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Transcripts involved in hemostasis: Exploring salivary complexes from Haementeria vizottoi leeches through transcriptomics, phylogenetic studies and structural features
Throughout evolution, parasites have adapted in order to successfully intervene in the host defense, producing specific peptides and proteins. Interestingly, these peptides and proteins have been exploited as potential drug candidates against several diseases. Furthermore, biotechnology studies and...
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Published in: | Toxicon (Oxford) 2015-11, Vol.106, p.20-29 |
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creator | Amorim, Adriane Michele Xavier Prado de Oliveira, Ursula Castro Faria, Fernanda Pasqualoto, Kerly Fernanda Mesquita Junqueira-de-Azevedo, Inácio de L.M. Chudzinski-Tavassi, Ana Marisa |
description | Throughout evolution, parasites have adapted in order to successfully intervene in the host defense, producing specific peptides and proteins. Interestingly, these peptides and proteins have been exploited as potential drug candidates against several diseases. Furthermore, biotechnology studies and cDNA libraries have remarkably contributed to identify potentially bioactive molecules. In this regard, herein, a cDNA library of salivary complexes from Haementeria vizottoi leeches was constructed, the transcriptome was characterized and a phylogenetic analysis was performed considering antistasin-like and antiplatelet-like proteins. Hundred twenty three transcripts were identified coding for putative proteins involved in animal feeding (representing about 10% of the expression level). These sequences showed similarities with myohemerythrins, carbonic anhydrases, anticoagulants, antimicrobials, proteases and protease inhibitors. The phylogenetic analysis, regarding antistasin-like and antiplatetlet-like proteins, revealed two main clades in the Rhynchobdellida leeches. As expected, the sequences from H. vizottoi have presented high similarities with those types of proteins. Thus, our findings could be helpful not only to identify new coagulation inhibitors, but also to better understand the biological composition of the salivary complexes.
•Haementeria vizottoi transcriptome revealed putative molecular components involved in hemostasis.•Detection of 123 molecules probably involved in animal feeding.•Identification of new putative coagulation inhibitors as antistasin-like and antiplatelet-like proteins.•Structurally, the Arg34Gly substitution may change the H. vizottoi antistasin-like function. |
doi_str_mv | 10.1016/j.toxicon.2015.09.002 |
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•Haementeria vizottoi transcriptome revealed putative molecular components involved in hemostasis.•Detection of 123 molecules probably involved in animal feeding.•Identification of new putative coagulation inhibitors as antistasin-like and antiplatelet-like proteins.•Structurally, the Arg34Gly substitution may change the H. vizottoi antistasin-like function.</description><identifier>ISSN: 0041-0101</identifier><identifier>EISSN: 1879-3150</identifier><identifier>DOI: 10.1016/j.toxicon.2015.09.002</identifier><identifier>PMID: 26363292</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Analogies ; Animals ; Anticoagulants ; Anticoagulants - chemistry ; Anticoagulants - isolation & purification ; Carbonic anhydrase ; Coagulation inhibitors ; Computational Biology ; Diseases ; Feeding Behavior ; Gene Expression Profiling ; Gene Library ; Hemostasis ; Hirudinea ; Leeches ; Leeches - chemistry ; Leeches - genetics ; Leeches - physiology ; Libraries ; Models, Molecular ; Peptides ; Phylogenetic studies ; Phylogeny ; Platelet Aggregation Inhibitors - chemistry ; Platelet Aggregation Inhibitors - isolation & purification ; Platelet inhibitors ; Proteins ; Rhynchobdellida ; RNA, Messenger - metabolism ; Salivary Glands - chemistry ; Sequence Alignment ; Sequence Analysis, Protein ; Transcriptome</subject><ispartof>Toxicon (Oxford), 2015-11, Vol.106, p.20-29</ispartof><rights>2015 Elsevier Ltd</rights><rights>Copyright © 2015 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c431t-be0824a6108ec98002fa9c6a0a115e2a0d5147b7277d98eff831cc09db24ad163</citedby><cites>FETCH-LOGICAL-c431t-be0824a6108ec98002fa9c6a0a115e2a0d5147b7277d98eff831cc09db24ad163</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26363292$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Amorim, Adriane Michele Xavier Prado</creatorcontrib><creatorcontrib>de Oliveira, Ursula Castro</creatorcontrib><creatorcontrib>Faria, Fernanda</creatorcontrib><creatorcontrib>Pasqualoto, Kerly Fernanda Mesquita</creatorcontrib><creatorcontrib>Junqueira-de-Azevedo, Inácio de L.M.</creatorcontrib><creatorcontrib>Chudzinski-Tavassi, Ana Marisa</creatorcontrib><title>Transcripts involved in hemostasis: Exploring salivary complexes from Haementeria vizottoi leeches through transcriptomics, phylogenetic studies and structural features</title><title>Toxicon (Oxford)</title><addtitle>Toxicon</addtitle><description>Throughout evolution, parasites have adapted in order to successfully intervene in the host defense, producing specific peptides and proteins. Interestingly, these peptides and proteins have been exploited as potential drug candidates against several diseases. Furthermore, biotechnology studies and cDNA libraries have remarkably contributed to identify potentially bioactive molecules. In this regard, herein, a cDNA library of salivary complexes from Haementeria vizottoi leeches was constructed, the transcriptome was characterized and a phylogenetic analysis was performed considering antistasin-like and antiplatelet-like proteins. Hundred twenty three transcripts were identified coding for putative proteins involved in animal feeding (representing about 10% of the expression level). These sequences showed similarities with myohemerythrins, carbonic anhydrases, anticoagulants, antimicrobials, proteases and protease inhibitors. The phylogenetic analysis, regarding antistasin-like and antiplatetlet-like proteins, revealed two main clades in the Rhynchobdellida leeches. As expected, the sequences from H. vizottoi have presented high similarities with those types of proteins. Thus, our findings could be helpful not only to identify new coagulation inhibitors, but also to better understand the biological composition of the salivary complexes.
