Enzymatic Characterization of a Cubilin-Related Serine Proteinase from the Hard Tick Haemaphysalis longicornis

Miyoshi, Takeharu; Tsuji, Naotoshi; Islam, M. Khyrul; Kamio, Tsugihiko; Fujisaki, Kozo

doi:10.1292/jvms.66.1195

Cited by 13 publications

(5 citation statements)

References 15 publications

(27 reference statements)

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“…But a great number of serine proteases are involved in digestion, with trypsins as the most extensively studied group. In the hard tick Haemaphysalis longicornis , the HlSP gene ( H. longicornis Serine Protease) seemed to have similar enzymatic activity with trypsin and was involved in blood meal digestion [84]. The larvae of the ectoparasitoid Euplectrus separatae release saliva containing a trypsin-like enzyme to digest the host tissues [85].…”

Section: Venom and Nutritional Functionsmentioning

confidence: 99%

Venom Proteins of the Parasitoid Wasp Nasonia vitripennis: Recent Discovery of an Untapped Pharmacopee

Danneels

Rivers

Graaf

2010

Toxins

110

107

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Adult females of Nasonia vitripennis inject a venomous mixture into its host flies prior to oviposition. Recently, the entire genome of this ectoparasitoid wasp was sequenced, enabling the identification of 79 venom proteins. The next challenge will be to unravel their specific functions, but based on homolog studies, some predictions already can be made. Parasitization has an enormous impact on hosts physiology of which five major effects are discussed in this review: the impact on immune responses, induction of developmental arrest, increases in lipid levels, apoptosis and nutrient releases. The value of deciphering this venom is also discussed.

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Section: Venom and Nutritional Functionsmentioning

confidence: 99%

Venom Proteins of the Parasitoid Wasp Nasonia vitripennis: Recent Discovery of an Untapped Pharmacopee

Danneels

Rivers

Graaf

2010

Toxins

110

107

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show abstract

“…A venom trehalase has been proposed to convert the abundant host trehalose sugars into glucose [ 2 ]. Additionally, several proteases found in Nasonia venom are homologous to peptides used by the ectoparasitoid Euplectrus separatae and the tick Haemaphysalis longicornis for blood meal digestion [ 15 , 16 ].…”

Section: Introductionmentioning

confidence: 99%

The venom gland transcriptome of the parasitoid wasp Nasonia vitripennis highlights the importance of novel genes in venom function

Sim

Wheeler

2016

BMC Genomics

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BackgroundPrior to egg laying the parasitoid wasp Nasonia vitripennis envenomates its pupal host with a complex mixture of venom peptides. This venom induces several dramatic changes in the host, including developmental arrest, immunosuppression, and altered metabolism. The diverse and potent bioactivity of N. vitripennis venom provides opportunities for the development of novel acting pharmaceuticals based on these molecules. However, currently very little is known about the specific functions of individual venom peptides or what mechanisms underlie the hosts response to envenomation. Many of the venom peptides also lack bioinformatically derived annotations because no homologs can be identified in the sequences databases. The RNA interference system of N. vitripennis provides a method for functional characterisation of venom protein encoding genes, however working with the current list of 79 candidates represents a daunting task. For this reason we were interested in determining the expression levels of venom encoding genes in the venom gland, as this information could be used to rank candidates for further study. To do this we carried out deep transcriptome sequencing of the venom gland and ovary tissue and used RNA-seq to rank the venom protein encoding genes by expression level. The generation of a specific venom gland transcriptome dataset also provides further opportunities to investigate novel features of this specialised organ.ResultsRNA-seq revealed that the highest expressed venom encoding gene in the venom gland was ‘Venom protein Y’. The highest expressed annotated gene in this tissue was serine protease Nasvi2EG007167, which has previously been implicated in the apoptotic activity of N. vitripennis venom. As expected the RNA-seq confirmed that venom encoding genes are almost exclusively expressed in the venom gland relative to the neighbouring ovary tissue. Novel genes appear to perform key roles in N. vitripennis venom function, with over half of the 15 highest expressed venom encoding loci lacking bioinformatic annotations. The high throughput sequencing data also provided evidence for the existence of an additional 472 previously undescribed transcribed regions in the N. vitripennis genome. Finally, metatranscriptomic analysis of the venom gland transcriptome finds little evidence for the role of Wolbachia in the venom system.ConclusionsThe expression level information provided here for the N. vitripennis venom protein encoding genes represents a valuable dataset that can be used by the research community to rank candidates for further functional characterisation. These candidates represent bioactive peptides valuable in the development of new pharmaceuticals.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-016-2924-7) contains supplementary material, which is available to authorized users.

