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is a blood-feeding hard tick known for transmitting a variety of pathogens, including How the parasites in the imbibed blood become anchored in the midgut of ticks is still unknown. Leucine-rich repeat domain (LRR)-containing protein, which is associated with the innate immune reaction and conserved in many species, has been detected in and has previously been indicated in inhibiting the growth of However, the detailed mechanism is unknown. In this study, one of the ligands for LRR from (HlLRR) was identified in , designated BmActin, using glutathione transferase (GST) pulldown experiments and immunofluorescence assays. Moreover, RNA interference of HlLRR led to a decrease in the BmActin mRNA expression in the midgut of fully engorged ticks which fed on -infected mice. We also found that the expression level of the innate immune molecules in , defensin, antimicrobial peptides (AMPs), and lysozyme, were downregulated after the knockdown of HlLRR. However, subolesin expression was upregulated. These results indicate that HlLRR not only recognizes BmActin but may also modulate innate immunity in ticks to influence growth, which will further benefit the development of anti- vaccines or drugs.
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http://dx.doi.org/10.1128/IAI.00268-20 | DOI Listing |
Trends Plant Sci
September 2025
Department of Plant and Environmental Sciences, Section of Transport Biology, University of Copenhagen, Thorvaldsensvej 40, 1871 Frederiksberg C, Denmark. Electronic address:
Plants have developed sophisticated signaling mechanisms to adapt to environmental changes, and secreted peptides play crucial roles. Sulfated tyrosine (sTyr) peptides are important regulators of plant growth, nutrient uptake, defense responses, and seed development. This study delves into the evolution of sTyr peptides, their receptors, and the enzyme tyrosylprotein sulfotransferase (TPST) that is responsible for their activation.
View Article and Find Full Text PDFBiochimie
September 2025
Immunopathology and Viral Reservoir Unit, National Center of Microbiology, Instituto de Salud Carlos III, Majadahonda, Madrid, Spain; Biomedical Research Center Network in Infectious Diseases (CIBERINFEC), Instituto de Salud Carlos III, Majadahonda, Madrid, Spain.
TLR8 and TLR9 are innate immune receptors belonging to the TLR family that are essential for viral recognition and early immune activation. Their dysfunction is linked to increased susceptibility to infections. TLR8 detects viral single- and double-stranded RNA, while TLR9 recognizes viral DNA molecules with CpG motifs.
View Article and Find Full Text PDFJ Biol Chem
September 2025
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA, United States; Aligning Science Across Parkinson's (ASAP) Collaborative Research Network, San Francisco, CA, United States. Electronic address:
PPM1H phosphatase reverses Parkinson's disease-associated, Leucine Rich Repeat Kinase 2-mediated, Rab GTPase phosphorylation. We showed previously that PPM1H relies on an N-terminal amphipathic helix for Golgi membrane localization and this helix enables PPM1H to associate with liposomes in vitro; binding to highly curved liposomes activates PPM1H's phosphatase activity. We show here that PPM1H also contains an allosteric binding site for its non-phosphorylated reaction products, Rab8A and Rab10.
View Article and Find Full Text PDFThe end-stage pathology of Parkinson's disease (PD) involves the loss of dopamine-producing neurons in the substantia nigra pars compacta (SNc). However, synaptic deregulation of these neurons begins much earlier. Understanding the mechanisms behind synaptic deficits is crucial for early therapeutic intervention, yet these remain largely unknown.
View Article and Find Full Text PDFVolume-regulated anion channels (VRACs) are large-pore channels present in nearly all vertebrate cells, playing key roles in cell volume regulation and autocrine/paracrine signaling. Here, we identify the ubiquitously expressed puromycin-sensitive aminopeptidase (PSA) as a binding partner of the obligatory VRAC subunit SWELL1 (also known as LRRC8A) and report the cryo-electron microscopy structure of the SWELL1-PSA complex. Three PSA molecules associate with a single SWELL1 hexamer, coupling adjacent leucine-rich repeat (LRR) domains into local dimers.
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