•Haementeria vizottoi transcriptome revealed putative molecular components involved in hemostasis.•Detection of 123 molecules probably involved in animal feeding.•Identification of new putative coagulation inhibitors as antistasin-like and antiplatelet-like proteins.•Structurally, the Arg34Gly substitution may change the H. vizottoi antistasin-like function.</description><subject>Analogies</subject><subject>Animals</subject><subject>Anticoagulants</subject><subject>Anticoagulants - chemistry</subject><subject>Anticoagulants - isolation & purification</subject><subject>Carbonic anhydrase</subject><subject>Coagulation inhibitors</subject><subject>Computational Biology</subject><subject>Diseases</subject><subject>Feeding Behavior</subject><subject>Gene Expression Profiling</subject><subject>Gene Library</subject><subject>Hemostasis</subject><subject>Hirudinea</subject><subject>Leeches</subject><subject>Leeches - chemistry</subject><subject>Leeches - genetics</subject><subject>Leeches - physiology</subject><subject>Libraries</subject><subject>Models, Molecular</subject><subject>Peptides</subject><subject>Phylogenetic studies</subject><subject>Phylogeny</subject><subject>Platelet Aggregation Inhibitors - chemistry</subject><subject>Platelet Aggregation Inhibitors - isolation & purification</subject><subject>Platelet inhibitors</subject><subject>Proteins</subject><subject>Rhynchobdellida</subject><subject>RNA, Messenger - metabolism</subject><subject>Salivary Glands - chemistry</subject><subject>Sequence Alignment</subject><subject>Sequence Analysis, Protein</subject><subject>Transcriptome</subject><issn>0041-0101</issn><issn>1879-3150</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><recordid>eNqNkc1u1DAUhSMEotPCI4C8ZEHCtfNrNqiqWopUiU1ZWx77ZuKREwfbiaY8EY-JRzN0CyufxXfusc7JsncUCgq0-bQvojsY5aaCAa0L4AUAe5FtaNfyvKQ1vMw2ABXNIeEX2WUIewAoO968zi5YUzYl42yT_X70cgrKmzkGYqbV2RV1EmTA0YUogwmfye1hts6baUeCtGaV_okoN84WDxhI791I7iWOOEX0RpLV_HIxOkMsohoSEQfvlt1A4nOUG40KH8k8PFm3wwmjUSTERZtEy0kn7RcVFy8t6VEmgeFN9qqXNuDb83uV_bi7fby5zx--f_12c_2Qq6qkMd8idKySDYUOFe9SJ73kqpEgKa2RSdA1rdpty9pW8w77viupUsD1Nrk0bcqr7MPp7uzdzwVDFKMJCq2VE7olCNo2jAKvWvYfKGsb3pXdEa1PqPIuBI-9mL0ZU5GCgjjuKfbivKc47imAi_T35Ht_jli2I-pn198BE_DlBGDqZDXoRVAGJ4XaeFRRaGf-EfEHDby6JQ</recordid><startdate>20151101</startdate><enddate>20151101</enddate><creator>Amorim, Adriane Michele Xavier Prado</creator><creator>de Oliveira, Ursula Castro</creator><creator>Faria, Fernanda</creator><creator>Pasqualoto, Kerly Fernanda Mesquita</creator><creator>Junqueira-de-Azevedo, Inácio de L.M.</creator><creator>Chudzinski-Tavassi, Ana Marisa</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>7U7</scope><scope>C1K</scope><scope>8FD</scope><scope>FR3</scope><scope>KR7</scope></search><sort><creationdate>20151101</creationdate><title>Transcripts involved in hemostasis: Exploring salivary complexes from Haementeria vizottoi leeches through transcriptomics, phylogenetic studies and structural features</title><author>Amorim, Adriane Michele Xavier Prado ; de Oliveira, Ursula Castro ; Faria, Fernanda ; Pasqualoto, Kerly Fernanda Mesquita ; Junqueira-de-Azevedo, Inácio de L.M. ; Chudzinski-Tavassi, Ana Marisa</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c431t-be0824a6108ec98002fa9c6a0a115e2a0d5147b7277d98eff831cc09db24ad163</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Analogies</topic><topic>Animals</topic><topic>Anticoagulants</topic><topic>Anticoagulants - chemistry</topic><topic>Anticoagulants - isolation & purification</topic><topic>Carbonic anhydrase</topic><topic>Coagulation inhibitors</topic><topic>Computational Biology</topic><topic>Diseases</topic><topic>Feeding Behavior</topic><topic>Gene Expression Profiling</topic><topic>Gene Library</topic><topic>Hemostasis</topic><topic>Hirudinea</topic><topic>Leeches</topic><topic>Leeches - chemistry</topic><topic>Leeches - genetics</topic><topic>Leeches - physiology</topic><topic>Libraries</topic><topic>Models, Molecular</topic><topic>Peptides</topic><topic>Phylogenetic studies</topic><topic>Phylogeny</topic><topic>Platelet Aggregation Inhibitors - chemistry</topic><topic>Platelet Aggregation Inhibitors - isolation & purification</topic><topic>Platelet inhibitors</topic><topic>Proteins</topic><topic>Rhynchobdellida</topic><topic>RNA, Messenger - metabolism</topic><topic>Salivary Glands - chemistry</topic><topic>Sequence Alignment</topic><topic>Sequence Analysis, Protein</topic><topic>Transcriptome</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Amorim, Adriane Michele Xavier Prado</creatorcontrib><creatorcontrib>de Oliveira, Ursula Castro</creatorcontrib><creatorcontrib>Faria, Fernanda</creatorcontrib><creatorcontrib>Pasqualoto, Kerly Fernanda Mesquita</creatorcontrib><creatorcontrib>Junqueira-de-Azevedo, Inácio de L.M.