Document Detail


Antibacterial and proteolytic activity in venom from the endoparasitic wasp Pimpla hypochondriaca (Hymenoptera: Ichneumonidae).
MedLine Citation:
PMID:  14511827     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Venom from the endoparasitic wasp, Pimpla hypochondriaca, is composed of a mixture of high and low molecular weight proteins, possesses phenoloxidase activity, has immunosuppressive properties, and induces paralysis in several insect species. In the present study we demonstrate that P. hypochondriaca venom also contains antibacterial and proteolytic activity. Antibacterial activity was detected against the Gram-negative bacteria Escherichia coli and Xanthamonas campestris but not against Pseudomonas syringae nor against two Gram-positive bacteria, Bacillus cereus and Bacillus subtilis. Endopeptidase and aminopeptidase activity in venom was detected using the synthetic fluorogenic substrates N-t-BOC-Phe-Ser-Arg-AMC, Arg-AMC and Leu-Arg. The aminopeptidase activity towards Arg-AMC was sensitive to amastatin (70% inhibition), an aminopeptidase inhibitor. Angiotensin-converting enzyme (ACE)-like enzyme activity was detected, by reverse-phase HPLC using the synthetic tripeptide Hip-His-Leu as a substrate. This activity was sensitive to captopril, an ACE inhibitor (IC(50) 3.8 x 10(-8) M). Using an antiserum raised against recombinant Drosophila melanogaster ACE-like enzyme, (rAnce), Western blot analysis revealed an immunoreactive protein, with a molecular weight estimate of 74 kDa, in P. hypochondriaca venom. The possibility that the endopeptidase, aminopeptidase and ACE are involved in the processing of peptide precursors in the venom sac is discussed.
Authors:
M P Dani; E H Richards; R E Isaac; J P Edwards
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of insect physiology     Volume:  49     ISSN:  0022-1910     ISO Abbreviation:  J. Insect Physiol.     Publication Date:  2003 Oct 
Date Detail:
Created Date:  2003-09-26     Completed Date:  2004-01-20     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985080R     Medline TA:  J Insect Physiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  945-54     Citation Subset:  IM    
Affiliation:
Central Science Laboratory, Sand Hutton, York YO41 1LZ, UK. p.dani@csl.gov.uk
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MeSH Terms
Descriptor/Qualifier:
Aminopeptidases / metabolism
Angiotensin-Converting Enzyme Inhibitors / pharmacology
Animals
Anti-Bacterial Agents / pharmacology*
Arthropod Venoms / chemistry,  metabolism,  pharmacology*
Bacillus cereus / drug effects
Bacillus subtilis / drug effects
Captopril
Dipeptidases / metabolism
Endopeptidases / metabolism
Escherichia coli / drug effects
Female
Hymenoptera / enzymology,  metabolism*
Microbial Sensitivity Tests
Peptides / pharmacology
Peptidyl-Dipeptidase A / metabolism
Pseudomonas syringae / drug effects
Xanthomonas campestris / drug effects
Chemical
Reg. No./Substance:
0/Angiotensin-Converting Enzyme Inhibitors; 0/Anti-Bacterial Agents; 0/Arthropod Venoms; 0/Peptides; 62571-86-2/Captopril; 67655-94-1/amastatin; EC 3.4.-/Endopeptidases; EC 3.4.11.-/Aminopeptidases; EC 3.4.13.-/Dipeptidases; EC 3.4.15.1/Peptidyl-Dipeptidase A

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


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