Toxic polypeptides of the hydra—a bioinformatic approach to cnidarian allomones
Cnidarians such as hydrae and sea anemones are sessile, predatory, soft bodied animals which depend on offensive and defensive allomones for prey capture and survival. These allomones are distributed throughout the entire organism both in specialized stinging cells (nematocytes) and in the body tiss...
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Veröffentlicht in: | Toxicon (Oxford) 2005-06, Vol.45 (7), p.865-879 |
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creator | Sher, Daniel Knebel, Alin Bsor, Tamar Nesher, Nir Tal, Tzachy Morgenstern, David Cohen, Eran Fishman, Yelena Zlotkin, Eliahu |
description | Cnidarians such as hydrae and sea anemones are sessile, predatory, soft bodied animals which depend on offensive and defensive allomones for prey capture and survival. These allomones are distributed throughout the entire organism both in specialized stinging cells (nematocytes) and in the body tissues. The cnidarian allomonal system is composed of neurotoxins, cytolysins and toxic phospholipapses.
The present bioinformatic survey was motivated by the fact that while hydrae are the most studied model cnidarian, little is known about their allomones. A large-scale EST database from
Hydra magnipapillata was searched for orthologs of known cnidarian allomones, as well as for allomones found in other venomous organisms.
We show that the hydrae express orthologs of cnidarian phospholipase A2 toxins and cytolysins belonging to the actinoporin family, but could not find orthologs of the ‘classic’ short chain neurotoxins affecting sodium and potassium conductance. Hydrae also express proteins similar to elapid-like phospholipases, CRISP proteins, Prokineticin-like polypeptides and toxic deoxyribonucleases. Our results illustrate a high level of complexity in the hydra allomonal system, suggest that several toxins represent a basal component of all cnidarian allomones, and raise the intriguing possibility that similar proteins may fulfill both endogenous and allomonal roles in cnidaria. |
doi_str_mv | 10.1016/j.toxicon.2005.02.004 |
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The present bioinformatic survey was motivated by the fact that while hydrae are the most studied model cnidarian, little is known about their allomones. A large-scale EST database from
Hydra magnipapillata was searched for orthologs of known cnidarian allomones, as well as for allomones found in other venomous organisms.
We show that the hydrae express orthologs of cnidarian phospholipase A2 toxins and cytolysins belonging to the actinoporin family, but could not find orthologs of the ‘classic’ short chain neurotoxins affecting sodium and potassium conductance. Hydrae also express proteins similar to elapid-like phospholipases, CRISP proteins, Prokineticin-like polypeptides and toxic deoxyribonucleases. Our results illustrate a high level of complexity in the hydra allomonal system, suggest that several toxins represent a basal component of all cnidarian allomones, and raise the intriguing possibility that similar proteins may fulfill both endogenous and allomonal roles in cnidaria.</description><identifier>ISSN: 0041-0101</identifier><identifier>EISSN: 1879-3150</identifier><identifier>DOI: 10.1016/j.toxicon.2005.02.004</identifier><identifier>PMID: 15904682</identifier><identifier>CODEN: TOXIA6</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Actinoporin ; Allomone ; Amino Acid Sequence ; Animal poisons toxicology. Antivenoms ; Animals ; Biological and medical sciences ; Cnidaria ; Cnidarian Venoms - genetics ; Computational Biology ; CRISP ; Databases, Protein ; Expressed Sequence Tags ; Hydra ; Hydra - genetics ; Hydra - metabolism ; Hydra magnipapillata ; Marine ; Medical sciences ; Nematocyst ; Neurotoxin ; Peptides ; Pheromones - genetics ; Phospholipase ; Phospholipases A - metabolism ; Phospholipases A2 ; Prokineticin ; Toxicology ; Venom</subject><ispartof>Toxicon (Oxford), 2005-06, Vol.45 (7), p.865-879</ispartof><rights>2005 Elsevier Ltd</rights><rights>2005 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c424t-a280c14820dd53e0bc9135177fcf431a7d7f93532b512ee151ea8f31f959c58e3</citedby><cites>FETCH-LOGICAL-c424t-a280c14820dd53e0bc9135177fcf431a7d7f93532b512ee151ea8f31f959c58e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0041010105000553$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16837584$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15904682$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sher, Daniel</creatorcontrib><creatorcontrib>Knebel, Alin</creatorcontrib><creatorcontrib>Bsor, Tamar</creatorcontrib><creatorcontrib>Nesher, Nir</creatorcontrib><creatorcontrib>Tal, Tzachy</creatorcontrib><creatorcontrib>Morgenstern, David</creatorcontrib><creatorcontrib>Cohen, Eran</creatorcontrib><creatorcontrib>Fishman, Yelena</creatorcontrib><creatorcontrib>Zlotkin, Eliahu</creatorcontrib><title>Toxic polypeptides of the hydra—a bioinformatic approach to cnidarian allomones</title><title>Toxicon (Oxford)</title><addtitle>Toxicon</addtitle><description>Cnidarians such as hydrae and sea anemones are sessile, predatory, soft bodied animals which depend on offensive and defensive allomones for prey capture and survival. These allomones are distributed throughout the entire organism both in specialized stinging cells (nematocytes) and in the body tissues. The cnidarian allomonal system is composed of neurotoxins, cytolysins and toxic phospholipapses.
