A comparative survey of the hydrolytic enzymes of ectoparasitic and free-living mites

Nisbet, Alasdair J.; Billingsley, Peter F.

doi:10.1016/s0020-7519(99)00169-1

Cited by 60 publications

(63 citation statements)

References 36 publications

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“…Michaud et al (1996) had previously shown that protease activity in extracts from T. urticae was almost totally explained by cysteine-protease type in both in vitro assays and in zymograms. Likewise, proteolytic activities from T. urticae extracts were inhibited by E-64 and pepstatin A indicating cysteine-and aspartic-protease activities, respectively, in this mite (Nisbet and Billingsley 2000). We have detected both cathepsin B-and L-like activities in T. urticae and B. chilensis whole extracts using specific substrates.…”

Section: Discussionmentioning

confidence: 61%

“…The midgut is the site for synthesis and secretion of digestive enzymes and absorption of nutrients, Processed food and cells pass into the posterior midgut, subsequently compacted in the hindgut and excreted as faecal pellets (Hamilton et al 2003). Mite species that feed on plants rely mostly on cysteine peptidase activities for the digestión of dietary proteins (Nisbet and Billingsley 2000). Particularly, protease activity in extracts from T. urticae was almost totally explained by cysteine type protease activity in vitro assays and in zymograms (Michaud et al 1996).…”

Section: Introductionmentioning

confidence: 99%

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Expression of a barley cystatin gene in maize enhances resistance against phytophagous mites by altering their cysteine-proteases

et al. 2010

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Phytocystatins are inhibitors of cysteine-proteases from plants putatively involved in plant defence based on their capability of inhibit heterologous enzymes. We have previously characterised the whole cystatin gene family members from barley (HvCPI-1 to HvCPI-13). The aim of this study was to assess the effects of barley cystatins on two phytophagous spider mites, Tetranychus urticae and Brevipalpus chilensis. The determination of proteolytic activity profile in both mite species showed the presence of the cysteine-proteases, putative targets of cystatins, among other enzymatic activities. All barley cystatins, except HvCPI-1 and HvCPI-7, inhibited in vitro mite cathepsin L-and/or cathepsin B-like activities, HvCPI-6 being the strongest inhibitor for both mite species. Transgenic maize plants expressing HvCPI-6 protein were generated and the functional integrity of the cystatin transgene was confirmed by in vitro inhibitory effect observed against T urticae and B. chilensis protein extracts. Feeding experiments impaired on transgenic lines performed with T urticae impaired mite development and reproductive performance. Besides, a significant reduction of cathepsin L-like and/or cathepsin B-like activities was observed when the spider mite fed on maize plants expressing HvCPI-6 cystatin. These findings reveal the potential of barley cystatins as acaricide proteins to protect plants against two important mite pests.

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Section: Discussionmentioning

confidence: 61%

Section: Introductionmentioning

confidence: 99%

Expression of a barley cystatin gene in maize enhances resistance against phytophagous mites by altering their cysteine-proteases

et al. 2010

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“…This parasite lives in the bladder of Salmonid fishes. Nisbet and Billingsley (2000) found a significant effect of diet on the activity of hydrolases in extracts obtained from saprophytes. The highest activity of these 19 hydrolases was found in the extract obtained from a free-living Acarus siro, whereas in extracts from saprophytes which live on blood and plants, the amount of active hydrolases was much lower.…”

Section: Discussionmentioning

confidence: 94%

“…It is broken down when parasites penetrate host tissues (Hotez et al, 1994). Nisbet and Billingsley (2000) found a particularly high activity of N-acetyl-β-glucosaminidase in excretes obtained from parasitic saprophytes (Dermanyssus gallinae and Psoroptes ovis). According to these authors, the enzyme plays an important role in the development processes of all invertebrates.…”

Section: Discussionmentioning

confidence: 94%

The activity of selected hydrolases of adult female Ascaris suum, Goeze 1782

Dziekońska-Rynko

2006

Helminthologia

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59 SummaryThe activity of hydrolases was measured in the perienteric fluid, muscles and three sections of the intestine of female Ascaris suum. In none of the examined samples was the activity of lipase and α-galactosidase detected. The activity of hydrolases in anterior, middle and posterior sections of the A. suum intestine was similar. The high activity of the following glucosidases: β-galactosidase (lactase), N-acetyl-β glucosaminidase and α-fucosidase, was detected in the contents and extracts from the intestinal wall, apart from the activity of those found in earlier studies. In perienteric fluid and in extracts from muscles, a high activity of β-glucuronidase and β-glucosidase was detected; such activity was not found in the intestine.

