Identification and intra-specific variability analysis of secreted and membrane-bound proteins from Echinococcus granulosus
Echinococcus granulosus, the etiological agent of cystic hydatid disease, exists as a series of strains or genotypes, differing in biological features. Many of the secreted and membrane-bound proteins (S/M) from helminth parasites are involved in the host–parasite interplay and constitute potential...
Gespeichert in:
Veröffentlicht in: | Parasitology international 2006-01, Vol.55, p.S63-S67 |
---|---|
Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | S67 |
---|---|
container_issue | |
container_start_page | S63 |
container_title | Parasitology international |
container_volume | 55 |
creator | Rosenzvit, Mara C. Camicia, Federico Kamenetzky, Laura Muzulin, Patricia M. Gutierrez, Ariana M. |
description | Echinococcus granulosus, the etiological agent of cystic hydatid disease, exists as a series of strains or genotypes, differing in biological features. Many of the secreted and membrane-bound proteins (S/M) from helminth parasites are involved in the host–parasite interplay and constitute potential targets for diagnosis, anti-parasitic drugs and vaccines. A number of
E. granulosus S/M proteins were identified using the signal sequence trap technique. Six out of seven cDNA fragments of these newly identified proteins showed nucleotide and amino acid sequence variation. Inter-strain variation was reported for other characterized S/M proteins as the vaccine target EG95 and the major hydatid cyst fluid antigen, Antigen B (AgB). AgB is highly polymorphic, 101 different sequences related to AgB were reported so far and were grouped in 5 genes (
EgB1–
EgB5) and one pseudogene (
EgB2p) exclusive of G5, G6/G7 genotypes. The significance of AgB polymorphism and possible consequences in diagnostic performance are discussed. The diagnostic value of the new protein variants detected in
E. granulosus strains could be determined through standardized inter-laboratory studies as the recently done by the South American Network for Hydatid Serology. |
doi_str_mv | 10.1016/j.parint.2005.11.009 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67632611</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1383576905001121</els_id><sourcerecordid>17082469</sourcerecordid><originalsourceid>FETCH-LOGICAL-c510t-6df2a0127200eacd0a42e0cfdd7cd86c0d154327f9910e85316aa622da20c9463</originalsourceid><addsrcrecordid>eNqFkU9v1DAQxS0EoqXwDRDKiVvCjJ3YyQUJVQUqVeICZ8s7noBXSbzYSaUVXx4vuxI3OPnf770ZzxPiNUKDgPrdvjm4FJa1kQBdg9gADE_ENfZG1aDk8LTsVa_qzujhSrzIeQ-AnTH4XFyhVrqXGq_Fr3vPyxrGQG4Ncanc4qtimlydD0yn--qxlHG7MIX1WJ7ddMwhV3GsMlPilf0fzczzLrmF613cyvGQ4sphydWY4lzd0Y-wRIpEW66-F2ybYt7yS_FsdFPmV5f1Rnz7ePf19nP98OXT_e2Hh5o6hLXWfpQOUJryUXbkwbWSgUbvDfleE3jsWiXNOAwI3HcKtXNaSu8k0NBqdSPenn1LVz83zqudQyaeptJv3LLVRqsyDPwviAZ62eqhgO0ZpBRzTjzaQwqzS0eLYE_p2L09p2NP6VhEW9IpsjcX_203s_8rusRRgPdngMs4HgMnmynwQuxDYlqtj-HfFX4DlV6lfA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17082469</pqid></control><display><type>article</type><title>Identification and intra-specific variability analysis of secreted and membrane-bound proteins from Echinococcus granulosus</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>Rosenzvit, Mara C. ; Camicia, Federico ; Kamenetzky, Laura ; Muzulin, Patricia M. ; Gutierrez, Ariana M.</creator><creatorcontrib>Rosenzvit, Mara C. ; Camicia, Federico ; Kamenetzky, Laura ; Muzulin, Patricia M. ; Gutierrez, Ariana M.</creatorcontrib><description>Echinococcus granulosus, the etiological agent of cystic hydatid disease, exists as a series of strains or genotypes, differing in biological features. Many of the secreted and membrane-bound proteins (S/M) from helminth parasites are involved in the host–parasite interplay and constitute potential targets for diagnosis, anti-parasitic drugs and vaccines. A number of
