Effects of parasitization and envenomation by the endoparasitic Wasp Pimpla turionellae L. (Hymenoptera: Ichneumonidae) on hemolymph protein profile of its host Galleria mellonella L. (Lepidoptera: Pyralidae) (original) (raw)
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2013
The effects of dose-dependent envenomation and by parasitization of Pimpla turionellae L. (Hymenoptera: Ichneumonidae) on the hemolymph protein profile of its host Galleria mellonella L. (Lepidoptera: Pyralidae) were investigated. Hemolymph proteins were analyzed using spectrophotometry and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The gel was subsequently scanned and the optical densities (OD) of the bands were analyzed. The quantities of proteins detected 4, 8, and 24 h post-treatments in hemolymph of parasitized and envenomated host pupae did not differ much when compared with those of controls. Of the seventeen different protein bands detected at a range of 19.6-181.12 kDa in the hemolymph, there were only changes in OD values of bands at 23.418, 24.714, 32.434, 34.811, and 45.385 kDa following envenomation and parasitism. The electrophoretic pattern of hemolymph proteins from venom injected and control groups of larvae did not differ much from that of pupae except for new protein bands detected at 33.823 and 41.553 kDa. However, three bands with 45.385, 99.000, and 126.850 kDa were not detected in larvae. Hemolymph protein quantity remained steady at all time points tested except for increases for some bands at 8 h following envenomation. The amount of 34.811 kDa protein decreased immediately at 8 h postinjection of 0.02 and 0.05 VRE of venom whereas injection all venom doses except 0.1 VRE resulted in an increase in the amount for 41.553 and 43.412 kDa proteins. There were no qualitative changes in term of novel protein bands in the hemolymph of hosts. Therefore, we suggest that host regulation of G. mellonella by parasitism or envenomation of P. turionellae involves quantitative changes in the host plasma proteins but does not lead to the up-regulation of novel proteins.
Turk. J. Biol, 2011
Venom from the endoparasitoid Pimpla turionellae L. (Hymenoptera: Ichneumonidae) contains a mixture of biologically active components, which display potent paralytic, cytotoxic, and cytolytic eff ects towards hosts. Here, we further investigate if parasitism or envenomation by P. turionellae alters total protein of its host Galleria mellonella L. (Lepidoptera: Pyralidae). Various venom concentrations representing doses previously determined to yield host responses yet fall below the calculated LD99 were used for pupae and larvae. Parasitization was only assayed for host pupa since P. turionellae females normally parasitize host prepupae and pupae in nature. Hemolymph total protein concentration remained relatively steady at all doses and at all time points tested in parasitized and venom-injected host pupae and larvae. Th e only exception to this trend was with the highest dose of venom (0.5 VRE) at 24 h for larvae that almost 2 times higher amount of protein were detected with regard to untreated ones. It is likely that the increase in protein concentration in a non-permissive host stage in the present study was induced by venom and/or general injury because the same trend was also observed in null-and PBS-injected larvae. However, neither of the treatments increased the protein concentration of G. mellonella larvae to the same extent that 0.5 VRE injection did, indicating that the increase observed in the latter treatment was not simply the result of wounding or injection of fl uid. Th us, we favor the possibility that stress proteins may play a role in this event. Pimpla turionellae (Hymenoptera: Ichneumonidae) parazitlemesi ve zehir enjeksiyonu sonrası konak Galleria mellonella (Lepidoptera: Pyralidae) hemolenf toplam proteinindeki değişiklikler Özet: Endoparazitoid Pimpla turionellae L. (Hymenoptera: Ichneumonidae) zehiri konak türü üzerinde felç edici, sitotoksik ve sitolitik etkiler gösteren biyolojik olarak aktif bileşenlerin karışımıdır. Bu çalışmada, P. turionellae dişilerinden elde edilen zehir salgısının ve doğal parazitlemenin konak tür, Galleria mellonella L. (Lepidoptera: Pyralidae) hemolenfi toplam protein miktarına etkileri belirlendi. Konak pupa ve larvaları için daha önce tepki verdikleri hesaplanan LD 99 dozu altındaki farklı zehir dozları kullanıldı. P. turionellae dişileri doğada sadece konak prepupa ve
Annals of the Entomological Society of America, 2010
The effects of dose-dependent envenomation by and parasitization of Pimpla turionellae Linnaeus (Hymenoptera: Ichneumonidae) on the ratio of hemolymph free amino acids of the host species Galleria mellonella Linnaeus (Lepidoptera: Pyralidae) pupae and larvae were investigated. Of the seventeen different free amino acids detected in the hemolymph of host pupae and larvae by high performance liquid chromatography, the ratio of free amino acids from parasitized and envenomated host pupae did not differ much when compared with those of unparasitized, null-or PBS-injected controls at different time points post-treatments. The exceptions to this trend were an increase in parasitized host pupae for glutamic acid with regard to other experimental groups at 4 and 8 h and a decrease in parasitized host pupae for leucine with regard to 0.01 and 0.05 VRE at 24 h post-treatments. In contrast to pupae, hemolypmh free amino acids of G. mellonella larvae differed upon venom injection among treatments and at different time points post-treatments. The ratios of alanine and leucine at 8 h and glutamic acid, serine, glycine+glutamine, valine, methionine, and phenylalanine at 24 h post-treatments differed from those of controls in treatment groups. However, there appeared no changes in the ratio of hemolypmh free amino acids in host larvae at 4 h post-treatments. Our study indicated that parasitism and experimental envenomation of G. mellonella by wasps resulted in different effects in the quantity of free amino acids depending on host developmental stage.
