Extracellular vesicles released by Trypanosoma evansi: induction analysis and proteomics
Trypanosoma evansi is a unicellular protozoan responsible for causing a disease known as “surra,” which is found in different regions of the world and primarily affects horses and camels. Few information is known about virulence factors released from the parasite within the animals. The organism can...
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| Veröffentlicht in: | Parasitology research (1987) 2024-09, Vol.123 (9), p.314-314, Article 314 |
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| container_title | Parasitology research (1987) |
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| creator | Ungri, Amanda Martins dos Santos Sabatke, Bruna Fernanda Rossi, Izadora Volpato das Neves, Gabriella Bassi Marques, Júlia Ribeiro, Brenda Guedes Borges, Gabriela Kaiser Moreira, Renato Simões Ramírez, Marcel Ivan Miletti, Luiz Claudio |
| description | Trypanosoma evansi
is a unicellular protozoan responsible for causing a disease known as “surra,” which is found in different regions of the world and primarily affects horses and camels. Few information is known about virulence factors released from the parasite within the animals. The organism can secrete extracellular vesicles (EVs), which transport a variety of molecules, including proteins. Before being considered exclusively as a means for eliminating unwanted substances, extracellular vesicles (EVs) have emerged as key players in intercellular communication, facilitating interactions between cells, host cells, and parasites, and even between parasites themselves. Thus, they may be used as potential biomarkers. This study aimed to assess the induction of EVs production by Ca
+2
, conduct a proteomic analysis of the EVs released by
T. evansi
, and identify epitopes that could serve as biomarkers. The findings indicated that Ca
+2
is not an effective promoter of vesiculation in
T. evansi
. Furthermore, the proteomic analysis has identified multiple proteins that have been investigated as biomarkers or vaccine antigens, previously. A total of 442 proteins were identified, with 7 of them specifically recognizing 9 epitopes that are unique to
T. evansi
. At least one of these epitopes of TevSTIB805.9.11580 have been previously identified, which increases the possibility of further investigating its potential as a biomarker. |
| doi_str_mv | 10.1007/s00436-024-08330-x |
| format | Article |
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is a unicellular protozoan responsible for causing a disease known as “surra,” which is found in different regions of the world and primarily affects horses and camels. Few information is known about virulence factors released from the parasite within the animals. The organism can secrete extracellular vesicles (EVs), which transport a variety of molecules, including proteins. Before being considered exclusively as a means for eliminating unwanted substances, extracellular vesicles (EVs) have emerged as key players in intercellular communication, facilitating interactions between cells, host cells, and parasites, and even between parasites themselves. Thus, they may be used as potential biomarkers. This study aimed to assess the induction of EVs production by Ca
+2
, conduct a proteomic analysis of the EVs released by
T. evansi
, and identify epitopes that could serve as biomarkers. The findings indicated that Ca
+2
is not an effective promoter of vesiculation in
T. evansi
. Furthermore, the proteomic analysis has identified multiple proteins that have been investigated as biomarkers or vaccine antigens, previously. A total of 442 proteins were identified, with 7 of them specifically recognizing 9 epitopes that are unique to
T. evansi