The present bioinformatic survey was motivated by the fact that while hydrae are the most studied model cnidarian, little is known about their allomones. A large-scale EST database from
Hydra magnipapillata was searched for orthologs of known cnidarian allomones, as well as for allomones found in other venomous organisms.
We show that the hydrae express orthologs of cnidarian phospholipase A2 toxins and cytolysins belonging to the actinoporin family, but could not find orthologs of the ‘classic’ short chain neurotoxins affecting sodium and potassium conductance. Hydrae also express proteins similar to elapid-like phospholipases, CRISP proteins, Prokineticin-like polypeptides and toxic deoxyribonucleases. Our results illustrate a high level of complexity in the hydra allomonal system, suggest that several toxins represent a basal component of all cnidarian allomones, and raise the intriguing possibility that similar proteins may fulfill both endogenous and allomonal roles in cnidaria.</description><subject>Actinoporin</subject><subject>Allomone</subject><subject>Amino Acid Sequence</subject><subject>Animal poisons toxicology. Antivenoms</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cnidaria</subject><subject>Cnidarian Venoms - genetics</subject><subject>Computational Biology</subject><subject>CRISP</subject><subject>Databases, Protein</subject><subject>Expressed Sequence Tags</subject><subject>Hydra</subject><subject>Hydra - genetics</subject><subject>Hydra - metabolism</subject><subject>Hydra magnipapillata</subject><subject>Marine</subject><subject>Medical sciences</subject><subject>Nematocyst</subject><subject>Neurotoxin</subject><subject>Peptides</subject><subject>Pheromones - genetics</subject><subject>Phospholipase</subject><subject>Phospholipases A - metabolism</subject><subject>Phospholipases A2</subject><subject>Prokineticin</subject><subject>Toxicology</subject><subject>Venom</subject><issn>0041-0101</issn><issn>1879-3150</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMFq3DAQhkVJabZpH6HFl_RmZyRZtnwKIaRNIVAKyVlopRGrxbYcyRuytzxEn7BPEi1ryDGngeH7_xk-Qr5RqCjQ5mJbzeHZmzBWDEBUwCqA-gNZUdl2JacCTsgqb2gJGT8ln1PaAgCXXfOJnFLRQd1ItiJ_7w8txRT6_YTT7C2mIrhi3mCx2duo_7_808XaBz-6EAc9Z1ZPUwzabIo5FGb0Vkevx0L3fRjCiOkL-eh0n_DrMs_Iw8-b--vb8u7Pr9_XV3elqVk9l5pJMLSWDKwVHGFtOsoFbVtnXM2pbm3rOi44WwvKEKmgqKXj1HWiM0IiPyM_jr35m8cdplkNPhnsez1i2CXFsiXGaJNBcQRNDClFdGqKftBxryiog0u1VYtLdXCpgKlsLue-Lwd26wHtW2qRl4HzBdDJ6N5FPRqf3rhG8lbIQ9HlkcOs48ljVMl4HA1aH9HMygb_ziuv5bWWZw</recordid><startdate>20050601</startdate><enddate>20050601</enddate><creator>Sher, Daniel</creator><creator>Knebel, Alin</creator><creator>Bsor, Tamar</creator><creator>Nesher, Nir</creator><creator>Tal, Tzachy</creator><creator>Morgenstern, David</creator><creator>Cohen, Eran</creator><creator>Fishman, Yelena</creator><creator>Zlotkin, Eliahu</creator><general>Elsevier Ltd</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>7QO</scope><scope>7TN</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>H97</scope><scope>L.G</scope><scope>P64</scope></search><sort><creationdate>20050601</creationdate><title>Toxic polypeptides of the hydra—a bioinformatic approach to cnidarian allomones</title><author>Sher, Daniel ; Knebel, Alin ; Bsor, Tamar ; Nesher, Nir ; Tal, Tzachy ; Morgenstern, David ; Cohen, Eran ; Fishman, Yelena ; Zlotkin, Eliahu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c424t-a280c14820dd53e0bc9135177fcf431a7d7f93532b512ee151ea8f31f959c58e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Actinoporin</topic><topic>Allomone</topic><topic>Amino Acid Sequence</topic><topic>Animal poisons toxicology. Antivenoms</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cnidaria</topic><topic>Cnidarian Venoms - genetics</topic><topic>Computational Biology</topic><topic>CRISP</topic><topic>Databases, Protein</topic><topic>Expressed Sequence Tags</topic><topic>Hydra</topic><topic>Hydra - genetics</topic><topic>Hydra - metabolism</topic><topic>Hydra magnipapillata</topic><topic>Marine</topic><topic>Medical sciences</topic><topic>Nematocyst</topic><topic>Neurotoxin</topic><topic>Peptides</topic><topic>Pheromones - genetics</topic><topic>Phospholipase</topic><topic>Phospholipases A - metabolism</topic><topic>Phospholipases A2</topic><topic>Prokineticin</topic><topic>Toxicology</topic><topic>Venom</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sher, Daniel</creatorcontrib><creatorcontrib>Knebel, Alin</creatorcontrib><creatorcontrib>Bsor, Tamar</creatorcontrib><creatorcontrib>Nesher, Nir</creatorcontrib><creatorcontrib>Tal, Tzachy</creatorcontrib><creatorcontrib>Morgenstern, David</creatorcontrib><creatorcontrib>Cohen, Eran</creatorcontrib><creatorcontrib>Fishman, Yelena</creatorcontrib><creatorcontrib>Zlotkin, Eliahu</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>Biotechnology Research Abstracts</collection><collection>Oceanic Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Toxicon (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sher, Daniel</au><au>Knebel, Alin</au><au>Bsor, Tamar</au><au>Nesher, Nir</au><au>Tal, Tzachy</au><au>Morgenstern, David</au><au>Cohen, Eran</au><au>Fishman, Yelena</au><au>Zlotkin, Eliahu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Toxic polypeptides of the hydra—a bioinformatic approach to cnidarian allomones</atitle><jtitle>Toxicon (Oxford)</jtitle><addtitle>Toxicon</addtitle><date>2005-06-01</date><risdate>2005</risdate><volume>45</volume><issue>7</issue><spage>865</spage><epage>879</epage><pages>865-879</pages><issn>0041-0101</issn><eissn>1879-3150</eissn><coden>TOXIA6</coden><abstract>Cnidarians such as hydrae and sea anemones are sessile, predatory, soft bodied animals which depend on offensive and defensive allomones for prey capture and survival. These allomones are distributed throughout the entire organism both in specialized stinging cells (nematocytes) and in the body tissues. The cnidarian allomonal system is composed of neurotoxins, cytolysins and toxic phospholipapses.
The present bioinformatic survey was motivated by the fact that while hydrae are the most studied model cnidarian, little is known about their allomones. A large-scale EST database from
Hydra magnipapillata was searched for orthologs of known cnidarian allomones, as well as for allomones found in other venomous organisms.
We show that the hydrae express orthologs of cnidarian phospholipase A2 toxins and cytolysins belonging to the actinoporin family, but could not find orthologs of the ‘classic’ short chain neurotoxins affecting sodium and potassium conductance. Hydrae also express proteins similar to elapid-like phospholipases, CRISP proteins, Prokineticin-like polypeptides and toxic deoxyribonucleases. Our results illustrate a high level of complexity in the hydra allomonal system, suggest that several toxins represent a basal component of all cnidarian allomones, and raise the intriguing possibility that similar proteins may fulfill both endogenous and allomonal roles in cnidaria.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>15904682</pmid><doi>10.1016/j.toxicon.2005.02.004</doi><tpages>15</tpages></addata></record> |
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subjects | Actinoporin Allomone Amino Acid Sequence Animal poisons toxicology. Antivenoms Animals Biological and medical sciences Cnidaria Cnidarian Venoms - genetics Computational Biology CRISP Databases, Protein Expressed Sequence Tags Hydra Hydra - genetics Hydra - metabolism Hydra magnipapillata Marine Medical sciences Nematocyst Neurotoxin Peptides Pheromones - genetics Phospholipase Phospholipases A - metabolism Phospholipases A2 Prokineticin Toxicology Venom |
title | Toxic polypeptides of the hydra—a bioinformatic approach to cnidarian allomones |
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