Document Detail


Three toxins with phospholipase activity isolated from the yellow-legged hornet (Vespa verutina) venom.
MedLine Citation:
PMID:  10484737     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The yellow-legged hornet, Vespa verutina, is widely distributed in both the mountain area and the suburbs of Taiwan and possesses highly toxic venom (LD50=0.02 microl/g mouse). By gel filtration on Fractogel (TSK HW 50f) followed by cation-exchange chromatography on Mono S column, three toxins designated as verutoxin 1, 2a and 2b (VT-1, VT-2a and VT-2b) were isolated from the venom. The toxin VT-1 had a molecular mass of 34,982 Da and an LD50 value of 3.61 microg/g mouse. Toxin VT-2a and 2b were more basic and more toxic than VT-1. VT-2a and 2b were isotoxins with molecular masses differing in only 14 Da (33,360 and 33,374 Da, respectively) and had a similar toxicity in mice (LD50=0.87 microg/g mouse). All three toxins were capable of catalyzing the hydrolysis of emulsified phospholipids and lysophosphatide, but not sphingomyelin. Analysis of the hydrolyzed products (fatty acid and lyso-compound) by a liquid chromatography/mass spectrometer revealed that the toxins liberates fatty acid mainly from the 1-position of the synthetic phospholipid. This result indicates that verutoxins possess phospholipase A1 activity. Toxin VT-1 showed higher phospholipase activity than VT-2a and 2b. However, the latter toxins exhibited much higher direct hemolytic activity toward the mouse red blood cells. Vespid phospholipases are known as one of the three major venom allergens in many species of wasps. Our studies indicate that vespid phospholipases A1, in addition to acting as allergens, possess direct toxic actions that may also cause death in animals. Toxin VT-2a and 2b which possess potent hemolytic activity and high lethality in mice may act as the lethal factor of V. verutina venom.
Authors:
C L Ho; Y L Lin; S F Li
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Toxicon : official journal of the International Society on Toxinology     Volume:  37     ISSN:  0041-0101     ISO Abbreviation:  Toxicon     Publication Date:  1999 Jul 
Date Detail:
Created Date:  1999-09-03     Completed Date:  1999-09-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  1307333     Medline TA:  Toxicon     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  1015-24     Citation Subset:  IM    
Affiliation:
Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei, Taiwan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Chromatography, Gel
Chromatography, Ion Exchange
Fatty Acids / metabolism
Gas Chromatography-Mass Spectrometry
Hemolysis / drug effects*
Mice
Mice, Inbred ICR
Molecular Sequence Data
Phospholipases / chemistry,  toxicity*
Wasp Venoms / enzymology*,  isolation & purification,  toxicity*
Chemical
Reg. No./Substance:
0/Fatty Acids; 0/Wasp Venoms; EC 3.1.-/Phospholipases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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