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Function and evolution of the aquaporin IsAQP1 in the Lyme disease vector Ixodes scapularis
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Abstract
Ticks are important vectors of pathogenic viruses, bacteria, and protozoans to humans, wildlife, and domestic animals. Due to their life cycles, ticks face significant challenges related to water homeostasis. When blood‐feeding, they must excrete water and ions, but when off‐host (for stretches lasting several months), they must conserve water to avoid desiccation. Aquaporins (AQPs), a family of membrane‐bound water channels, are key players in osmoregulation in many animals but remain poorly characterized in ticks. Here, we bioinformatically identified AQP‐like genes from the deer tick Ixodes scapularis and used phylogenetic approaches to map the evolution of the aquaporin gene family in arthropods. Most arachnid AQP‐like sequences (including those of I. scapularis ) formed a monophyletic group clustered within aquaglycerolporins (GLPs) from bacteria to vertebrates. This gene family is absent from insects, revealing divergent evolutionary paths for AQPs in different hematophagous arthropods. Next, we sequenced the full‐length cDNA of I. scapularis aquaporin 1 ( IsAQP1 ) and expressed it heterologously in Xenopus oocytes to functionally characterize its permeability to water and solutes. Additionally, we examined IsAQP1 expression across different life stages and adult female organs. We found IsAQP1 is an efficient water channel with high expression in salivary glands prior to feeding, suggesting it plays a role in osmoregulation before or during blood feeding. Its functional properties are unique: unlike most GLPs, IsAQP1 has low glycerol permeability, and unlike most AQPs, it is insensitive to mercury. Together, our results suggest IsAQP1 plays an important role in tick water balance physiology and that it may hold promise as a target of novel vector control efforts.
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Research works printed but not linked: 1
- 10.1603/0022-2585(2008)45[68:aapfto]2.0.co;2 · DOI
Cited by
Fourteen anti-tick vaccine targets are variably conserved in cattle fever ticks
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Metadata
- Authors
- Tsujimoto, H., Metz, H. C., Smith, A. A., Sakamoto, J. M., Pal, U., & Rasgon, J. L.
- Affiliations
- Pennsylvania State University (US)
- University of Maryland, College Park (US)
- Corresponding author
- Rasgon, Jason L.
- Venue
- Insect Molecular Biology
- Publisher
- Wiley
- Published
- 2023-02-22
- Volume
- 32
- Issue
- 4
- Pages
- 329-339
- ISSN
- 0962-1075 (ISSN-L)
- 1365-2583
- OpenAlex
- W4317679762
- Cited by
- 6
- References
- 71
- Citations by year
- 2025: 3 · 2024: 1 · 2023: 2
- FWCI
- 0.53
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Insect Molecular Biology (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Agriculture (PEN04769)
- Pennsylvania Department of Health
- Directorate for Biological Sciences (1645331)
- National Institute of Allergy and Infectious Diseases (R01AI080615)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Life Sciences › Immunology and Microbiology › Parasitology › Vector-borne infectious diseases
- Life Sciences › Agricultural and Biological Sciences › Ecology, Evolution, Behavior and Systematics › Study of Mite Species
- Keywords
- aquaporins, Ixodes scapularis, osmoregulation, water homeostasis, glycerol permeability, salivary glands, tick life stages, vector control, hematophagous arthropods
- MeSH terms
- Animals, Bacteria, Disease Vectors, Female, Humans, Lyme Disease, Phylogeny, Water, Ixodes, Aquaporin 1
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