Background: Sodium channels (SCs) in mites and insects are target sites for pesticides, including pyrethroids. Point mutations in the SC gene have been reported to change the structural conformation of the protein and its sensitivity to pesticides. To find mutations in the SC gene of the mite Varroa destructor (VmNa), the authors analysed the VmNa gene sequences available in GenBank and prepared specific primers for the amplification of two fragments containing the regions coding for (i) the domain II S4-S6 region (bp 2805-3337) and (ii) the domain III S4-3' terminus region (bp 4737-6500), as determined according to the VmNa cDNA sequence AY259834.
Results: Sensitive and resistant mite populations did not differ in the amino acid sequences of the III S4-3' terminus VmNa region. However, differences were found in the IIS4-IIS6 fragment. In the resistant population, the mutation C(3004) → G resulted in the substitution L(1002) → V (codon ctg → gtg) at the position equivalent to that of the housefly L925 in the domain II S5 helix. Additionally, the mutation F(1052) → L (codon ttc → ctc) at the position equivalent to that of the housefly F975 in the domain II P-loop connecting segments S5 and S6 was detected in both the resistant and sensitive populations.
Conclusion: All individuals that survived the tau-fluvalinate treatment in the bioassay harboured the L(1002) → V mutation combined with the F(1052), while dead individuals from both the sensitive and resistant populations harboured mostly the L(1002) residue and either of the two residues at position 1052.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1002/ps.3679 | DOI Listing |
Mol Biol Rep
January 2025
Department of Molecular Biology Vadi Kampüsü, Istanbul Atlas University, Anadolu Cd., No 40, