Characterization of aspartic proteinases from the gut of the tick, Rhipicephalus appendiculatus neuman

Vundla, Waha R.M.; Brossard, Michel; Pearson, David; Labongo, V. L.

doi:10.1016/0965-1748(92)90079-t

Cited by 9 publications

(4 citation statements)

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“…Cathepsins, another component of the tick multiple enzyme system, are believed to be involved in the digestion of blood. The current knowledge of the molecular characteristics of tick digestive enzymes began to be assembled in the 1980s to 1990s by isolation and partial characterization of acidic aspartic peptidases of cathepsin D from soft and hard ticks [ 40 , 41 ]. Later, Mendiola et al reported that aspartic (cathepsin D-like) and cysteine (cathepsin L-like) peptidases are the major hemoglobinolytic enzymes in R. microplus.…”

Section: Discussionmentioning

confidence: 99%

Differential sialotranscriptomes of unfed and fed Rhipicephalus haemaphysaloides, with particular regard to differentially expressed genes of cysteine proteases

Gong

Zhou

et al. 2015

Parasites Vectors

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BackgroundRhipicephalus haemaphysaloides, a hard tick, is a common ectoparasite and can be found in many countries. It is recognized as the primary vector of bovine babesiosis in the south of China. During blood feeding, the tick’s salivary glands secret numerous essential multifunctional proteins. In this study, a R. haemaphysaloides salivary gland transcriptome was described following the production and analysis of the transcripts from the two cDNA libraries of unfed and fed female ticks. The study focused on the differentially expressed genes and cysteine proteases, which play essential roles in the tick life cycle, that were detected most commonly in the up-regulation libraries.MethodsThe sialotranscriptome was assembled and analyzed though bioinformatic tools and the cysteine protease which is differentially expressed form sialotranscriptome were confirmed by Real-time PCR in salivary glands and different developments of ticks.ResultsOn the basis of sequence similarities with other species in various databases, we analyzed the unfed and fed sialotranscriptome of R. haemaphysaloides to identify the differentially expressed proteins secreted from the salivary glands during blood feeding and to investigate their biological functions. There were 25,113 transcripts (35 % of the total assembled transcripts) that showed significant similarity to known proteins with high BLAST from other species annotated. In total, 88 % and 89 % of the sequencing reads could be mapped back to assembled sequences in the unfed and fed library, respectively. Comparison of the abundance of transcripts from similar contigs of the two salivary gland cDNA libraries allowed the identification of differentially expressed genes. In total, there were 1179 up-regulated genes and 574 down-regulated genes found by comparing the two libraries. Twenty-five predicted cysteine proteases were screened from the transcript databases, whereas only six protein molecules were confirmed by gene cloning and molecular expression in E.coli which all belonged to the cysteine protease family. Bioinformatic evolutionary analysis showed the relationship of cysteine proteases in ticks with those of other species, suggesting the origin and conservation of these genes. Analysis of sequences from different tick species indicated the further relationships among the proteases, suggesting the closely related function of these genes. Thus, we confirmed their changes in unfed, fed and engorged ticks and salivary glands. The dynamic changes revealed their important roles in the tick life cycle.ConclusionsOur survey provided an insight into the R. haemaphysaloides sialotranscriptome. The dynamic changes of cysteine proteases in ticks will assist further study of these proteases, which may contribute to the development of anti-tick vaccines or drugs, as well as improving understanding of the roles of cysteine proteases in the tick life cycle.Electronic supplementary materialThe online version of this article (doi:10.1186/s13071-015-1213-7) contains supplementary material, wh...

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Section: Discussionmentioning

confidence: 99%

Differential sialotranscriptomes of unfed and fed Rhipicephalus haemaphysaloides, with particular regard to differentially expressed genes of cysteine proteases

Gong

Zhou

et al. 2015

Parasites Vectors

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“…Also, a multifunctional cysteine protease with optimum pH of 5 was mainly expressed in the midgut epithelium and was specifically localized in the lysosomal vacuoles and possibly released into the gut lumen in Haemaphysalis longicornis (Tsuiji et al, 2008). On the other hand, proteolytic activity have been detected and proteinases have been identified in the midgut of fed ticks showed optimal activities at acidic pH range of about 3-5 in argasid (Tatchell, 1964;Tatchell et al, 1972;Akov et al, 1976;Akov, 1982;Grandjean, 1984) and ixodids (Bogin and Hadani, 1973;Vundla, 1992;Mendiola et al, 1996;Mulenga et al, 1999;Boldbaatar et al, 2006;Horn et al, 2009). Generally, previous studies Proteolytic digestion of blood meal in Ornithodoros erraticus, a vector of B. crocidurae 47 demonstrated that the main digestive proteinases are rather similar to mammalian cathepsin D which is an aspartic proteinase (Coons et al, 1986).…”

Section: Discussionmentioning

confidence: 99%

Proteolytic digestion of blood meal in Ornithodoros erraticus, a vector of Borrelia crocidurae causing relapsing fever in Egypt.

Shanbaky

Helmy

Khater

et al. 2011

Egyptian Academic Journal of Biological Sciences. C, Physiology

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Proteolytic activity was demonstrated in each of the midgut lumen content (MLC) and midgut wall (MW) of the mated unfed and fed female and male Ornithodoros erraticus. In both midgut compartments proteinase activity levels increased after feeding to reach at their peaks about double times the levels in the unfed controls. The peak levels of the proteolytic activity were attained on 1 and 1-2 days after feeding (daf) in the MLC (48 and 31.10-32.63 µg alanine ×10³/ min/ mg gut content) and on 5-6 and 5-7 daf in the MW (196.33-200.33 and 156.80-161.23 µg alanine ×10³/ min/ mg tissue) in the female and male tick, respectively. However, the proteolytic activity in the MLC was much lower than that in the MW of all the corresponding physiological states studied, and represented about one fourth and one fifth of it at the peak activity levels in the female and male tick, respectively. Generally, proteolytic activity was higher in the female than male ticks in the unfed and up to the 2 nd daf in the MLC and in all the corresponding examined states in the MW throughout the period of study (20 daf). Changes in the level of proteolytic activity in each midgut compartment of the female and male ticks infected with Borrelia crocidurae followed almost the same pattern in the uninfected controls. However, the level was lower in the MW of Borrelia infected ticks than uninfected ones throughout most (2-20 daf) of the period of study. The present results were discussed and conclusions conformed to the view of intracellular proteolytic digestion of blood meal in the MW, but did not exclude a possible role of extracellular proteolytic digestion in the MLC.

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“…Since the 1970s, none of the digestive tick cathepsin D reports (23,26,42,43) reflected the functional diversity of multiple tick cathepsin D paralogs and the coordinated hemoglobinolytic action of cysteine and aspartic peptidases (4,5,44). Therefore, identification and full cloning of all I. ricinus cathepsin D genes was the primary concern of this study.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Gut-associated Cathepsin D Hemoglobinase from Tick Ixodes ricinus (IrCD1)

Sojka

Franta

Frantová

et al. 2012

Journal of Biological Chemistry

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Background: Aspartic peptidase activity initiates a multienzyme hemoglobinolysis inside tick guts. Results: IrCD1 is a structurally unique hemoglobinolytic cathepsin D that is up-regulated in tick gut cells during feeding. Conclusion: IrCD1 is the major intestinal aspartic peptidase of I. ricinus. Significance: Biochemical and functional characterization of IrCD1 completes our knowledge on initial host hemoglobin degradation inside tick gut cells.

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Characterization of aspartic proteinases from the gut of the tick, Rhipicephalus appendiculatus neuman

Cited by 9 publications

References 20 publications

Differential sialotranscriptomes of unfed and fed Rhipicephalus haemaphysaloides, with particular regard to differentially expressed genes of cysteine proteases

Differential sialotranscriptomes of unfed and fed Rhipicephalus haemaphysaloides, with particular regard to differentially expressed genes of cysteine proteases

Proteolytic digestion of blood meal in Ornithodoros erraticus, a vector of Borrelia crocidurae causing relapsing fever in Egypt.

Characterization of Gut-associated Cathepsin D Hemoglobinase from Tick Ixodes ricinus (IrCD1)

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