Cathepsin L—a novel cysteine protease from Haemaphysalis flava Neumann, 1897

Sun, Yali; He, Li; Yu, Liang; Guo, Jiaying; Zheng, Na; Liu, Qin; Zhao, Junlong

doi:10.1007/s00436-019-06271-4

Cited by 6 publications

(2 citation statements)

References 44 publications

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“…Several studies have documented potential functional roles of cysteine proteases in tick physiology [91][92][93]. In a lone study, a cysteine protease from H. longicornis when silenced by RNAi, showed to be involved with digestion of a blood meal and increased the number of Babesia parasites [94]. Recently, a cathepsin L from the tick, R. microplus (BmCL1), was shown to interact with thrombin at pH 7.5 and impair thrombin-induced fibrinogen clotting via a fibrinogenolytic activity [95].…”

Section: B) Majority Of Proteases In a Americanum Saliva Are Metallomentioning

confidence: 99%

Time-resolved proteomic profile of Amblyomma americanum tick saliva during feeding

et al. 2020

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Amblyomma americanum ticks transmit more than a third of human tick-borne disease (TBD) agents in the United States. Tick saliva proteins are critical to success of ticks as vectors of TBD agents, and thus might serve as targets in tick antigen-based vaccines to prevent TBD infections. We describe a systems biology approach to identify, by LC-MS/MS, saliva proteins (tick = 1182, rabbit = 335) that A. americanum ticks likely inject into the host every 24 h during the first 8 days of feeding, and towards the end of feeding. Searching against entries in GenBank grouped tick and rabbit proteins into 27 and 25 functional categories. Aside from housekeeping-like proteins, majority of tick saliva proteins belong to the tick-specific (no homology to non-tick organisms: 32%), protease inhibitors (13%), proteases (8%), glycine-rich proteins (6%) and lipocalins (4%) categories. Global secretion dynamics analysis suggests that majority (74%) of proteins in this study are associated with regulating initial tick feeding functions and transmission of pathogens as they are secreted within 24-48 h of tick attachment. Comparative analysis of the A. americanum tick saliva proteome to five other tick saliva proteomes identified 284 conserved tick saliva proteins: we speculate that these regulate critical tick feeding functions and might serve as tick vaccine antigens. We discuss our findings in the context of understanding A. americanum tick feeding physiology as a means through which we can find effective targets for a vaccine against tick feeding.

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Section: B) Majority Of Proteases In a Americanum Saliva Are Metallomentioning

confidence: 99%

Time-resolved proteomic profile of Amblyomma americanum tick saliva during feeding

et al. 2020

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“…Tick cysteine proteases, including L and B cathepsins and longipain, are mostly expressed in the midgut and involved in blood meal digestion, embryogenesis and pathogen transmission [ 76 – 78 ]. However, the abundance of cysteine proteases found in O. erraticus saliva suggests that they might be also playing a role in tick feeding.…”

Section: Resultsmentioning

confidence: 99%

A proteomics informed by transcriptomics insight into the proteome of Ornithodoros erraticus adult tick saliva

et al. 2022

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Background The argasid tick Ornithodoros erraticus is the main vector of tick-borne human relapsing fever (TBRF) and African swine fever (ASF) in the Mediterranean Basin. The prevention and control of these diseases would greatly benefit from the elimination of O. erraticus populations, and anti-tick vaccines are envisaged as an effective and sustainable alternative to chemical acaricide usage for tick control. Ornithodoros erraticus saliva contains bioactive proteins that play essential functions in tick feeding and host defence modulation, which may contribute to host infection by tick-borne pathogens. Hence, these proteins could be candidate antigen targets for the development of vaccines aimed at the control and prevention of O. erraticus infestations and the diseases this tick transmits. The objective of the present work was to obtain and characterise the proteome of the saliva of O. erraticus adult ticks as a means to identify and select novel salivary antigen targets. Methods A proteomics informed by transcriptomics (PIT) approach was applied to analyse samples of female and male saliva separately using the previously obtained O. erraticus sialotranscriptome as a reference database and two different mass spectrometry techniques, namely liquid chromatography–tandem mass spectrometry (LC–MS/MS) in data-dependent acquisition mode and sequential window acquisition of all theoretical fragment ion spectra MS (SWATH-MS). Results Up to 264 and 263 proteins were identified by LC–MS/MS in the saliva of O. erraticus female and male ticks, respectively, totalling 387 non-redundant proteins. Of these, 224 were further quantified by SWATH-MS in the saliva of both male and female ticks. Quantified proteins were classified into 23 functional categories and their abundance compared between sexes. Heme/iron-binding proteins, protease inhibitors, proteases, lipocalins and immune-related proteins were the categories most abundantly expressed in females, while glycolytic enzymes, protease inhibitors and lipocalins were the most abundantly expressed in males. Ninety-seven proteins were differentially expressed between the sexes, of which 37 and 60 were overexpressed in females and males, respectively. Conclusions The PIT approach demonstrated its usefulness for proteomics studies of O. erraticus, a non-model organism without genomic sequences available, allowing the publication of the first comprehensive proteome of the saliva of O. erraticus reported to date. These findings confirm important quantitative differences between sexes in the O. erraticus saliva proteome, unveil novel salivary proteins and functions at the tick–host feeding interface and improve our understanding of the physiology of feeding in O. erraticus ticks. The integration of O. erraticus sialoproteomic and sialotranscriptomic data will drive a more rational selection of salivary candidates as antigen targets for the development of vaccines aimed at the control of O. erraticus infestations and the diseases it transmits. Graphical Abstract

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De novo transcriptome sequencing and comparative analysis of Haemaphysalis flava Neumann, 1897 at larvae and nymph stages

Guo

Sun

Luo

et al. 2019

Infection, Genetics and Evolution

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Cathepsin L—a novel cysteine protease from Haemaphysalis flava Neumann, 1897

Cited by 6 publications

References 44 publications

Time-resolved proteomic profile of Amblyomma americanum tick saliva during feeding

Time-resolved proteomic profile of Amblyomma americanum tick saliva during feeding

A proteomics informed by transcriptomics insight into the proteome of Ornithodoros erraticus adult tick saliva

De novo transcriptome sequencing and comparative analysis of Haemaphysalis flava Neumann, 1897 at larvae and nymph stages

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