Echinococcus multilocularis metacestodes : Immunological and immunocytochemical analysis of the relationships between alkaline phosphatase and the Em2 antigen
Echinococcus multilocularis metacestodes possess an alkaline phosphatase (EmAP) which has been extensively characterized at the biochemical level in previous studies. The apparent molecular weight of the enzyme monomer and its isoelectric point matched those originally described for the Em2 antigen,...
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| Veröffentlicht in: | Experimental parasitology 1997-10, Vol.87 (2), p.142-149 |
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| creator | LAWTON, P HEMPHILL, A DEPLAZES, P GOTTSTEIN, B SARCIRON, M.-E |
| description | Echinococcus multilocularis metacestodes possess an alkaline phosphatase (EmAP) which has been extensively characterized at the biochemical level in previous studies. The apparent molecular weight of the enzyme monomer and its isoelectric point matched those originally described for the Em2 antigen, a reference antigen currently used for the immunodiagnosis of E. multilocularis infection. These observations raised questions about the molecular relationship between the two molecules. In order to investigate the relations between EmAP and the Em2 antigen, immunoblotting and ELISA were carried out using polyclonal and monoclonal antibodies directed against EmAP and the Em2 antigen, respectively. In addition, the localization of EmAP and the Em2 antigen was compared by immunofluorescence and immunogold electron microscopy in in vitro-generated E. multilocularis metacestodes. The results show that common epitopes between EmAP and Em2 exist, which are predominantly of a peptidic nature. Both antigens are localized in an acellular parasite structure, the laminated layer, with additional locations for the EmAP on the glycocalyx and in the central region of invaginated protoscoleces. These results suggest a putative functional relationship between the two antigens and that Em2 could originate from EmAP. |
| doi_str_mv | 10.1006/expr.1997.4190 |
| format | Article |
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The apparent molecular weight of the enzyme monomer and its isoelectric point matched those originally described for the Em2 antigen, a reference antigen currently used for the immunodiagnosis of E. multilocularis infection. These observations raised questions about the molecular relationship between the two molecules. In order to investigate the relations between EmAP and the Em2 antigen, immunoblotting and ELISA were carried out using polyclonal and monoclonal antibodies directed against EmAP and the Em2 antigen, respectively. In addition, the localization of EmAP and the Em2 antigen was compared by immunofluorescence and immunogold electron microscopy in in vitro-generated E. multilocularis metacestodes. The results show that common epitopes between EmAP and Em2 exist, which are predominantly of a peptidic nature. Both antigens are localized in an acellular parasite structure, the laminated layer, with additional locations for the EmAP on the glycocalyx and in the central region of invaginated protoscoleces. These results suggest a putative functional relationship between the two antigens and that Em2 could originate from EmAP.</description><identifier>ISSN: 0014-4894</identifier><identifier>EISSN: 1090-2449</identifier><identifier>DOI: 10.1006/expr.1997.4190</identifier><identifier>PMID: 9326889</identifier><identifier>CODEN: EXPAAA</identifier><language>eng</language><publisher>San Diego, CA: Elsevier</publisher><subject>Alkaline Phosphatase - analysis ; Alkaline Phosphatase - immunology ; Animals ; Antibodies, Monoclonal - immunology ; Antigens, Helminth - analysis ; Antigens, Helminth - immunology ; Biochemistry. Physiology. Immunology. Molecular biology ; Biological and medical sciences ; Echinococcus - enzymology ; Echinococcus - immunology ; Echinococcus - ultrastructure ; Enzyme-Linked Immunosorbent Assay ; Epitopes - immunology ; Fluorescent Antibody Technique ; Fundamental and applied biological sciences. Psychology ; Gerbillinae ; Humans ; Immunoblotting ; Immunohistochemistry ; Immunology ; Invertebrates ; Life Sciences ; Microbiology and Parasitology ; Microscopy, Immunoelectron ; Nemathelminthia. Plathelmintha ; Parasitology ; Physiology. Development</subject><ispartof>Experimental parasitology, 1997-10, Vol.87 (2), p.142-149</ispartof><rights>1998 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><orcidid>0000-0002-0622-2128 ; 0000-0003-0782-3723 ; 0000-0003-1661-8705</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2058097$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9326889$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://univ-lyon1.hal.science/hal-02110824$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>LAWTON, P</creatorcontrib><creatorcontrib>HEMPHILL, A</creatorcontrib><creatorcontrib>DEPLAZES, P</creatorcontrib><creatorcontrib>GOTTSTEIN, B</creatorcontrib><creatorcontrib>SARCIRON, M.