E. granulosus S/M proteins were identified using the signal sequence trap technique. Six out of seven cDNA fragments of these newly identified proteins showed nucleotide and amino acid sequence variation. Inter-strain variation was reported for other characterized S/M proteins as the vaccine target EG95 and the major hydatid cyst fluid antigen, Antigen B (AgB). AgB is highly polymorphic, 101 different sequences related to AgB were reported so far and were grouped in 5 genes (
EgB1–
EgB5) and one pseudogene (
EgB2p) exclusive of G5, G6/G7 genotypes. The significance of AgB polymorphism and possible consequences in diagnostic performance are discussed. The diagnostic value of the new protein variants detected in
E. granulosus strains could be determined through standardized inter-laboratory studies as the recently done by the South American Network for Hydatid Serology.</description><identifier>ISSN: 1383-5769</identifier><identifier>EISSN: 1873-0329</identifier><identifier>DOI: 10.1016/j.parint.2005.11.009</identifier><identifier>PMID: 16368261</identifier><language>eng</language><publisher>Netherlands: Elsevier Ireland Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Antigen B ; Base Sequence ; Cell Membrane - metabolism ; Echinococcus granulosus ; Echinococcus granulosus - genetics ; Echinococcus granulosus - metabolism ; Genetic Variation ; Helminth Proteins - chemistry ; Helminth Proteins - genetics ; Helminth Proteins - metabolism ; Helminth Proteins - secretion ; Intra-specific variation ; Lipoproteins - chemistry ; Lipoproteins - genetics ; Lipoproteins - metabolism ; Lipoproteins - secretion ; Molecular Sequence Data ; Platyhelminth parasites ; Secreted and membrane-bound proteins</subject><ispartof>Parasitology international, 2006-01, Vol.55, p.S63-S67</ispartof><rights>2005 Elsevier Ireland Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c510t-6df2a0127200eacd0a42e0cfdd7cd86c0d154327f9910e85316aa622da20c9463</citedby><cites>FETCH-LOGICAL-c510t-6df2a0127200eacd0a42e0cfdd7cd86c0d154327f9910e85316aa622da20c9463</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.parint.2005.11.009$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,782,786,3552,27931,27932,46002</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16368261$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rosenzvit, Mara C.</creatorcontrib><creatorcontrib>Camicia, Federico</creatorcontrib><creatorcontrib>Kamenetzky, Laura</creatorcontrib><creatorcontrib>Muzulin, Patricia M.</creatorcontrib><creatorcontrib>Gutierrez, Ariana M.</creatorcontrib><title>Identification and intra-specific variability analysis of secreted and membrane-bound proteins from Echinococcus granulosus</title><title>Parasitology international</title><addtitle>Parasitol Int</addtitle><description>Echinococcus granulosus, the etiological agent of cystic hydatid disease, exists as a series of strains or genotypes, differing in biological features. Many of the secreted and membrane-bound proteins (S/M) from helminth parasites are involved in the host–parasite interplay and constitute potential targets for diagnosis, anti-parasitic drugs and vaccines. A number of
E. granulosus S/M proteins were identified using the signal sequence trap technique. Six out of seven cDNA fragments of these newly identified proteins showed nucleotide and amino acid sequence variation. Inter-strain variation was reported for other characterized S/M proteins as the vaccine target EG95 and the major hydatid cyst fluid antigen, Antigen B (AgB). AgB is highly polymorphic, 101 different sequences related to AgB were reported so far and were grouped in 5 genes (
