Eimeria bovis-triggered neutrophil extracellular trap formation is CD11b-, ERK 1/2-, p38 MAP kinase- and SOCE-dependent
Eimeria bovis is an important coccidian parasite that causes high economic losses in the cattle industry. We recently showed that polymorphonuclear neutrophils (PMN) react upon E. bovis sporozoite exposure by neutrophil extracellular trap (NET) formation. We focused here on the molecular mechanisms...
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description | Eimeria bovis is an important coccidian parasite that causes high economic losses in the cattle industry. We recently showed that polymorphonuclear neutrophils (PMN) react upon E. bovis sporozoite exposure by neutrophil extracellular trap (NET) formation. We focused here on the molecular mechanisms that are involved in this process. The sporozoite encounter led to an enhanced surface expression of neutrophil CD11b suggesting a potential role of this receptor in E. bovis-mediated NETosis. Antibody-mediated blockage of CD11b confirmed this assumption and led to a significantly decreased sporozoite-triggered NET. In addition, E. bovis-induced NETosis was found to be Ca²⁺-dependent since the inhibition of store-operated calcium entry (SOCE) significantly diminished NET. Furthermore, NADPH oxidase, neutrophil elastase (NE) and myeloperoxidase (MPO) were confirmed as key molecules in sporozoite-triggered NETosis, as inhibition thereof blocked parasite-triggered NET. PMN degranulation analyses revealed a significant release of matrix metalloprotease-9 containing granules upon sporozoite exposure. We further show a significantly enhanced phosphorylation of ERK1/2 and p38 MAPK in sporozoite-exposed PMN indicating a key role of this signaling pathway in E. bovis-mediated NETosis. Accordingly, ERK 1/2 and p38 MAPK inhibition led to a significant decrease in NET formation. Finally, we demonstrate that sporozoite-induced NETosis is neither a stage-, species-, nor host-specific process. |
doi_str_mv | 10.1186/s13567-015-0155-6 |
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We recently showed that polymorphonuclear neutrophils (PMN) react upon E. bovis sporozoite exposure by neutrophil extracellular trap (NET) formation. We focused here on the molecular mechanisms that are involved in this process. The sporozoite encounter led to an enhanced surface expression of neutrophil CD11b suggesting a potential role of this receptor in E. bovis-mediated NETosis. Antibody-mediated blockage of CD11b confirmed this assumption and led to a significantly decreased sporozoite-triggered NET. In addition, E. bovis-induced NETosis was found to be Ca²⁺-dependent since the inhibition of store-operated calcium entry (SOCE) significantly diminished NET. Furthermore, NADPH oxidase, neutrophil elastase (NE) and myeloperoxidase (MPO) were confirmed as key molecules in sporozoite-triggered NETosis, as inhibition thereof blocked parasite-triggered NET. PMN degranulation analyses revealed a significant release of matrix metalloprotease-9 containing granules upon sporozoite exposure. We further show a significantly enhanced phosphorylation of ERK1/2 and p38 MAPK in sporozoite-exposed PMN indicating a key role of this signaling pathway in E. bovis-mediated NETosis. Accordingly, ERK 1/2 and p38 MAPK inhibition led to a significant decrease in NET formation. Finally, we demonstrate that sporozoite-induced NETosis is neither a stage-, species-, nor host-specific process.