Proteomic analysis of castor bean tick Ixodes ricinus: a focus on chemosensory organs
In arthropods, the large majority of studies on olfaction have been focused on insects, where most of the proteins involved have been identified. In particular, chemosensing in insects relies on two families of membrane receptors, olfactory/gustatory receptors (ORs/GRs) and ionotropic receptors (IRs...
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Veröffentlicht in: | Insect biochemistry and molecular biology 2016-11, Vol.78, p.58-68 |
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description | In arthropods, the large majority of studies on olfaction have been focused on insects, where most of the proteins involved have been identified. In particular, chemosensing in insects relies on two families of membrane receptors, olfactory/gustatory receptors (ORs/GRs) and ionotropic receptors (IRs), and two classes of soluble proteins, odorant-binding proteins (OBPs) and chemosensory proteins (CSPs). In other arthropods, such as ticks and mites, only IRs have been identified, while genes encoding for OBPs and CSPs are absent. A third class of soluble proteins, called Niemann-Pick C2 (NPC2) has been suggested as potential carrier for semiochemicals both in insects and other arthropods.
Here we report the results of a proteomic analysis on olfactory organs (Haller's organ and palps) and control tissues of the tick Ixodes ricinus, and of immunostaining experiments targeting NPC2s. Adopting different extraction and proteomic approaches, we identified a large number of proteins, and highlighted those differentially expressed. None of the 13 NPC2s known for this species was found. On the other hand, using immunocytochemistry, we detected reaction against one NPC2 in the Haller's organ and palp sensilla. We hypothesized that the low concentration of such proteins in the tick's tissues could possibly explain the discrepant results. In ligand-binding assays the corresponding recombinant NPC2 showed good affinity to the fluorescent probe N-phenylnaphthylamine and to few organic compounds, supporting a putative role of NPC2s as odorant carriers.
[Display omitted]
•In insects soluble olfactory proteins are widely studied, while proteins with similar functions are unknown in Acari.•We hypothesized that Niemann Pick C2 proteins (NPC2) act as odorant carriers in tick chemosensilla.•We performed a proteomic study of chemosensory organs of the tick Ixodes ricinus to search for soluble olfactory proteins.•A member of NPC2 proteins was detected in chemosensilla by immunocytochemistry; its affinity to some odorants was measured. |
doi_str_mv | 10.1016/j.ibmb.2016.09.004 |
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Here we report the results of a proteomic analysis on olfactory organs (Haller's organ and palps) and control tissues of the tick Ixodes ricinus, and of immunostaining experiments targeting NPC2s. Adopting different extraction and proteomic approaches, we identified a large number of proteins, and highlighted those differentially expressed. None of the 13 NPC2s known for this species was found. On the other hand, using immunocytochemistry, we detected reaction against one NPC2 in the Haller's organ and palp sensilla. We hypothesized that the low concentration of such proteins in the tick's tissues could possibly explain the discrepant results. In ligand-binding assays the corresponding recombinant NPC2 showed good affinity to the fluorescent probe N-phenylnaphthylamine and to few organic compounds, supporting a putative role of NPC2s as odorant carriers.
[Display omitted]
•In insects soluble olfactory proteins are widely studied, while proteins with similar functions are unknown in Acari.•We hypothesized that Niemann Pick C2 proteins (NPC2) act as odorant carriers in tick chemosensilla.•We performed a proteomic study of chemosensory organs of the tick Ixodes ricinus to search for soluble olfactory proteins.•A member of NPC2 proteins was detected in chemosensilla by immunocytochemistry; its affinity to some odorants was measured.</description><identifier>ISSN: 0965-1748</identifier><identifier>EISSN: 1879-0240</identifier><identifier>DOI: 10.1016/j.ibmb.2016.09.004</identifier><identifier>PMID: 27693516</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Animals ; Arthropod Antennae - physiology ; Arthropod Proteins - genetics ; Arthropod Proteins - metabolism ; Arthropoda ; Female ; Haller’s organ ; Ixodes - genetics ; Ixodes - growth & development ; Ixodes - physiology ; Ixodes ricinus ; Ixodidae ; Male ; Nymph - growth & development ; Olfaction ; Proteome ; Proteomics ; Receptors, Odorant - genetics ; Receptors, Odorant - metabolism ; Soluble olfactory proteins ; Ticks</subject><ispartof>Insect biochemistry and molecular biology, 2016-11, Vol.78, p.58-68</ispartof><rights>2016 Elsevier Ltd</rights><rights>Copyright © 2016 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c389t-f07ab29bb4b2f6d62aa833cf9ae4225ab32ce51b093434a35ac67c7cc10a152f3</citedby><cites>FETCH-LOGICAL-c389t-f07ab29bb4b2f6d62aa833cf9ae4225ab32ce51b093434a35ac67c7cc10a152f3</cites><orcidid>0000-0002-2939-2103</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ibmb.2016.09.004$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27693516$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Iovinella, Immacolata</creatorcontrib><creatorcontrib>Ban, Liping</creatorcontrib><creatorcontrib>Song, Limei</creatorcontrib><creatorcontrib>Pelosi, Paolo</creatorcontrib><creatorcontrib>Dani, Francesca Romana</creatorcontrib><title>Proteomic analysis of castor bean tick Ixodes ricinus: a focus on chemosensory organs</title><title>Insect biochemistry and molecular biology</title><addtitle>Insect Biochem Mol Biol</addtitle><description>In arthropods, the large majority of studies on olfaction have been focused on insects, where most of the proteins involved have been identified. In particular, chemosensing in insects relies on two families of membrane receptors, olfactory/gustatory receptors (ORs/GRs) and ionotropic receptors (IRs), and two classes of soluble proteins, odorant-binding proteins (OBPs) and chemosensory proteins (CSPs). In other arthropods, such as ticks and mites, only IRs have been identified, while genes encoding for OBPs and CSPs are absent. A third class of soluble proteins, called Niemann-Pick C2 (NPC2) has been suggested as potential carrier for semiochemicals both in insects and other arthropods.