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“…A particularly high activity in all the mites studies was typical of N-acetyl-b-glucosaminidase. According to Nisbet and Billingsley (2000), the results they obtained were caused by the fact that the mite extracts were mostly made of larval stages, the enzyme being present during moulting in all invertebrates. In the experiment described in this paper, high activity of the enzyme was observed in extracts of the two nematode larval stages studied.…”

Section: Discussionmentioning

confidence: 99%

Activity of selected hydrolases in excretion-secretion products and homogenates from L 3 and L 4 larvae of Anisakis simplex (Nematoda: Anisakidae) parasitising herring

Dziekońska-Rynko¹,

Rokicki²,

Jabłonowski³

2003

Acta Ichthyol. Piscat.

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Dziekoƒska-Rynko J., Rokicki J., Jab∏onowski Z., 2003. Activity of selected hydrolases in excretion-secretion products and homogenates from L 3 and L 4 larvae of Anisakis simplex (Nematoda: Anisakidae) parasitising herring. Acta Ichthyol. Piscat. 33 (2): 125-136.Background. Proteolytic enzymes may serve multiple functions: they may inhibit the host's blood clotting, protect the parasite from the host's immune response, facilitate parasite's migration within a tissue by decomposing the tissue barrier, enhance the hatching and moulting of larvae, and play an important role in their feeding. Learning their identity leads to a better understanding of a host-parasite system. The objective of this study was to check, using biochemical methods, if, in addition to proteases, ES products and extracts of 3rd and 4th larval stages of Anisakis simplex (Rudolphi, 1809) contain other hydrolases. Material and methods. Stage-3 larvae (L 3 ) of A. simplex were removed from Baltic herring, Clupea harengus membras Linnaeus, 1761 caught in the Baltic Sea. Stage-4 larvae (L 4 ) were obtained from an L 3 stage culture kept in Eagle's medium. The solutions containing ES products were collected and dialysed at 4°C against distilled water for 24 h. Larval extracts were obtained by homogenising the larvae in a physiological saline (0.9 % NaCl) solution in a glass homogeniser. The homogenate was centrifuged for 10 min at 3000 G. The supernatant was used in enzyme activity assays. Enzymatic activity of ES products and homogenates of L 3 and L 4 larvae of A. simplex was determined with the API ZYM test.Results. The excretion-secretion product of L 3 and L 4 larvae of A. simplex revealed activities of 10-and 11 hydrolases, respectively. Activity of esterase, esterase lipase, valine arylamidase, and N-acetyl-ß-glucosaminidase in the L 4 larvae extracts was higher than the activity of a corresponding enzyme assayed in the L 3 extracts. Only in the case of acid phosphatase, its activity in L 3 ES products was twice that of the activity found in ES products of L 4 larvae. Enzymes such as trypsin, chymotrypsin, and ß-glucosidase were not detected in extracts from L 3 larvae.

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A comparative survey of the hydrolytic enzymes of ectoparasitic and free-living mites

Cited by 60 publications

References 36 publications

Expression of a barley cystatin gene in maize enhances resistance against phytophagous mites by altering their cysteine-proteases

Expression of a barley cystatin gene in maize enhances resistance against phytophagous mites by altering their cysteine-proteases

The activity of selected hydrolases of adult female Ascaris suum, Goeze 1782

Activity of selected hydrolases in excretion-secretion products and homogenates from L 3 and L 4 larvae of Anisakis simplex (Nematoda: Anisakidae) parasitising herring

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