</creatorcontrib><creatorcontrib>Chudzinski-Tavassi, Ana Marisa</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Civil Engineering Abstracts</collection><jtitle>Toxicon (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Amorim, Adriane Michele Xavier Prado</au><au>de Oliveira, Ursula Castro</au><au>Faria, Fernanda</au><au>Pasqualoto, Kerly Fernanda Mesquita</au><au>Junqueira-de-Azevedo, Inácio de L.M.</au><au>Chudzinski-Tavassi, Ana Marisa</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transcripts involved in hemostasis: Exploring salivary complexes from Haementeria vizottoi leeches through transcriptomics, phylogenetic studies and structural features</atitle><jtitle>Toxicon (Oxford)</jtitle><addtitle>Toxicon</addtitle><date>2015-11-01</date><risdate>2015</risdate><volume>106</volume><spage>20</spage><epage>29</epage><pages>20-29</pages><issn>0041-0101</issn><eissn>1879-3150</eissn><abstract>Throughout evolution, parasites have adapted in order to successfully intervene in the host defense, producing specific peptides and proteins. Interestingly, these peptides and proteins have been exploited as potential drug candidates against several diseases. Furthermore, biotechnology studies and cDNA libraries have remarkably contributed to identify potentially bioactive molecules. In this regard, herein, a cDNA library of salivary complexes from Haementeria vizottoi leeches was constructed, the transcriptome was characterized and a phylogenetic analysis was performed considering antistasin-like and antiplatelet-like proteins. Hundred twenty three transcripts were identified coding for putative proteins involved in animal feeding (representing about 10% of the expression level). These sequences showed similarities with myohemerythrins, carbonic anhydrases, anticoagulants, antimicrobials, proteases and protease inhibitors. The phylogenetic analysis, regarding antistasin-like and antiplatetlet-like proteins, revealed two main clades in the Rhynchobdellida leeches. As expected, the sequences from H. vizottoi have presented high similarities with those types of proteins. Thus, our findings could be helpful not only to identify new coagulation inhibitors, but also to better understand the biological composition of the salivary complexes.
•Haementeria vizottoi transcriptome revealed putative molecular components involved in hemostasis.•Detection of 123 molecules probably involved in animal feeding.•Identification of new putative coagulation inhibitors as antistasin-like and antiplatelet-like proteins.•Structurally, the Arg34Gly substitution may change the H. vizottoi antistasin-like function.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>26363292</pmid><doi>10.1016/j.toxicon.2015.09.002</doi><tpages>10</tpages></addata></record> |
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subjects | Analogies Animals Anticoagulants Anticoagulants - chemistry Anticoagulants - isolation & purification Carbonic anhydrase Coagulation inhibitors Computational Biology Diseases Feeding Behavior Gene Expression Profiling Gene Library Hemostasis Hirudinea Leeches Leeches - chemistry Leeches - genetics Leeches - physiology Libraries Models, Molecular Peptides Phylogenetic studies Phylogeny Platelet Aggregation Inhibitors - chemistry Platelet Aggregation Inhibitors - isolation & purification Platelet inhibitors Proteins Rhynchobdellida RNA, Messenger - metabolism Salivary Glands - chemistry Sequence Alignment Sequence Analysis, Protein Transcriptome |
title | Transcripts involved in hemostasis: Exploring salivary complexes from Haementeria vizottoi leeches through transcriptomics, phylogenetic studies and structural features |
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