</description><identifier>ISSN: 1297-9716</identifier><identifier>ISSN: 0928-4249</identifier><identifier>EISSN: 1297-9716</identifier><identifier>DOI: 10.1186/s13567-015-0155-6</identifier><identifier>PMID: 25885264</identifier><language>eng</language><publisher>England: Springer-Verlag</publisher><subject>Animals ; calcium ; Cattle ; Cattle Diseases - immunology ; Cattle Diseases - parasitology ; Coccidiosis - immunology ; Coccidiosis - parasitology ; Coccidiosis - veterinary ; Eimeria - immunology ; Eimeria - ultrastructure ; Eimeria bovis ; elastase ; Extracellular Traps - immunology ; gelatinase B ; granules ; host specificity ; Immunity, Innate ; industry ; Life Sciences ; Microscopy, Electron, Scanning - veterinary ; Microscopy, Fluorescence - veterinary ; mitogen-activated protein kinase ; myeloperoxidase ; NADP (coenzyme) ; neutrophils ; Neutrophils - immunology ; parasites ; phosphorylation ; signal transduction ; Sporozoites - immunology ; Sporozoites - ultrastructure</subject><ispartof>Veterinary research (Paris), 2015-03, Vol.46 (1), p.23-23</ispartof><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>Muñoz-Caro et al.; licensee BioMed Central. 2015</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c696t-b7e61fb8335264cc6adfa0b6e45724d759a31ac11b74ac1e29945804ce05369c3</citedby><cites>FETCH-LOGICAL-c696t-b7e61fb8335264cc6adfa0b6e45724d759a31ac11b74ac1e29945804ce05369c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4349228/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4349228/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,724,777,781,861,882,27905,27906,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25885264$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-01290672$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Muñoz-Caro, Tamara</creatorcontrib><creatorcontrib>Mena Huertas, Sandra Jaqueline</creatorcontrib><creatorcontrib>Conejeros, Ivan</creatorcontrib><creatorcontrib>Alarcón, Pablo</creatorcontrib><creatorcontrib>Hidalgo, María A</creatorcontrib><creatorcontrib>Burgos, Rafael A</creatorcontrib><creatorcontrib>Hermosilla, Carlos</creatorcontrib><creatorcontrib>Taubert, Anja</creatorcontrib><title>Eimeria bovis-triggered neutrophil extracellular trap formation is CD11b-, ERK 1/2-, p38 MAP kinase- and SOCE-dependent</title><title>Veterinary research (Paris)</title><addtitle>Vet Res</addtitle><description>Eimeria bovis is an important coccidian parasite that causes high economic losses in the cattle industry. We recently showed that polymorphonuclear neutrophils (PMN) react upon E. bovis sporozoite exposure by neutrophil extracellular trap (NET) formation. We focused here on the molecular mechanisms that are involved in this process. The sporozoite encounter led to an enhanced surface expression of neutrophil CD11b suggesting a potential role of this receptor in E. bovis-mediated NETosis. Antibody-mediated blockage of CD11b confirmed this assumption and led to a significantly decreased sporozoite-triggered NET. In addition, E. bovis-induced NETosis was found to be Ca²⁺-dependent since the inhibition of store-operated calcium entry (SOCE) significantly diminished NET. Furthermore, NADPH oxidase, neutrophil elastase (NE) and myeloperoxidase (MPO) were confirmed as key molecules in sporozoite-triggered NETosis, as inhibition thereof blocked parasite-triggered NET. PMN degranulation analyses revealed a significant release of matrix metalloprotease-9 containing granules upon sporozoite exposure. We further show a significantly enhanced phosphorylation of ERK1/2 and p38 MAPK in sporozoite-exposed PMN indicating a key role of this signaling pathway in E. bovis-mediated NETosis. Accordingly, ERK 1/2 and p38 MAPK inhibition led to a significant decrease in NET formation. Finally, we demonstrate that sporozoite-induced NETosis is neither a stage-, species-, nor host-specific process.