EgB1–
EgB5) and one pseudogene (
EgB2p) exclusive of G5, G6/G7 genotypes. The significance of AgB polymorphism and possible consequences in diagnostic performance are discussed. The diagnostic value of the new protein variants detected in
E. granulosus strains could be determined through standardized inter-laboratory studies as the recently done by the South American Network for Hydatid Serology.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antigen B</subject><subject>Base Sequence</subject><subject>Cell Membrane - metabolism</subject><subject>Echinococcus granulosus</subject><subject>Echinococcus granulosus - genetics</subject><subject>Echinococcus granulosus - metabolism</subject><subject>Genetic Variation</subject><subject>Helminth Proteins - chemistry</subject><subject>Helminth Proteins - genetics</subject><subject>Helminth Proteins - metabolism</subject><subject>Helminth Proteins - secretion</subject><subject>Intra-specific variation</subject><subject>Lipoproteins - chemistry</subject><subject>Lipoproteins - genetics</subject><subject>Lipoproteins - metabolism</subject><subject>Lipoproteins - secretion</subject><subject>Molecular Sequence Data</subject><subject>Platyhelminth parasites</subject><subject>Secreted and membrane-bound proteins</subject><issn>1383-5769</issn><issn>1873-0329</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9v1DAQxS0EoqXwDRDKiVvCjJ3YyQUJVQUqVeICZ8s7noBXSbzYSaUVXx4vuxI3OPnf770ZzxPiNUKDgPrdvjm4FJa1kQBdg9gADE_ENfZG1aDk8LTsVa_qzujhSrzIeQ-AnTH4XFyhVrqXGq_Fr3vPyxrGQG4Ncanc4qtimlydD0yn--qxlHG7MIX1WJ7ddMwhV3GsMlPilf0fzczzLrmF613cyvGQ4sphydWY4lzd0Y-wRIpEW66-F2ybYt7yS_FsdFPmV5f1Rnz7ePf19nP98OXT_e2Hh5o6hLXWfpQOUJryUXbkwbWSgUbvDfleE3jsWiXNOAwI3HcKtXNaSu8k0NBqdSPenn1LVz83zqudQyaeptJv3LLVRqsyDPwviAZ62eqhgO0ZpBRzTjzaQwqzS0eLYE_p2L09p2NP6VhEW9IpsjcX_203s_8rusRRgPdngMs4HgMnmynwQuxDYlqtj-HfFX4DlV6lfA</recordid><startdate>20060101</startdate><enddate>20060101</enddate><creator>Rosenzvit, Mara C.</creator><creator>Camicia, Federico</creator><creator>Kamenetzky, Laura</creator><creator>Muzulin, Patricia M.</creator><creator>Gutierrez, Ariana M.</creator><general>Elsevier Ireland Ltd</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20060101</creationdate><title>Identification and intra-specific variability analysis of secreted and membrane-bound proteins from Echinococcus granulosus</title><author>Rosenzvit, Mara C. ; Camicia, Federico ; Kamenetzky, Laura ; Muzulin, Patricia M. ; Gutierrez, Ariana M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c510t-6df2a0127200eacd0a42e0cfdd7cd86c0d154327f9910e85316aa622da20c9463</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antigen B</topic><topic>Base Sequence</topic><topic>Cell Membrane - metabolism</topic><topic>Echinococcus granulosus</topic><topic>Echinococcus granulosus - genetics</topic><topic>Echinococcus granulosus - metabolism</topic><topic>Genetic Variation</topic><topic>Helminth Proteins - chemistry</topic><topic>Helminth Proteins - genetics</topic><topic>Helminth Proteins - metabolism</topic><topic>Helminth Proteins - secretion</topic><topic>Intra-specific variation</topic><topic>Lipoproteins - chemistry</topic><topic>Lipoproteins - genetics</topic><topic>Lipoproteins - metabolism</topic><topic>Lipoproteins - secretion</topic><topic>Molecular Sequence Data</topic><topic>Platyhelminth parasites</topic><topic>Secreted and membrane-bound proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rosenzvit, Mara C.</creatorcontrib><creatorcontrib>Camicia, Federico</creatorcontrib><creatorcontrib>Kamenetzky, Laura</creatorcontrib><creatorcontrib>Muzulin, Patricia M.