The effects of dose-dependent envenomation by and parasitization of Pimpla turionellae Linnaeus (Hymenoptera: Ichneumonidae) on the ratio of hemolymph free amino acids of the host species Galleria mellonella Linnaeus (Lepidoptera: Pyralidae) pupae and larvae were investigated. Of the seventeen different free amino acids detected in the hemolymph of host pupae and larvae by high performance liquid chromatography, the ratio of free amino acids from parasitized and envenomated host pupae did not differ much when compared with those of unparasitized, null-or PBS-injected controls at different time points post-treatments. The exceptions to this trend were an increase in parasitized host pupae for glutamic acid with regard to other experimental groups at 4 and 8 h and a decrease in parasitized host pupae for leucine with regard to 0.01 and 0.05 VRE at 24 h post-treatments. In contrast to pupae, hemolypmh free amino acids of G. mellonella larvae differed upon venom injection among treatmen...
Annals of the Entomological Society of America
Paralytic, cytotoxic, and cytolytic effects of Pimpla turionellae L. (Hymenoptera: Ichneumonidae) venom has previously been shown toward its natural host Galleria mellonella L. (Lepidoptera: Pyralidae). The effects of P. turionellae venom and parasitization on hemolymph carbohydrate and lipid levels of the host larvae and pupae were studied in the present study for a more complete understanding of metabolic alterations that accompany parasitism. Larval and pupal carbohydrate levels were increased at 4 and 24 h posttreatment at lower venom doses. Venom-induced reductions were only observed at the highest venom dose in larval stage at two time points posttreatment. Parasitization reduced the pupal hemolymph carbohydrate at 24 h postoviposition compared to untreated control. The magnitude of differences in lipid content of larva was not dose dependent and fluctuated among treatments. However, in pupal stage venom caused an elevation in total lipid content except for 0.05 VRE. Total lipid amounts of G. mellonella pupae were reduced by > 50% postparasitization. We conclude that experimental envenomation and parasitization of G. mellonella by the idiobiont endoparasitoid P. turionellae altered carbohydrate and lipid contents depending on host developmental stage.
Archives of Insect Biochemistry and Physiology, 2015
Ectoparasitoids inject venom into hemolymph during oviposition. We determined the influence of envenomation by the parasitoid, Habrobracon hebetor, on the hemocytes of its larval host, Galleria mellonella. An increase in both intracellular Са(2+) content and phospholipase C activity of the host hemocytes was recorded during 2 days following envenomation by the parasitoid. The decreased hemocyte viability was detected 1, 2, and 24 h after the envenomation. Injecting of the crude venom (final protein concentration 3 μg/ml) into the G. mellonella larvae led to the reduced hemocyte adhesion. The larval envenomation caused a decrease in transmembrane potential of the hemocytes. These findings document the suppression of hemocytic immune effectors in the parasitized host larvae.
Archives of Insect Biochemistry and Physiology, 2006
During parasitism, the ectoparasitic wasp Nasonia vitripennis (Walker) (Hymenoptera: Pteromalidae) induces a developmental arrest in host pupae that is sustained until the fly is either consumed by developing larvae or the onset of death. Bioassays using fluids collected from the female reproductive system (calyx, alkaline gland, acid gland, and venom reservoir) indicated that the venom gland and venom reservoir are the sources of the arrestant and inducer(s) of death. Infrared spectroscopic analyses revealed that crude venom is acidic and composed of amines, peptides, and proteins, which apparently are not glycosylated. Reversed phase high performance liquid chromatography (HPLC) and sodium dodecyl polyacrylamide gel electrophoresis (SDS-PAGE) confirmed the proteinaceous nature of venom and that it is composed mostly of mid to high molecular weight proteins in the range of 13 to 200.5 kilodaltons (kDa). Ammonium sulfate precipitation and centrifugal size exclusion membranes were used to isolate venom proteins. SDS-PAGE protein profiles of the isolated venom fractions displaying biological activity suggest that multiple proteins contribute to arresting host development and eliciting death. Additionally, HPLC fractionation coupled with use of several internal standards implied that two of the low molecular weight proteins were apamin and histamine. However, in vitro assays using BTI-TN-5B1-4 cells contradict the presence of these agents. Arch. Insect Biochem. Physiol. 61:24-41, 2006. Abbreviations used: HPLC = high performance liquid chromatography; I.R. = infrared spectroscopy; kDa = kilodalton; LC 99 = lethal concentration to kill 100% of population; LD = light-dark; MWCO = molecular weight cutoff; SDS-PAGE = sodium dodecyl sulfate polyacrylamide gel electrophoresis; TFA = trifluoroacetic acid; VRE = venom reservoir equivalent.
Insect Biochemistry and Molecular Biology, 2003
Activation of prophenoloxidase (proPO) in insects is a defense mechanism against intruding microorganisms and parasites. Pattern recognition molecules induce activation of an enzymatic cascade involving serine proteinases, which leads to the conversion of proPO to active phenoloxidase (PO). Phenolic compounds produced by pPO-activation are toxic to invaders. Here, we describe the isolation of a venom protein from the parasitoid, Cotesia rubecula, injected into the host, Pieris rapae, which is homologous to serine proteinase homologs (SPH). The data presented here indicate that the protein interferes with the proteolytic cascade, which under normal circumstances leads to the activation of proPO and melanin formation.