Trans-sialidase and mucins of Trypanosoma cruzi: an important interplay for the parasite
A dense glycocalix covers the surface of Trypanosoma cruzi, the agent of Chagas disease. Sialic acid in the surface of the parasite plays an important role in the infectious process, however, T. cruzi is unable to synthesize sialic acid or the usual donor CMP-sialic acid. Instead, T. cruzi expresses...
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| Veröffentlicht in: | Carbohydrate research 2011-09, Vol.346 (12), p.1389-1393 |
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| creator | Eugenia Giorgi, M. de Lederkremer, Rosa M. |
| description | A dense glycocalix covers the surface of Trypanosoma cruzi, the agent of Chagas disease. Sialic acid in the surface of the parasite plays an important role in the infectious process, however, T. cruzi is unable to synthesize sialic acid or the usual donor CMP-sialic acid. Instead, T. cruzi expresses a unique enzyme, the trans-sialidase (TcTS) involved in the transfer of sialic acid from host glycoconjugates to mucins of the parasite. The mucins are the major glycoproteins in the insect stage epimastigotes and in the infective trypomastigotes. Both, the mucins and the TcTS are anchored to the plasma membrane by a glycosylphosphatidylinositol anchor. Thus, TcTS may be shed into the bloodstream of the mammal host by the action of a parasite phosphatidylinositol-phospholipase C, affecting the immune system. The composition and structure of the sugars in the parasite mucins is characteristic of each differentiation stage, also, interstrain variations were described for epimastigote mucins. This review focus on the characteristics of the interplay between the trans-sialidase and the mucins of T. cruzi and summarizes the known carbohydrate structures of the mucins. |
| doi_str_mv | 10.1016/j.carres.2011.04.006 |
| format | Article |
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Sialic acid in the surface of the parasite plays an important role in the infectious process, however, T. cruzi is unable to synthesize sialic acid or the usual donor CMP-sialic acid. Instead, T. cruzi expresses a unique enzyme, the trans-sialidase (TcTS) involved in the transfer of sialic acid from host glycoconjugates to mucins of the parasite. The mucins are the major glycoproteins in the insect stage epimastigotes and in the infective trypomastigotes. Both, the mucins and the TcTS are anchored to the plasma membrane by a glycosylphosphatidylinositol anchor. Thus, TcTS may be shed into the bloodstream of the mammal host by the action of a parasite phosphatidylinositol-phospholipase C, affecting the immune system. The composition and structure of the sugars in the parasite mucins is characteristic of each differentiation stage, also, interstrain variations were described for epimastigote mucins. This review focus on the characteristics of the interplay between the trans-sialidase and the mucins of T. cruzi and summarizes the known carbohydrate structures of the mucins.</description><identifier>ISSN: 0008-6215</identifier><identifier>EISSN: 1873-426X</identifier><identifier>DOI: 10.1016/j.carres.2011.04.006</identifier><identifier>PMID: 21645882</identifier><language>eng</language><publisher>Netherlands: Elsevier Ltd</publisher><subject>Animals ; blood flow ; Carbohydrate Sequence ; Chagas disease ; Chagas Disease - metabolism ; Chagas Disease - parasitology ; Enzyme Inhibitors - chemical synthesis ; Enzyme Inhibitors - pharmacology ; Enzyme Inhibitors - therapeutic use ; epimastigotes ; Glycoconjugates - chemistry ; Glycoconjugates - metabolism ; Glycoproteins - antagonists & inhibitors ; Glycoproteins - metabolism ; Glycosylphosphatidylinositols - metabolism ; Humans ; immune system ; insects ; Life Cycle Stages ; mammals ; Molecular Sequence Data ; Mucins ; Mucins - chemistry ; Mucins - metabolism ; Neuraminidase - antagonists & inhibitors ; Neuraminidase - metabolism ; parasites ; plasma membrane ; Protein Binding ; sialic acids ; Sialic Acids - metabolism ; Species Specificity ; Trans-sialidase ; Trypanosoma cruzi ; Trypanosoma cruzi - enzymology ; trypomastigotes ; Type C Phospholipases - metabolism</subject><ispartof>Carbohydrate research, 2011-09, Vol.346 (12), p.1389-1393</ispartof><rights>2011 Elsevier Ltd</rights><rights>Copyright © 2011 Elsevier Ltd. 