Document Detail

Toxic polypeptides of the hydra--a bioinformatic approach to cnidarian allomones.
MedLine Citation:
PMID:  15904682     Owner:  NLM     Status:  MEDLINE    
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.
Daniel Sher; Alin Knebel; Tamar Bsor; Nir Nesher; Tzachy Tal; David Morgenstern; Eran Cohen; Yelena Fishman; Eliahu Zlotkin
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2005-03-31
Journal Detail:
Title:  Toxicon : official journal of the International Society on Toxinology     Volume:  45     ISSN:  0041-0101     ISO Abbreviation:  Toxicon     Publication Date:  2005 Jun 
Date Detail:
Created Date:  2005-05-20     Completed Date:  2005-09-16     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  1307333     Medline TA:  Toxicon     Country:  England    
Other Details:
Languages:  eng     Pagination:  865-79     Citation Subset:  IM    
Department of Cell and Animal Biology, Silberman Institute of Life Sciences, Hebrew University, Jerusalem, Israel.
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MeSH Terms
Amino Acid Sequence
Cnidarian Venoms / genetics*
Computational Biology*
Databases, Protein
Expressed Sequence Tags*
Hydra* / genetics,  metabolism
Pheromones / genetics*
Phospholipases A / metabolism
Phospholipases A2
Reg. No./Substance:
0/Cnidarian Venoms; 0/Peptides; 0/Pheromones; EC 3.1.1.-/Phospholipases A; EC A2

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