology research (1987), 2014-04, Vol.113 (4), p.1545-1554 |
| issn | 0932-0113 1432-1955 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1753461910 |
| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Amino Acid Sequence Animals Antibodies, Helminth - blood Biomedical and Life Sciences Biomedicine Cloning, Molecular Clonorchis sinensis Clonorchis sinensis - enzymology Clonorchis sinensis - genetics Clonorchis sinensis - immunology Epitopes, B-Lymphocyte - immunology Escherichia coli Ethenoadenosine Triphosphate - immunology Humans Immunity, Cellular Immunoglobulin G - blood Immunology Medical Microbiology Microbiology Molecular Sequence Data Original Paper Rats Rats, Sprague-Dawley Recombinant Proteins - genetics Recombinant Proteins - immunology Schistosoma japonicum Vacuolar Proton-Translocating ATPases - immunology |
| title | Molecular characterization and serological reactivity of a vacuolar ATP synthase subunit ε-like protein from Clonorchis sinensis |
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