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Sialic acid in the surface of the parasite plays an important role in the infectious process, however, T. cruzi is unable to synthesize sialic acid or the usual donor CMP-sialic acid. Instead, T. cruzi expresses a unique enzyme, the trans-sialidase (TcTS) involved in the transfer of sialic acid from host glycoconjugates to mucins of the parasite. The mucins are the major glycoproteins in the insect stage epimastigotes and in the infective trypomastigotes. Both, the mucins and the TcTS are anchored to the plasma membrane by a glycosylphosphatidylinositol anchor. Thus, TcTS may be shed into the bloodstream of the mammal host by the action of a parasite phosphatidylinositol-phospholipase C, affecting the immune system. The composition and structure of the sugars in the parasite mucins is characteristic of each differentiation stage, also, interstrain variations were described for epimastigote mucins. This review focus on the characteristics of the interplay between the trans-sialidase and the mucins of T. cruzi and summarizes the known carbohydrate structures of the mucins.</description><subject>Animals</subject><subject>blood flow</subject><subject>Carbohydrate Sequence</subject><subject>Chagas disease</subject><subject>Chagas Disease - metabolism</subject><subject>Chagas Disease - parasitology</subject><subject>Enzyme Inhibitors - chemical synthesis</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzyme Inhibitors - therapeutic use</subject><subject>epimastigotes</subject><subject>Glycoconjugates - chemistry</subject><subject>Glycoconjugates - metabolism</subject><subject>Glycoproteins - antagonists & inhibitors</subject><subject>Glycoproteins - metabolism</subject><subject>Glycosylphosphatidylinositols - metabolism</subject><subject>Humans</subject><subject>immune system</subject><subject>insects</subject><subject>Life Cycle Stages</subject><subject>mammals</subject><subject>Molecular Sequence Data</subject><subject>Mucins</subject><subject>Mucins - chemistry</subject><subject>Mucins - metabolism</subject><subject>Neuraminidase - antagonists & inhibitors</subject><subject>Neuraminidase - metabolism</subject><subject>parasites</subject><subject>plasma membrane</subject><subject>Protein Binding</subject><subject>sialic acids</subject><subject>Sialic Acids - metabolism</subject><subject>Species Specificity</subject><subject>Trans-sialidase</subject><subject>Trypanosoma cruzi</subject><subject>Trypanosoma cruzi - enzymology</subject><subject>trypomastigotes</subject><subject>Type C Phospholipases - metabolism</subject><issn>0008-6215</issn><issn>1873-426X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1v1DAQhi1URLeFf4CKb5wS_LWOw6FSVUFBqsSBrdSbNeuMqVdJHOwEafn1eJXCkdNopOd9Z_QQ8pazmjOuPxxqBylhrgXjvGaqZky_IBtuGlkpoR_PyIYxZiot-PacXOR8KCvTjX5FzgXXamuM2JDHXYIxVzlAHzrISGHs6LC4MGYaPd2l4wRjzHEA6tLyO3wsAA3DFNMM40zDOGOaejhSHxOdn5BOkCCHGV-Tlx76jG-e5yV5-Pxpd_uluv929_X25r5ySvK5Au292PJOCu-NkA1D13bYNSh1w5xhwiN4VNIp7oTZt_tWSykNNg5RmQbkJXm_9k4p_lwwz3YI2WHfw4hxydY0yrRNy1kh1Uq6FHNO6O2UwgDpaDmzJ6X2YFel9qTUMmWLrxK7ej6w7Afs_oX-OizAuxXwEC38SCHbh--lQZ98My5kIa5XAouIXwGTzS7g6LALCd1suxj-_8MffqmUCA</recordid><startdate>20110906</startdate><enddate>20110906</enddate><creator>Eugenia Giorgi, M.</creator><creator>de Lederkremer, Rosa M.