ArticleParasites & vectors2025
Aquaporins modulate the cold response of Haemaphysalis longicornis via changes in gene and protein expression of fatty acids.
Article in Parasites & vectors, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Surviving Alpine Winters Without Dehydration: Physiological and Transcriptomic Insights into the Freeze Avoidance ofInsects · 2026Article
- Genome-Wide Identification and Expression Analysis of the Aquaporin Gene Family in the Qinghai Toad-Headed Agama (Biology · 2025Article
- Sexual epigenetics: genome-wide analysis revealed differential DNA methylation in the vector tick Haemaphysalis longicornis.Parasites & vectors · 2025Article
- Navigating the Cold: Integrative Transcriptome Sequencing Approach Reveals Ionoregulatory and Whole-Body Responses to Cold Acclimation in Drosophila ananassae.Genome biology and evolution · 2025Article
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10 authors.
Funding
Abstract
backgroundAs ectotherms that spend most of their life in the environment (off-host), ticks face challenges in maintaining water balance, and some species must cope with severe low winter temperatures. Aquaporins (AQPs) are essential membrane proteins that enhance cold tolerance in many animals by regulating homeostatic processes. However, the dynamic expressions and involvement of aquaporins in the cold stress of ticks remain unclear.
methodsIn the present study, three AQP genes, HlAQP2, HlAQP3, and HlAQP5, belonging to the major intrinsic protein (MIP) superfamily, were characterized from the important vector tick Haemaphysalis longicornis. Then, multiple bioinformatics analyses were performed. Quantitative real-time PCR (qPCR) was used to detect different expressions of H. longicornis genes under different cold treatment conditions. RNA interference was used to explore the relationship between AQP and the cold response of H. longicornis. Additionally, proteomic and transcriptomic analyses were used to investigate the mechanisms underlying the effects of AQPs on cold response in ticks.
resultsThe amino acid sequence of AQPs shows high homology in Ixodida, with HlAQP2 and HlAQP5 proteins comprising two asparagine-proline-alanine (NPA) motifs, whereas HlAQP3 protein was featured by glycerol facilitator GlpF channel. The spatiotemporal expression of AQPs in H. longicornis varied significantly after low temperature treatment, and different expression patterns were observed over prolonged exposure periods. RNAi knockdown of AQPs significantly increased tick mortality after treatment at a sublethal temperature of - 14 °C for 2 h. Proteomic and transcriptomic analysis revealed that the differentially expressed genes and proteins caused by the knockdown of AQPs are mainly enriched in the fatty acid metabolism pathway.
conclusionsThe above results indicated that AQPs could regulate tick cold response by modulating water balance and fatty acid metabolism.
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