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“…In the tick Haemaphysalis longicornis , a similar serine peptidase (HlSP) which contains the CUB domain, was characterized. This enzyme is also up-regulated during feeding, is capable of albumin hydrolysis and presents an optimum pH of 5 against synthetic substrates [ 76 ]. In contrast to the acidic characteristics of HlSP, using scorpion MMG samples, it was not possible to observe Z-FR-MCA hydrolysis at pHs below 7 in the absence of reducing agents.…”

Section: Discussionmentioning

confidence: 99%

Biochemical, Transcriptomic and Proteomic Analyses of Digestion in the Scorpion Tityus serrulatus: Insights into Function and Evolution of Digestion in an Ancient Arthropod

et al. 2015

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Scorpions are among the oldest terrestrial arthropods and they have passed through small morphological changes during their evolutionary history on land. They are efficient predators capable of capturing and consuming large preys and due to envenomation these animals can become a human health challenge. Understanding the physiology of scorpions can not only lead to evolutionary insights but also is a crucial step in the development of control strategies. However, the digestive process in scorpions has been scarcely studied. In this work, we describe the combinatory use of next generation sequencing, proteomic analysis and biochemical assays in order to investigate the digestive process in the yellow scorpion Tityus serrulatus, mainly focusing in the initial protein digestion. The transcriptome generated database allowed the quantitative identification by mass spectrometry of different enzymes and proteins involved in digestion. All the results suggested that cysteine cathepsins play an important role in protein digestion. Two digestive cysteine cathepsins were isolated and characterized presenting acidic characteristics (pH optima and stability), zymogen conversion to the mature form after acidic activation and a cross-class inhibition by pepstatin. A more elucidative picture of the molecular mechanism of digestion in a scorpion was proposed based on our results from Tityus serrulatus. The midgut and midgut glands (MMG) are composed by secretory and digestive cells. In fasting animals, the secretory granules are ready for the next predation event, containing enzymes needed for alkaline extra-oral digestion which will compose the digestive fluid, such as trypsins, astacins and chitinase. The digestive vacuoles are filled with an acidic proteolytic cocktail to the intracellular digestion composed by cathepsins L, B, F, D and legumain. Other proteins as lipases, carbohydrases, ctenitoxins and a chitolectin with a perithrophin domain were also detected. Evolutionarily, a large gene duplication of cathepsin L occurred in Arachnida with the sequences from ticks being completely divergent from other arachnids probably due to the particular selective pressures over this group.

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Enzymatic Characterization of a Cubilin-Related Serine Proteinase from the Hard Tick Haemaphysalis longicornis

Cited by 13 publications

References 15 publications

Venom Proteins of the Parasitoid Wasp Nasonia vitripennis: Recent Discovery of an Untapped Pharmacopee

Venom Proteins of the Parasitoid Wasp Nasonia vitripennis: Recent Discovery of an Untapped Pharmacopee

The venom gland transcriptome of the parasitoid wasp Nasonia vitripennis highlights the importance of novel genes in venom function

Biochemical, Transcriptomic and Proteomic Analyses of Digestion in the Scorpion Tityus serrulatus: Insights into Function and Evolution of Digestion in an Ancient Arthropod

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