| Antibacterial and proteolytic activity in venom from the endoparasitic wasp Pimpla hypochondriaca (Hymenoptera: Ichneumonidae). | |
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MedLine Citation:
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PMID: 14511827 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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M P Dani; E H Richards; R E Isaac; J P Edwards |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of insect physiology Volume: 49 ISSN: 0022-1910 ISO Abbreviation: J. Insect Physiol. Publication Date: 2003 Oct |
Date Detail:
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Created Date: 2003-09-26 Completed Date: 2004-01-20 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 2985080R Medline TA: J Insect Physiol Country: England |
Other Details:
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Languages: eng Pagination: 945-54 Citation Subset: IM |
Affiliation:
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Central Science Laboratory, Sand Hutton, York YO41 1LZ, UK. p.dani@csl.gov.uk |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Aminopeptidases
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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:
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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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