Host cell-specific protein expression in vitro in Ehrlichia ruminantium
Ehrlichia ruminantium, a tick-transmitted pathogen, is the causative agent of heartwater in ruminants. In this study, a proteomic approach was used to identify host cell-specific E. ruminantium proteins encoded by the map1 multigene family, expressed in vitro in bovine endothelial and tick cell cult...
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| Veröffentlicht in: | Veterinary microbiology 2008-04, Vol.128 (1), p.136-147 |
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| creator | Postigo, M. Taoufik, A. Bell-Sakyi, L. Bekker, C.P.J. de Vries, E. Morrison, W.I. Jongejan, F. |
| description | Ehrlichia ruminantium, a tick-transmitted pathogen, is the causative agent of heartwater in ruminants. In this study, a proteomic approach was used to identify host cell-specific
E. ruminantium proteins encoded by the
map1 multigene family, expressed
in vitro in bovine endothelial and tick cell cultures. Two-dimensional gel electrophoresis combined with mass spectrometry analysis was used to establish the identities of immunodominant proteins. Proteins extracted from
E. ruminantium-infected endothelial cells were shown to be products of the
map1 gene, whereas tick cell-derived
E. ruminantium proteins were products of a different gene,
map1-1. The expressed proteins were found to be glycosylated. Differential expression of MAP1 family proteins
in vitro in mammalian and tick cell cultures indicates that the
map1 multigene family might be involved in the adaptation of
E. ruminantium to the mammalian host and vector tick. |
| doi_str_mv | 10.1016/j.vetmic.2007.09.023 |
| format | Article |
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E. ruminantium proteins encoded by the
map1 multigene family, expressed
in vitro in bovine endothelial and tick cell cultures. Two-dimensional gel electrophoresis combined with mass spectrometry analysis was used to establish the identities of immunodominant proteins. Proteins extracted from
E. ruminantium-infected endothelial cells were shown to be products of the
map1 gene, whereas tick cell-derived
E. ruminantium proteins were products of a different gene,
map1-1. The expressed proteins were found to be glycosylated. Differential expression of MAP1 family proteins
in vitro in mammalian and tick cell cultures indicates that the
map1 multigene family might be involved in the adaptation of
E. ruminantium to the mammalian host and vector tick.</description><identifier>ISSN: 0378-1135</identifier><identifier>EISSN: 1873-2542</identifier><identifier>DOI: 10.1016/j.vetmic.2007.09.023</identifier><identifier>PMID: 18006251</identifier><identifier>CODEN: VMICDQ</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Antibodies, Monoclonal - metabolism ; Bacterial Proteins - biosynthesis ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacteriology ; Biological and medical sciences ; Cattle ; Cattle Diseases - microbiology ; Cells, Cultured ; Ehrlichia ruminantium ; Ehrlichia ruminantium - genetics ; Ehrlichia ruminantium - physiology ; Endothelial Cells - cytology ; Endothelial Cells - microbiology ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Bacterial - physiology ; Glycosylation ; Heartwater Disease - microbiology ; Host-Pathogen Interactions - physiology ; Immunodominant Epitopes - biosynthesis ; Immunodominant Epitopes - chemistry ; Immunodominant Epitopes - genetics ; Ixodidae ; Ixodidae - cytology ; Ixodidae - microbiology ; map1 multigene family ; Microbiology ; Miscellaneous ; Peptides - genetics ; Peptides - metabolism ; Protein expression ; Proteins ; Proteomics ; Recombinant Proteins - biosynthesis ; Ruminantia ; Sequence Alignment ; Sheep ; Tick cell lines</subject><ispartof>Veterinary microbiology, 2008-04, Vol.128 (1), p.136-147</ispartof><rights>2007 Elsevier B.V.</rights><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c533t-c296623a031a448e9c34fb207d39920a4736652913f7200020b41c9cdcfb969d3</citedby><cites>FETCH-LOGICAL-c533t-c296623a031a448e9c34fb207d39920a4736652913f7200020b41c9cdcfb969d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0378113507004786$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20121236$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18006251$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Postigo, M.</creatorcontrib><creatorcontrib>Taoufik, A.</creatorcontrib><creatorcontrib>Bell-Sakyi, L.</creatorcontrib><creatorcontrib>Bekker, C.P.J.</creatorcontrib><creatorcontrib>de Vries, E.</creatorcontrib><creatorcontrib>Morrison, W.I.</creatorcontrib><creatorcontrib>Jongejan, F.</creatorcontrib><title>Host cell-specific protein expression in vitro in Ehrlichia ruminantium</title><title>Veterinary microbiology</title><addtitle>Vet Microbiol</addtitle><description>Ehrlichia ruminantium, a tick-transmitted pathogen, is the causative agent of heartwater in ruminants. In this study, a proteomic approach was used to identify host cell-specific