Here we report the results of a proteomic analysis on olfactory organs (Haller's organ and palps) and control tissues of the tick Ixodes ricinus, and of immunostaining experiments targeting NPC2s. Adopting different extraction and proteomic approaches, we identified a large number of proteins, and highlighted those differentially expressed. None of the 13 NPC2s known for this species was found. On the other hand, using immunocytochemistry, we detected reaction against one NPC2 in the Haller's organ and palp sensilla. We hypothesized that the low concentration of such proteins in the tick's tissues could possibly explain the discrepant results. In ligand-binding assays the corresponding recombinant NPC2 showed good affinity to the fluorescent probe N-phenylnaphthylamine and to few organic compounds, supporting a putative role of NPC2s as odorant carriers.
[Display omitted]
•In insects soluble olfactory proteins are widely studied, while proteins with similar functions are unknown in Acari.•We hypothesized that Niemann Pick C2 proteins (NPC2) act as odorant carriers in tick chemosensilla.•We performed a proteomic study of chemosensory organs of the tick Ixodes ricinus to search for soluble olfactory proteins.•A member of NPC2 proteins was detected in chemosensilla by immunocytochemistry; its affinity to some odorants was measured.</description><subject>Animals</subject><subject>Arthropod Antennae - physiology</subject><subject>Arthropod Proteins - genetics</subject><subject>Arthropod Proteins - metabolism</subject><subject>Arthropoda</subject><subject>Female</subject><subject>Haller’s organ</subject><subject>Ixodes - genetics</subject><subject>Ixodes - growth & development</subject><subject>Ixodes - physiology</subject><subject>Ixodes ricinus</subject><subject>Ixodidae</subject><subject>Male</subject><subject>Nymph - growth & development</subject><subject>Olfaction</subject><subject>Proteome</subject><subject>Proteomics</subject><subject>Receptors, Odorant - genetics</subject><subject>Receptors, Odorant - metabolism</subject><subject>Soluble olfactory proteins</subject><subject>Ticks</subject><issn>0965-1748</issn><issn>1879-0240</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1v1DAURa0KRIeBP8ACeckmwZ9JjNigqqWVKsGCri375aV4mMTFL0HMvyejKSwrNu--xbl3cRh7I0UthWze7-oUx1ir9a-Fq4UwZ2wju9ZVQhnxjG2Ea2wlW9Ods5dEO7ESxrYv2LlqG6etbDbs7mvJM-YxAQ9T2B8oEc8Dh0BzLjximPic4Ae_-Z17JF4SpGmhDzzwIcOyshOH7zhmwolyOfBc7sNEr9jzIewJXz_mlt1dXX67uK5uv3y-ufh0W4Hu3FwNog1RuRhNVEPTNyqETmsYXECjlA1RK0Aro3DaaBO0DdC00AJIEaRVg96yd6fdh5J_LkizHxMB7vdhwryQl51utbJCyP9BrTadXe-WqRMKJRMVHPxDSWMoBy-FP5r3O38074_mvXB-9bqW3j7uL3HE_l_lr-oV-HgCcBXyK2HxBAknwD4VhNn3OT21_wcTAZSo</recordid><startdate>201611</startdate><enddate>201611</enddate><creator>Iovinella, Immacolata</creator><creator>Ban, Liping</creator><creator>Song, Limei</creator><creator>Pelosi, Paolo</creator><creator>Dani, Francesca Romana</creator><general>Elsevier 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>7X8</scope><scope>7QR</scope><scope>7SS</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><orcidid>https://orcid.org/0000-0002-2939-2103</orcidid></search><sort><creationdate>201611</creationdate><title>Proteomic analysis of castor bean tick Ixodes ricinus: a focus on chemosensory organs</title><author>Iovinella, Immacolata ; Ban, Liping ; Song, Limei ; Pelosi, Paolo ; Dani, Francesca Romana</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-f07ab29bb4b2f6d62aa833cf9ae4225ab32ce51b093434a35ac67c7cc10a152f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Animals</topic><topic>Arthropod Antennae - physiology</topic><topic>Arthropod Proteins - genetics</topic><topic>Arthropod Proteins - metabolism</topic><topic>Arthropoda</topic><topic>Female</topic><topic>Haller’s organ</topic><topic>Ixodes - genetics</topic><topic>Ixodes - growth & development</topic><topic>Ixodes - physiology</topic><topic>Ixodes ricinus</topic><topic>Ixodidae</topic><topic>Male</topic><topic>Nymph - growth & development</topic><topic>Olfaction</topic><topic>Proteome</topic><topic>Proteomics</topic><topic>Receptors, Odorant - genetics</topic><topic>Receptors, Odorant - metabolism</topic><topic>Soluble olfactory proteins</topic><topic>Ticks</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Iovinella, Immacolata</creatorcontrib><creatorcontrib>Ban, Liping</creatorcontrib><creatorcontrib>Song, Limei</creatorcontrib><creatorcontrib>Pelosi, Paolo</creatorcontrib><creatorcontrib>Dani, Francesca Romana</creatorcontrib><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>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Insect biochemistry and molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Iovinella, Immacolata</au><au>Ban, Liping</au><au>Song, Limei</au><au>Pelosi, Paolo</au><au>Dani, Francesca Romana</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteomic analysis of castor bean tick Ixodes ricinus: a focus on chemosensory organs</atitle><jtitle>Insect biochemistry and molecular biology</jtitle><addtitle>Insect Biochem Mol Biol</addtitle><date>2016-11</date><risdate>2016</risdate><volume>78</volume><spage>58</spage><epage>68</epage><pages>58-68</pages><issn>0965-1748</issn><eissn>1879-0240</eissn><abstract>In arthropods, the large majority of studies on olfaction have been focused on insects, where most of the proteins involved have been identified. In particular, chemosensing in insects relies on two families of membrane receptors, olfactory/gustatory receptors (ORs/GRs) and ionotropic receptors (IRs), and two classes of soluble proteins, odorant-binding proteins (OBPs) and chemosensory proteins (CSPs). In other arthropods, such as ticks and mites, only IRs have been identified, while genes encoding for OBPs and CSPs are absent. A third class of soluble proteins, called Niemann-Pick C2 (NPC2) has been suggested as potential carrier for semiochemicals both in insects and other arthropods.
Here we report the results of a proteomic analysis on olfactory organs (Haller's organ and palps) and control tissues of the tick Ixodes ricinus, and of immunostaining experiments targeting NPC2s. Adopting different extraction and proteomic approaches, we identified a large number of proteins, and highlighted those differentially expressed. None of the 13 NPC2s known for this species was found. On the other hand, using immunocytochemistry, we detected reaction against one NPC2 in the Haller's organ and palp sensilla. We hypothesized that the low concentration of such proteins in the tick's tissues could possibly explain the discrepant results. In ligand-binding assays the corresponding recombinant NPC2 showed good affinity to the fluorescent probe N-phenylnaphthylamine and to few organic compounds, supporting a putative role of NPC2s as odorant carriers.
[Display omitted]
•In insects soluble olfactory proteins are widely studied, while proteins with similar functions are unknown in Acari.•We hypothesized that Niemann Pick C2 proteins (NPC2) act as odorant carriers in tick chemosensilla.•We performed a proteomic study of chemosensory organs of the tick Ixodes ricinus to search for soluble olfactory proteins.•A member of NPC2 proteins was detected in chemosensilla by immunocytochemistry; its affinity to some odorants was measured.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>27693516</pmid><doi>10.1016/j.ibmb.2016.09.004</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0002-2939-2103</orcidid></addata></record> |
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subjects | Animals Arthropod Antennae - physiology Arthropod Proteins - genetics Arthropod Proteins - metabolism Arthropoda Female Haller’s organ Ixodes - genetics Ixodes - growth & development Ixodes - physiology Ixodes ricinus Ixodidae Male Nymph - growth & development Olfaction Proteome Proteomics Receptors, Odorant - genetics Receptors, Odorant - metabolism Soluble olfactory proteins Ticks |
title | Proteomic analysis of castor bean tick Ixodes ricinus: a focus on chemosensory organs |
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