. At least one of these epitopes of TevSTIB805.9.11580 have been previously identified, which increases the possibility of further investigating its potential as a biomarker.</description><identifier>ISSN: 0932-0113</identifier><identifier>ISSN: 1432-1955</identifier><identifier>EISSN: 1432-1955</identifier><identifier>DOI: 10.1007/s00436-024-08330-x</identifier><identifier>PMID: 39225716</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Animals ; Biomarkers ; Biomedical and Life Sciences ; Biomedicine ; Calcium - metabolism ; cell communication ; Cell interactions ; Epitopes ; Epitopes - immunology ; Extracellular vesicles ; Extracellular Vesicles - metabolism ; Immunology ; Medical Microbiology ; Microbiology ; Parasites ; Protein transport ; Proteins ; Proteome ; Proteomics ; Protozoan Proteins - genetics ; Protozoan Proteins - metabolism ; Surra ; Trypanosoma - genetics ; Trypanosoma - metabolism ; Trypanosoma evansi ; Trypanosomiasis - parasitology ; vaccines ; virulence ; Virulence factors</subject><ispartof>Parasitology research (1987), 2024-09, Vol.123 (9), p.314-314, Article 314</ispartof><rights>The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2024. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c289t-9a9b140c3703bf8a452292866c2d70be68578f44ef5a028ffd2a8c04f4eb924f3</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/s00436-024-08330-x$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00436-024-08330-x$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39225716$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ungri, Amanda Martins</creatorcontrib><creatorcontrib>dos Santos Sabatke, Bruna Fernanda</creatorcontrib><creatorcontrib>Rossi, Izadora Volpato</creatorcontrib><creatorcontrib>das Neves, Gabriella Bassi</creatorcontrib><creatorcontrib>Marques, Júlia</creatorcontrib><creatorcontrib>Ribeiro, Brenda Guedes</creatorcontrib><creatorcontrib>Borges, Gabriela Kaiser</creatorcontrib><creatorcontrib>Moreira, Renato Simões</creatorcontrib><creatorcontrib>Ramírez, Marcel Ivan</creatorcontrib><creatorcontrib>Miletti, Luiz Claudio</creatorcontrib><title>Extracellular vesicles released by Trypanosoma evansi: induction analysis and proteomics</title><title>Parasitology research (1987)</title><addtitle>Parasitol Res</addtitle><addtitle>Parasitol Res</addtitle><description>Trypanosoma evansi
is a unicellular protozoan responsible for causing a disease known as “surra,” which is found in different regions of the world and primarily affects horses and camels. Few information is known about virulence factors released from the parasite within the animals. The organism can secrete extracellular vesicles (EVs), which transport a variety of molecules, including proteins. Before being considered exclusively as a means for eliminating unwanted substances, extracellular vesicles (EVs) have emerged as key players in intercellular communication, facilitating interactions between cells, host cells, and parasites, and even between parasites themselves. Thus, they may be used as potential biomarkers. This study aimed to assess the induction of EVs production by Ca
+2
, conduct a proteomic analysis of the EVs released by
T. evansi
, and identify epitopes that could serve as biomarkers. The findings indicated that Ca
+2
is not an effective promoter of vesiculation in
T. evansi
. Furthermore, the proteomic analysis has identified multiple proteins that have been investigated as biomarkers or vaccine antigens, previously. A total of 442 proteins were identified, with 7 of them specifically recognizing 9 epitopes that are unique to
T. evansi
. At least one of these epitopes of TevSTIB805.9.11580 have been previously identified, which increases the possibility of further investigating its potential as a biomarker.</description><subject>Animals</subject><subject>Biomarkers</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Calcium - metabolism</subject><subject>cell communication</subject><subject>Cell interactions</subject><subject>Epitopes</subject><subject>Epitopes - immunology</subject><subject>Extracellular vesicles</subject><subject>Extracellular Vesicles - metabolism</subject><subject>Immunology</subject><subject>Medical Microbiology</subject><subject>Microbiology</subject><subject>Parasites</subject><subject>Protein transport</subject><subject>Proteins</subject><subject>Proteome</subject><subject>Proteomics</subject><subject>Protozoan Proteins - genetics</subject><subject>Protozoan Proteins - metabolism</subject><subject>Surra</subject><subject>Trypanosoma - genetics</subject><subject>Trypanosoma - metabolism</subject><subject>Trypanosoma evansi</subject><subject>Trypanosomiasis - parasitology</subject><subject>vaccines</subject><subject>virulence</subject><subject>Virulence factors</subject><issn>0932-0113</issn><issn>1432-1955</issn><issn>1432-1955</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1rFEEQhhtRzCb6B3KQAS9eRqu_pntyCyEaIeAlgremp6daJszHpmsm7P57e53EQA7BUxXUU29RPIydcvjMAcwXAlCyKkGoEqyUUO5esQ1XUpS81vo120Cde-BcHrFjolsAbiql3rIjWQuhDa827Nflbk4-YN8vvU_FPVIXeqQiYY-esC2afXGT9ls_TjQNvsB7P1J3VnRju4S5m8bCj77fU0e5aYttmmachi7QO_Ym-p7w_UM9YT-_Xt5cXJXXP759vzi_LoOw9VzWvm64giANyCZar7QQtbBVFURroMHKamOjUhi1B2FjbIW3AVRU2NRCRXnCPq25-fTdgjS7oaPDP37EaSEnuZZGW674f6AAwmgjDujHZ-jttKT86UppaaUQmRIrFdJElDC6beoGn_aOgzsocqsilxW5v4rcLi99eIhemgHbfyuPTjIgV4DyaPyN6en2C7F_ALGUnFw</recordid><startdate>20240901</startdate><enddate>20240901</enddate><creator>Ungri, Amanda Martins</creator><creator>dos Santos Sabatke, Bruna Fernanda</creator><creator>Rossi, Izadora Volpato</creator><creator>das Neves, Gabriella Bassi</creator><creator>Marques, Júlia</creator><creator>Ribeiro, Brenda Guedes</creator><creator>Borges, Gabriela Kaiser</creator><creator>Moreira, Renato Simões</creator><creator>Ramírez, Marcel Ivan</creator><creator>Miletti, Luiz Claudio</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</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>7S9</scope><scope>L.6</scope></search><sort><creationdate>20240901</creationdate><title>Extracellular vesicles released by Trypanosoma evansi: induction analysis and proteomics</title><author>Ungri, Amanda Martins ; 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is a unicellular protozoan responsible for causing a disease known as “surra,” which is found in different regions of the world and primarily affects horses and camels. Few information is known about virulence factors released from the parasite within the animals. The organism can secrete extracellular vesicles (EVs), which transport a variety of molecules, including proteins. Before being considered exclusively as a means for eliminating unwanted substances, extracellular vesicles (EVs) have emerged as key players in intercellular communication, facilitating interactions between cells, host cells, and parasites, and even between parasites themselves. Thus, they may be used as potential biomarkers. This study aimed to assess the induction of EVs production by Ca
+2
, conduct a proteomic analysis of the EVs released by
T. evansi
, and identify epitopes that could serve as biomarkers. The findings indicated that Ca
+2
is not an effective promoter of vesiculation in
T. evansi
. Furthermore, the proteomic analysis has identified multiple proteins that have been investigated as biomarkers or vaccine antigens, previously. A total of 442 proteins were identified, with 7 of them specifically recognizing 9 epitopes that are unique to
T. evansi
. At least one of these epitopes of TevSTIB805.9.11580 have been previously identified, which increases the possibility of further investigating its potential as a biomarker.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>39225716</pmid><doi>10.1007/s00436-024-08330-x</doi><tpages>1</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0932-0113 |
| ispartof | Parasitology research (1987), 2024-09, Vol.123 (9), p.314-314, Article 314 |
| issn | 0932-0113 1432-1955 1432-1955 |
| language | eng |
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| source | MEDLINE; SpringerLink Journals |
| subjects | Animals Biomarkers Biomedical and Life Sciences Biomedicine Calcium - metabolism cell communication Cell interactions Epitopes Epitopes - immunology Extracellular vesicles Extracellular Vesicles - metabolism Immunology Medical Microbiology Microbiology Parasites Protein transport Proteins Proteome Proteomics Protozoan Proteins - genetics Protozoan Proteins - metabolism Surra Trypanosoma - genetics Trypanosoma - metabolism Trypanosoma evansi Trypanosomiasis - parasitology vaccines virulence Virulence factors |
| title | Extracellular vesicles released by Trypanosoma evansi: induction analysis and proteomics |
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