</description><subject>Animals</subject><subject>calcium</subject><subject>Cattle</subject><subject>Cattle Diseases - immunology</subject><subject>Cattle Diseases - parasitology</subject><subject>Coccidiosis - immunology</subject><subject>Coccidiosis - parasitology</subject><subject>Coccidiosis - veterinary</subject><subject>Eimeria - immunology</subject><subject>Eimeria - ultrastructure</subject><subject>Eimeria bovis</subject><subject>elastase</subject><subject>Extracellular Traps - immunology</subject><subject>gelatinase B</subject><subject>granules</subject><subject>host specificity</subject><subject>Immunity, Innate</subject><subject>industry</subject><subject>Life Sciences</subject><subject>Microscopy, Electron, Scanning - veterinary</subject><subject>Microscopy, Fluorescence - veterinary</subject><subject>mitogen-activated protein kinase</subject><subject>myeloperoxidase</subject><subject>NADP (coenzyme)</subject><subject>neutrophils</subject><subject>Neutrophils - immunology</subject><subject>parasites</subject><subject>phosphorylation</subject><subject>signal transduction</subject><subject>Sporozoites - immunology</subject><subject>Sporozoites - ultrastructure</subject><issn>1297-9716</issn><issn>0928-4249</issn><issn>1297-9716</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUk1v1DAQjRCIfsAP4AI-goSpP8fJpdJqWShiURGlZ8tJnF1DEgc72cK_x1FKVThxGM2T_d7M83iy7BklbyjN4SxSLkFhQuUcEsOD7JiyQuFCUXh4Dx9lJzF-I4QCl-JxdsRknksG4ji72bjOBmdQ6Q8u4jG43c4GW6PeTmPww961yP4cg6ls206tCSjhATU-dGZ0vkcuovVbSkv8Gm2-fET0jCU08Bx9Wn1G311vosXI9DW6ulxvcG0H29e2H59kjxrTRvv0Np9m1-82X9cXeHv5_sN6tcUVFDDiUlmgTZlzPtutKjB1Y0gJVkjFRK1kYTg1VeqvREqWFYWQORGVJZJDUfHT7HypO0xlZ-sqtQ6m1UNwnQm_tDdO_33Tu73e-YMWXBSM5anAq6XA_h_ZxWqr5zOSpkxAsQNN3Je3zYL_Mdk46s7FeXCmt36KmoLKpQTC-f9QBeRApExUulCr4GMMtrmzQYme90Ave5CcyDmkhqR5fv_Zd4o_H58ILxZCY7w2u-Civr5iSZ2WhBdKAv8N_SW03A</recordid><startdate>20150305</startdate><enddate>20150305</enddate><creator>Muñoz-Caro, Tamara</creator><creator>Mena Huertas, Sandra Jaqueline</creator><creator>Conejeros, Ivan</creator><creator>Alarcón, Pablo</creator><creator>Hidalgo, María A</creator><creator>Burgos, Rafael A</creator><creator>Hermosilla, Carlos</creator><creator>Taubert, Anja</creator><general>Springer-Verlag</general><general>BioMed Central</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><scope>7S9</scope><scope>L.6</scope><scope>1XC</scope><scope>VOOES</scope><scope>5PM</scope></search><sort><creationdate>20150305</creationdate><title>Eimeria bovis-triggered neutrophil extracellular trap formation is CD11b-, ERK 1/2-, p38 MAP kinase- and SOCE-dependent</title><author>Muñoz-Caro, Tamara ; Mena Huertas, Sandra Jaqueline ; Conejeros, Ivan ; Alarcón, Pablo ; Hidalgo, María A ; Burgos, Rafael A ; Hermosilla, Carlos ; Taubert, Anja</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c696t-b7e61fb8335264cc6adfa0b6e45724d759a31ac11b74ac1e29945804ce05369c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Animals</topic><topic>calcium</topic><topic>Cattle</topic><topic>Cattle Diseases - immunology</topic><topic>Cattle Diseases - parasitology</topic><topic>Coccidiosis - immunology</topic><topic>Coccidiosis - parasitology</topic><topic>Coccidiosis - veterinary</topic><topic>Eimeria - immunology</topic><topic>Eimeria - ultrastructure</topic><topic>Eimeria bovis</topic><topic>elastase</topic><topic>Extracellular Traps - immunology</topic><topic>gelatinase B</topic><topic>granules</topic><topic>host specificity</topic><topic>Immunity, Innate</topic><topic>industry</topic><topic>Life Sciences</topic><topic>Microscopy, Electron, Scanning - veterinary</topic><topic>Microscopy, Fluorescence - veterinary</topic><topic>mitogen-activated protein kinase</topic><topic>myeloperoxidase</topic><topic>NADP (coenzyme)</topic><topic>neutrophils</topic><topic>Neutrophils - immunology</topic><topic>parasites</topic><topic>phosphorylation</topic><topic>signal transduction</topic><topic>Sporozoites - immunology</topic><topic>Sporozoites - ultrastructure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Muñoz-Caro, Tamara</creatorcontrib><creatorcontrib>Mena Huertas, Sandra Jaqueline</creatorcontrib><creatorcontrib>Conejeros, Ivan</creatorcontrib><creatorcontrib>Alarcón, Pablo</creatorcontrib><creatorcontrib>Hidalgo, María A</creatorcontrib><creatorcontrib>Burgos, Rafael A</creatorcontrib><creatorcontrib>Hermosilla, Carlos</creatorcontrib><creatorcontrib>Taubert, Anja</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><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Veterinary research (Paris)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Muñoz-Caro, Tamara</au><au>Mena Huertas, Sandra Jaqueline</au><au>Conejeros, Ivan</au><au>Alarcón, Pablo</au><au>Hidalgo, María A</au><au>Burgos, Rafael A</au><au>Hermosilla, Carlos</au><au>Taubert, Anja</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Eimeria bovis-triggered neutrophil extracellular trap formation is CD11b-, ERK 1/2-, p38 MAP kinase- and SOCE-dependent</atitle><jtitle>Veterinary research (Paris)</jtitle><addtitle>Vet Res</addtitle><date>2015-03-05</date><risdate>2015</risdate><volume>46</volume><issue>1</issue><spage>23</spage><epage>23</epage><pages>23-23</pages><issn>1297-9716</issn><issn>0928-4249</issn><eissn>1297-9716</eissn><abstract>Eimeria bovis is an important coccidian parasite that causes high economic losses in the cattle industry. We recently showed that polymorphonuclear neutrophils (PMN) react upon E. bovis sporozoite exposure by neutrophil extracellular trap (NET) formation. We focused here on the molecular mechanisms that are involved in this process. The sporozoite encounter led to an enhanced surface expression of neutrophil CD11b suggesting a potential role of this receptor in E. bovis-mediated NETosis. Antibody-mediated blockage of CD11b confirmed this assumption and led to a significantly decreased sporozoite-triggered NET. In addition, E. bovis-induced NETosis was found to be Ca²⁺-dependent since the inhibition of store-operated calcium entry (SOCE) significantly diminished NET. Furthermore, NADPH oxidase, neutrophil elastase (NE) and myeloperoxidase (MPO) were confirmed as key molecules in sporozoite-triggered NETosis, as inhibition thereof blocked parasite-triggered NET. PMN degranulation analyses revealed a significant release of matrix metalloprotease-9 containing granules upon sporozoite exposure. We further show a significantly enhanced phosphorylation of ERK1/2 and p38 MAPK in sporozoite-exposed PMN indicating a key role of this signaling pathway in E. bovis-mediated NETosis. Accordingly, ERK 1/2 and p38 MAPK inhibition led to a significant decrease in NET formation. Finally, we demonstrate that sporozoite-induced NETosis is neither a stage-, species-, nor host-specific process.</abstract><cop>England</cop><pub>Springer-Verlag</pub><pmid>25885264</pmid><doi>10.1186/s13567-015-0155-6</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals calcium Cattle Cattle Diseases - immunology Cattle Diseases - parasitology Coccidiosis - immunology Coccidiosis - parasitology Coccidiosis - veterinary Eimeria - immunology Eimeria - ultrastructure Eimeria bovis elastase Extracellular Traps - immunology gelatinase B granules host specificity Immunity, Innate industry Life Sciences Microscopy, Electron, Scanning - veterinary Microscopy, Fluorescence - veterinary mitogen-activated protein kinase myeloperoxidase NADP (coenzyme) neutrophils Neutrophils - immunology parasites phosphorylation signal transduction Sporozoites - immunology Sporozoites - ultrastructure |
title | Eimeria bovis-triggered neutrophil extracellular trap formation is CD11b-, ERK 1/2-, p38 MAP kinase- and SOCE-dependent |
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