-E</creatorcontrib><title>Echinococcus multilocularis metacestodes : Immunological and immunocytochemical analysis of the relationships between alkaline phosphatase and the Em2 antigen</title><title>Experimental parasitology</title><addtitle>Exp Parasitol</addtitle><description>Echinococcus multilocularis metacestodes possess an alkaline phosphatase (EmAP) which has been extensively characterized at the biochemical level in previous studies. The apparent molecular weight of the enzyme monomer and its isoelectric point matched those originally described for the Em2 antigen, a reference antigen currently used for the immunodiagnosis of E. multilocularis infection. These observations raised questions about the molecular relationship between the two molecules. In order to investigate the relations between EmAP and the Em2 antigen, immunoblotting and ELISA were carried out using polyclonal and monoclonal antibodies directed against EmAP and the Em2 antigen, respectively. In addition, the localization of EmAP and the Em2 antigen was compared by immunofluorescence and immunogold electron microscopy in in vitro-generated E. multilocularis metacestodes. The results show that common epitopes between EmAP and Em2 exist, which are predominantly of a peptidic nature. Both antigens are localized in an acellular parasite structure, the laminated layer, with additional locations for the EmAP on the glycocalyx and in the central region of invaginated protoscoleces. These results suggest a putative functional relationship between the two antigens and that Em2 could originate from EmAP.</description><subject>Alkaline Phosphatase - analysis</subject><subject>Alkaline Phosphatase - immunology</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antigens, Helminth - analysis</subject><subject>Antigens, Helminth - immunology</subject><subject>Biochemistry. Physiology. Immunology. Molecular biology</subject><subject>Biological and medical sciences</subject><subject>Echinococcus - enzymology</subject><subject>Echinococcus - immunology</subject><subject>Echinococcus - ultrastructure</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Epitopes - immunology</subject><subject>Fluorescent Antibody Technique</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gerbillinae</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Immunohistochemistry</subject><subject>Immunology</subject><subject>Invertebrates</subject><subject>Life Sciences</subject><subject>Microbiology and Parasitology</subject><subject>Microscopy, Immunoelectron</subject><subject>Nemathelminthia. Plathelmintha</subject><subject>Parasitology</subject><subject>Physiology. Development</subject><issn>0014-4894</issn><issn>1090-2449</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kEFv1DAQhS0EKkvhyg3JB4TUQ5ax493Y3KpqSyutxAXO0cQZNwYnDrFT2D_DbyVto55m5r1v3uEx9l7AVgDsP9PfcdoKY6qtEgZesI0AA4VUyrxkGwChCqWNes3epPQTALSQ6oydmVLutTYb9u9gOz9EG62dE-_nkH2Idg44-eWkjJZSji0l_oXf9v08xBDvvMXAcWi5f1TsKUfbUb_KGE5peY6O5474RAGzj0Pq_Jh4Q_kP0cAx_MLgB-JjF9PYYcZEj4kPL4deLnv2dzS8Za8chkTv1nnOflwfvl_dFMdvX2-vLo9FJ_cmF3tHrtForKFSIKpKaI2IYIywTjmnSq1g5yQ5qipUu7ZqQGNVyrZBKxoqz9nFU26HoR4n3-N0qiP6-ubyWD9oIIUALdW9WNhPT-w4xd_zUk_d-2QpBBwozqmuTAlG7tQCfljBuempfc5dy1_8j6uPaanOTThYn54xCTsNpir_A2ZgmDM</recordid><startdate>19971001</startdate><enddate>19971001</enddate><creator>LAWTON, P</creator><creator>HEMPHILL, A</creator><creator>DEPLAZES, P</creator><creator>GOTTSTEIN, B</creator><creator>SARCIRON, M.-E</creator><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>1XC</scope><scope>VOOES</scope><orcidid>https://orcid.org/0000-0002-0622-2128</orcidid><orcidid>https://orcid.org/0000-0003-0782-3723</orcidid><orcidid>https://orcid.org/0000-0003-1661-8705</orcidid></search><sort><creationdate>19971001</creationdate><title>Echinococcus multilocularis metacestodes : Immunological and immunocytochemical analysis of the relationships between alkaline phosphatase and the Em2 antigen</title><author>LAWTON, P ; HEMPHILL, A ; DEPLAZES, P ; GOTTSTEIN, B ; SARCIRON, M.