</creator><general>Elsevier Ltd</general><scope>FBQ</scope><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></search><sort><creationdate>20110906</creationdate><title>Trans-sialidase and mucins of Trypanosoma cruzi: an important interplay for the parasite</title><author>Eugenia Giorgi, M. ; de Lederkremer, Rosa M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c431t-a6ff251d32ff82370ec9ded7e3670c802feafe43c41c28b9b963338e7cee487a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animals</topic><topic>blood flow</topic><topic>Carbohydrate Sequence</topic><topic>Chagas disease</topic><topic>Chagas Disease - metabolism</topic><topic>Chagas Disease - parasitology</topic><topic>Enzyme Inhibitors - chemical synthesis</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Enzyme Inhibitors - therapeutic use</topic><topic>epimastigotes</topic><topic>Glycoconjugates - chemistry</topic><topic>Glycoconjugates - metabolism</topic><topic>Glycoproteins - antagonists & inhibitors</topic><topic>Glycoproteins - metabolism</topic><topic>Glycosylphosphatidylinositols - metabolism</topic><topic>Humans</topic><topic>immune system</topic><topic>insects</topic><topic>Life Cycle Stages</topic><topic>mammals</topic><topic>Molecular Sequence Data</topic><topic>Mucins</topic><topic>Mucins - chemistry</topic><topic>Mucins - metabolism</topic><topic>Neuraminidase - antagonists & inhibitors</topic><topic>Neuraminidase - metabolism</topic><topic>parasites</topic><topic>plasma membrane</topic><topic>Protein Binding</topic><topic>sialic acids</topic><topic>Sialic Acids - metabolism</topic><topic>Species Specificity</topic><topic>Trans-sialidase</topic><topic>Trypanosoma cruzi</topic><topic>Trypanosoma cruzi - enzymology</topic><topic>trypomastigotes</topic><topic>Type C Phospholipases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Eugenia Giorgi, M.</creatorcontrib><creatorcontrib>de Lederkremer, Rosa M.</creatorcontrib><collection>AGRIS</collection><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><jtitle>Carbohydrate research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Eugenia Giorgi, M.</au><au>de Lederkremer, Rosa M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Trans-sialidase and mucins of Trypanosoma cruzi: an important interplay for the parasite</atitle><jtitle>Carbohydrate research</jtitle><addtitle>Carbohydr Res</addtitle><date>2011-09-06</date><risdate>2011</risdate><volume>346</volume><issue>12</issue><spage>1389</spage><epage>1393</epage><pages>1389-1393</pages><issn>0008-6215</issn><eissn>1873-426X</eissn><abstract>A dense glycocalix covers the surface of Trypanosoma cruzi, the agent of Chagas disease. Sialic acid in the surface of the parasite plays an important role in the infectious process, however, T. cruzi is unable to synthesize sialic acid or the usual donor CMP-sialic acid. Instead, T. cruzi expresses a unique enzyme, the trans-sialidase (TcTS) involved in the transfer of sialic acid from host glycoconjugates to mucins of the parasite. The mucins are the major glycoproteins in the insect stage epimastigotes and in the infective trypomastigotes. Both, the mucins and the TcTS are anchored to the plasma membrane by a glycosylphosphatidylinositol anchor. Thus, TcTS may be shed into the bloodstream of the mammal host by the action of a parasite phosphatidylinositol-phospholipase C, affecting the immune system. The composition and structure of the sugars in the parasite mucins is characteristic of each differentiation stage, also, interstrain variations were described for epimastigote mucins. 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| subjects | Animals blood flow Carbohydrate Sequence Chagas disease Chagas Disease - metabolism Chagas Disease - parasitology Enzyme Inhibitors - chemical synthesis Enzyme Inhibitors - pharmacology Enzyme Inhibitors - therapeutic use epimastigotes Glycoconjugates - chemistry Glycoconjugates - metabolism Glycoproteins - antagonists & inhibitors Glycoproteins - metabolism Glycosylphosphatidylinositols - metabolism Humans immune system insects Life Cycle Stages mammals Molecular Sequence Data Mucins Mucins - chemistry Mucins - metabolism Neuraminidase - antagonists & inhibitors Neuraminidase - metabolism parasites plasma membrane Protein Binding sialic acids Sialic Acids - metabolism Species Specificity Trans-sialidase Trypanosoma cruzi Trypanosoma cruzi - enzymology trypomastigotes Type C Phospholipases - metabolism |
| title | Trans-sialidase and mucins of Trypanosoma cruzi: an important interplay for the parasite |
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