ArticleParasites & vectors2015
Rhipicephalus microplus and Ixodes ovatus cystatins in tick blood digestion and evasion of host immune response.
Article in Parasites & vectors, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 42 citations in OpenAlex.
- Amblyostatin-1, the first salivary cystatin with host immunomodulatory and anti-inflammatory properties from the Neotropical tickFrontiers in immunology · 2025Article
- A longitudinal transcriptomic analysis of Rhipicephalus microplus midgut upon feeding.Ticks and tick-borne diseases · 2024Article
- Changes in saliva protein profile throughout Rhipicephalus microplus blood feeding.Parasites & vectors · 2024Article
- Protease-bound structure of Ricistatin provides insights into the mechanism of action of tick salivary cystatins in the vertebrate host.Cellular and molecular life sciences : CMLS · 2023Article
- A longitudinal transcriptomic analysis from unfed to post-engorgement midguts of adult female Ixodes scapularis.Scientific reports · 2023Review
- Low Genetic Polymorphism in the Immunogenic Sequences ofVaccines · 2022Article
- Host Immune Responses to Salivary Components - A Critical Facet of Tick-Host Interactions.Frontiers in cellular and infection microbiology · 2022Review
- Mialostatin, a Novel Midgut Cystatin fromInternational journal of molecular sciences · 2021Article
- Immunomodulatory Proteins in Tick Saliva From a Structural Perspective.Frontiers in cellular and infection microbiology · 2021Review
- Protease Inhibitors in Tick Saliva: The Role of Serpins and Cystatins in Tick-host-Pathogen Interaction.Frontiers in cellular and infection microbiology · 2017Review
- Saliva from nymph and adult females of Haemaphysalis longicornis: a proteomic study.Parasites & vectors · 2015Article
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCystatins are a group of cysteine protease inhibitors responsible for physiological proteolysis regulation and present in a wide range of organisms. Studies about this class of inhibitors in parasites have contributed to clarify their roles in important physiological processes, like blood digestion and modulation of host immune response during blood feeding. Thus, cystatins are a subject of research on the development of new parasite control methods. Additionally, the characterization of proteins shared by different parasite species represents a valuable strategy to find potential targets in multi-species control methods. However, cystatin functions in ticks remain undetermined, especially in Rhipicephalus microplus and Ixodes ovatus, two species that affect livestock and human health, respectively.
methodsHere we report the inhibitory profile of two R. microplus (BrBmcys2b and BrBmcys2c) and one I. ovatus (JpIocys2a) cystatins to commercial cathepsins B, C, and L. The presence of native cystatins in R. microplus tissues was analyzed using sera against recombinant BrBmcys2b and BrBmcys2c. Also, a peptide from JpIocys2a was synthesized for rabbit immunization, and this serum was used to analyze the cross antigenicity between R. microplus and I. ovatus cystatins.
resultsEnzymatic inhibition profile of tick cystatins shows a distinct modulation for cathepsins related to tick blood digestion and evasion of host immune response. Furthermore, BrBmcys2b was detected in saliva and different tissues along tick stages, while BrBmcys2c was detected mainly in gut from partially engorged R. microplus females, demonstrating a distinct pattern of cystatin expression, secretion and traffic between tick tissues. Moreover, phylogenetic analysis suggests that JpIocys2a belongs to the group of tick gut secreted cystatins. Finally, cross-antigenicity assays revealed that antibodies against the JpIocys2a peptide recognize native and recombinant R. microplus cystatins.
conclusionThe presence of these proteins in different tissues and their ability to differentially inhibit cathepsins suggest distinct roles for JpIocys2a, BrBmcys2b, and BrBmcys2c in blood digestion, egg and larvae development, and modulation of host immune response in tick physiology. The cross-antigenicity between native and recombinant cystatins supports further experiments using JpIocys2a, BrBmcys2b, and BrBmcys2c as vaccine antigens.
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