-E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h269t-6fefb8a9c9e31aa47188aaa0991cf4ff438405f2efe77a45d7b08a732dbac1be3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Alkaline Phosphatase - analysis</topic><topic>Alkaline Phosphatase - immunology</topic><topic>Animals</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antigens, Helminth - analysis</topic><topic>Antigens, Helminth - immunology</topic><topic>Biochemistry. Physiology. Immunology. Molecular biology</topic><topic>Biological and medical sciences</topic><topic>Echinococcus - enzymology</topic><topic>Echinococcus - immunology</topic><topic>Echinococcus - ultrastructure</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Epitopes - immunology</topic><topic>Fluorescent Antibody Technique</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gerbillinae</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>Immunohistochemistry</topic><topic>Immunology</topic><topic>Invertebrates</topic><topic>Life Sciences</topic><topic>Microbiology and Parasitology</topic><topic>Microscopy, Immunoelectron</topic><topic>Nemathelminthia. Plathelmintha</topic><topic>Parasitology</topic><topic>Physiology. Development</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>LAWTON, P</creatorcontrib><creatorcontrib>HEMPHILL, A</creatorcontrib><creatorcontrib>DEPLAZES, P</creatorcontrib><creatorcontrib>GOTTSTEIN, B</creatorcontrib><creatorcontrib>SARCIRON, M.-E</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><jtitle>Experimental parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>LAWTON, P</au><au>HEMPHILL, A</au><au>DEPLAZES, P</au><au>GOTTSTEIN, B</au><au>SARCIRON, M.-E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Echinococcus multilocularis metacestodes : Immunological and immunocytochemical analysis of the relationships between alkaline phosphatase and the Em2 antigen</atitle><jtitle>Experimental parasitology</jtitle><addtitle>Exp Parasitol</addtitle><date>1997-10-01</date><risdate>1997</risdate><volume>87</volume><issue>2</issue><spage>142</spage><epage>149</epage><pages>142-149</pages><issn>0014-4894</issn><eissn>1090-2449</eissn><coden>EXPAAA</coden><abstract>Echinococcus multilocularis metacestodes possess an alkaline phosphatase (EmAP) which has been extensively characterized at the biochemical level in previous studies. The apparent molecular weight of the enzyme monomer and its isoelectric point matched those originally described for the Em2 antigen, a reference antigen currently used for the immunodiagnosis of E. multilocularis infection. These observations raised questions about the molecular relationship between the two molecules. In order to investigate the relations between EmAP and the Em2 antigen, immunoblotting and ELISA were carried out using polyclonal and monoclonal antibodies directed against EmAP and the Em2 antigen, respectively. In addition, the localization of EmAP and the Em2 antigen was compared by immunofluorescence and immunogold electron microscopy in in vitro-generated E. multilocularis metacestodes. The results show that common epitopes between EmAP and Em2 exist, which are predominantly of a peptidic nature. Both antigens are localized in an acellular parasite structure, the laminated layer, with additional locations for the EmAP on the glycocalyx and in the central region of invaginated protoscoleces. These results suggest a putative functional relationship between the two antigens and that Em2 could originate from EmAP.</abstract><cop>San Diego, CA</cop><pub>Elsevier</pub><pmid>9326889</pmid><doi>10.1006/expr.1997.4190</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-0622-2128</orcidid><orcidid>https://orcid.org/0000-0003-0782-3723</orcidid><orcidid>https://orcid.org/0000-0003-1661-8705</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Alkaline Phosphatase - analysis Alkaline Phosphatase - immunology Animals Antibodies, Monoclonal - immunology Antigens, Helminth - analysis Antigens, Helminth - immunology Biochemistry. Physiology. Immunology. Molecular biology Biological and medical sciences Echinococcus - enzymology Echinococcus - immunology Echinococcus - ultrastructure Enzyme-Linked Immunosorbent Assay Epitopes - immunology Fluorescent Antibody Technique Fundamental and applied biological sciences. Psychology Gerbillinae Humans Immunoblotting Immunohistochemistry Immunology Invertebrates Life Sciences Microbiology and Parasitology Microscopy, Immunoelectron Nemathelminthia. Plathelmintha Parasitology Physiology. Development |
| title | Echinococcus multilocularis metacestodes : Immunological and immunocytochemical analysis of the relationships between alkaline phosphatase and the Em2 antigen |
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