</creatorcontrib><creatorcontrib>Gutierrez, Ariana M.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Parasitology international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rosenzvit, Mara C.</au><au>Camicia, Federico</au><au>Kamenetzky, Laura</au><au>Muzulin, Patricia M.</au><au>Gutierrez, Ariana M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and intra-specific variability analysis of secreted and membrane-bound proteins from Echinococcus granulosus</atitle><jtitle>Parasitology international</jtitle><addtitle>Parasitol Int</addtitle><date>2006-01-01</date><risdate>2006</risdate><volume>55</volume><spage>S63</spage><epage>S67</epage><pages>S63-S67</pages><issn>1383-5769</issn><eissn>1873-0329</eissn><abstract>Echinococcus granulosus, the etiological agent of cystic hydatid disease, exists as a series of strains or genotypes, differing in biological features. Many of the secreted and membrane-bound proteins (S/M) from helminth parasites are involved in the host–parasite interplay and constitute potential targets for diagnosis, anti-parasitic drugs and vaccines. A number of
E. granulosus S/M proteins were identified using the signal sequence trap technique. Six out of seven cDNA fragments of these newly identified proteins showed nucleotide and amino acid sequence variation. Inter-strain variation was reported for other characterized S/M proteins as the vaccine target EG95 and the major hydatid cyst fluid antigen, Antigen B (AgB). AgB is highly polymorphic, 101 different sequences related to AgB were reported so far and were grouped in 5 genes (
EgB1–
EgB5) and one pseudogene (
EgB2p) exclusive of G5, G6/G7 genotypes. The significance of AgB polymorphism and possible consequences in diagnostic performance are discussed. The diagnostic value of the new protein variants detected in
E. granulosus strains could be determined through standardized inter-laboratory studies as the recently done by the South American Network for Hydatid Serology.</abstract><cop>Netherlands</cop><pub>Elsevier Ireland Ltd</pub><pmid>16368261</pmid><doi>10.1016/j.parint.2005.11.009</doi></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1383-5769 |
ispartof | Parasitology international, 2006-01, Vol.55, p.S63-S67 |
issn | 1383-5769 1873-0329 |
language | eng |
recordid | cdi_proquest_miscellaneous_67632611 |
source | MEDLINE; Access via ScienceDirect (Elsevier) |
subjects | Amino Acid Sequence Animals Antigen B Base Sequence Cell Membrane - metabolism Echinococcus granulosus Echinococcus granulosus - genetics Echinococcus granulosus - metabolism Genetic Variation Helminth Proteins - chemistry Helminth Proteins - genetics Helminth Proteins - metabolism Helminth Proteins - secretion Intra-specific variation Lipoproteins - chemistry Lipoproteins - genetics Lipoproteins - metabolism Lipoproteins - secretion Molecular Sequence Data Platyhelminth parasites Secreted and membrane-bound proteins |
title | Identification and intra-specific variability analysis of secreted and membrane-bound proteins from Echinococcus granulosus |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-04T12%3A28%3A11IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Identification%20and%20intra-specific%20variability%20analysis%20of%20secreted%20and%20membrane-bound%20proteins%20from%20Echinococcus%20granulosus&rft.jtitle=Parasitology%20international&rft.au=Rosenzvit,%20Mara%20C.&rft.date=2006-01-01&rft.volume=55&rft.spage=S63&rft.epage=S67&rft.pages=S63-S67&rft.issn=1383-5769&rft.eissn=1873-0329&rft_id=info:doi/10.1016/j.parint.2005.11.009&rft_dat=%3Cproquest_cross%3E17082469%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17082469&rft_id=info:pmid/16368261&rft_els_id=S1383576905001121&rfr_iscdi=true |