E. ruminantium proteins encoded by the
map1 multigene family, expressed
in vitro in bovine endothelial and tick cell cultures. Two-dimensional gel electrophoresis combined with mass spectrometry analysis was used to establish the identities of immunodominant proteins. Proteins extracted from
E. ruminantium-infected endothelial cells were shown to be products of the
map1 gene, whereas tick cell-derived
E. ruminantium proteins were products of a different gene,
map1-1. The expressed proteins were found to be glycosylated. Differential expression of MAP1 family proteins
in vitro in mammalian and tick cell cultures indicates that the
map1 multigene family might be involved in the adaptation of
E. ruminantium to the mammalian host and vector tick.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - metabolism</subject><subject>Bacterial Proteins - biosynthesis</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Cattle Diseases - microbiology</subject><subject>Cells, Cultured</subject><subject>Ehrlichia ruminantium</subject><subject>Ehrlichia ruminantium - genetics</subject><subject>Ehrlichia ruminantium - physiology</subject><subject>Endothelial Cells - cytology</subject><subject>Endothelial Cells - microbiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Bacterial - physiology</subject><subject>Glycosylation</subject><subject>Heartwater Disease - microbiology</subject><subject>Host-Pathogen Interactions - physiology</subject><subject>Immunodominant Epitopes - biosynthesis</subject><subject>Immunodominant Epitopes - chemistry</subject><subject>Immunodominant Epitopes - genetics</subject><subject>Ixodidae</subject><subject>Ixodidae - cytology</subject><subject>Ixodidae - microbiology</subject><subject>map1 multigene family</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Peptides - genetics</subject><subject>Peptides - metabolism</subject><subject>Protein expression</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Ruminantia</subject><subject>Sequence Alignment</subject><subject>Sheep</subject><subject>Tick cell lines</subject><issn>0378-1135</issn><issn>1873-2542</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1r3DAQhkVpSDYf_6AUX9qb3dHIlq1LoIQ0KQR6Sc5CO5bJLP7YSvaS_vto2SW5NaeZgWeGdx4hvkgoJEj9Y1Ps_DwwFQhQF2AKQPVJrGRTqxyrEj-LFai6yaVU1Zk4j3EDAKXRcCrOZAOgsZIrcXc_xTkj3_d53Hrijinbhmn2PGb-ZRt8jDyNWZp2PIdp39w-h57pmV0WloFHN868DJfipHN99FfHeiGeft0-3tznD3_uft_8fMipUmrOCY3WqBwo6cqy8YZU2a0R6lYZg-DKWmldoZGqq9NfgLAuJRlqqVsbbVp1Ib4f7qaQfxcfZztw3Md3o5-WaGvABmVVfwgiNKgBMYHlAaQwxRh8Z7eBBxf-WQl2b9pu7MG03Zu2YGwynda-Hu8v68G370tHtQn4dgRcJNd3wY3E8Y1DkChR6cRdHziftO3YBxuJ_Ui-5eBptu3E_0_yCgI9nLc</recordid><startdate>20080401</startdate><enddate>20080401</enddate><creator>Postigo, M.</creator><creator>Taoufik, A.</creator><creator>Bell-Sakyi, L.</creator><creator>Bekker, C.P.J.</creator><creator>de Vries, E.</creator><creator>Morrison, W.I.</creator><creator>Jongejan, F.</creator><general>Elsevier B.V</general><general>Elsevier Science</general><scope>IQODW</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20080401</creationdate><title>Host cell-specific protein expression in vitro in Ehrlichia ruminantium</title><author>Postigo, M. ; Taoufik, A. ; Bell-Sakyi, L. ; Bekker, C.P.J. ; de Vries, E. ; Morrison, W.I. ; Jongejan, F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c533t-c296623a031a448e9c34fb207d39920a4736652913f7200020b41c9cdcfb969d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Antibodies, Monoclonal - metabolism</topic><topic>Bacterial Proteins - biosynthesis</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Cattle Diseases - microbiology</topic><topic>Cells, Cultured</topic><topic>Ehrlichia ruminantium</topic><topic>Ehrlichia ruminantium - genetics</topic><topic>Ehrlichia