Antibacterial and proteolytic activity in venom from the endoparasitic wasp Pimpla hypochondriaca (Hymenoptera: Ichneumonidae)

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. hypochondriac...

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Bibliographic Details
Published in:Journal of insect physiology 2003-10, Vol.49 (10), p.945-954
Main Authors: Dani, M.P., Richards, E.H., Isaac, R.E., Edwards, J.P.
Format: Article
Language:English
Subjects:
aminopeptidases
Aminopeptidases - metabolism
Angiotensin I-converting enzyme
Angiotensin-Converting Enzyme Inhibitors - pharmacology
Animals
Anti-Bacterial Agents - pharmacology
Antibacterial activity
antibacterial properties
Arthropod Venoms - chemistry
Arthropod Venoms - metabolism
Arthropod Venoms - pharmacology
Bacillus cereus - drug effects
Bacillus subtilis - drug effects
Captopril
Dipeptidases - metabolism
Endopeptidases - metabolism
enzyme activity
enzyme inhibition
enzyme inhibitors
enzyme substrates
Escherichia coli - drug effects
Female
fractionation
Hymenoptera - enzymology
Hymenoptera - metabolism
Ichneumonidae
immunochemistry
insect biochemistry
Microbial Sensitivity Tests
molecular weight
Parasitoid
parasitoids
peptidases
Peptides - pharmacology
peptidyl-dipeptidase A
Peptidyl-Dipeptidase A - metabolism
phenoloxidase
Pimpla
Pimpla hypochondriaca
Proteases
proteinases
proteolysis
Pseudomonas syringae - drug effects
Venom
venoms
Vespidae
Xanthomonas campestris - drug effects
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Summary: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 Psuedomonas 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 3.8×10 −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.
ISSN:0022-1910
1879-1611
DOI:10.1016/S0022-1910(03)00163-X