ruminantium - physiology</topic><topic>Endothelial Cells - cytology</topic><topic>Endothelial Cells - microbiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Bacterial - physiology</topic><topic>Glycosylation</topic><topic>Heartwater Disease - microbiology</topic><topic>Host-Pathogen Interactions - physiology</topic><topic>Immunodominant Epitopes - biosynthesis</topic><topic>Immunodominant Epitopes - chemistry</topic><topic>Immunodominant Epitopes - genetics</topic><topic>Ixodidae</topic><topic>Ixodidae - cytology</topic><topic>Ixodidae - microbiology</topic><topic>map1 multigene family</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Peptides - genetics</topic><topic>Peptides - metabolism</topic><topic>Protein expression</topic><topic>Proteins</topic><topic>Proteomics</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Ruminantia</topic><topic>Sequence Alignment</topic><topic>Sheep</topic><topic>Tick cell lines</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Postigo, M.</creatorcontrib><creatorcontrib>Taoufik, A.</creatorcontrib><creatorcontrib>Bell-Sakyi, L.</creatorcontrib><creatorcontrib>Bekker, C.P.J.</creatorcontrib><creatorcontrib>de Vries, E.</creatorcontrib><creatorcontrib>Morrison, W.I.</creatorcontrib><creatorcontrib>Jongejan, F.</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>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Veterinary microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Postigo, M.</au><au>Taoufik, A.</au><au>Bell-Sakyi, L.</au><au>Bekker, C.P.J.</au><au>de Vries, E.</au><au>Morrison, W.I.</au><au>Jongejan, F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Host cell-specific protein expression in vitro in Ehrlichia ruminantium</atitle><jtitle>Veterinary microbiology</jtitle><addtitle>Vet Microbiol</addtitle><date>2008-04-01</date><risdate>2008</risdate><volume>128</volume><issue>1</issue><spage>136</spage><epage>147</epage><pages>136-147</pages><issn>0378-1135</issn><eissn>1873-2542</eissn><coden>VMICDQ</coden><abstract>Ehrlichia ruminantium, a tick-transmitted pathogen, is the causative agent of heartwater in ruminants. In this study, a proteomic approach was used to identify host cell-specific
E. ruminantium proteins encoded by the
map1 multigene family, expressed
in vitro in bovine endothelial and tick cell cultures. Two-dimensional gel electrophoresis combined with mass spectrometry analysis was used to establish the identities of immunodominant proteins. Proteins extracted from
E. ruminantium-infected endothelial cells were shown to be products of the
map1 gene, whereas tick cell-derived
E. ruminantium proteins were products of a different gene,
map1-1. The expressed proteins were found to be glycosylated. Differential expression of MAP1 family proteins
in vitro in mammalian and tick cell cultures indicates that the
map1 multigene family might be involved in the adaptation of
E. ruminantium to the mammalian host and vector tick.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>18006251</pmid><doi>10.1016/j.vetmic.2007.09.023</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1135 |
| ispartof | Veterinary microbiology, 2008-04, Vol.128 (1), p.136-147 |
| issn | 0378-1135 1873-2542 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70282157 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Antibodies, Monoclonal - metabolism Bacterial Proteins - biosynthesis Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Biological and medical sciences Cattle Cattle Diseases - microbiology Cells, Cultured Ehrlichia ruminantium Ehrlichia ruminantium - genetics Ehrlichia ruminantium - physiology Endothelial Cells - cytology Endothelial Cells - microbiology Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Bacterial - physiology Glycosylation Heartwater Disease - microbiology Host-Pathogen Interactions - physiology Immunodominant Epitopes - biosynthesis Immunodominant Epitopes - chemistry Immunodominant Epitopes - genetics Ixodidae Ixodidae - cytology Ixodidae - microbiology map1 multigene family Microbiology Miscellaneous Peptides - genetics Peptides - metabolism Protein expression Proteins Proteomics Recombinant Proteins - biosynthesis Ruminantia Sequence Alignment Sheep Tick cell lines |
| title | Host cell-specific protein expression in vitro in Ehrlichia ruminantium |
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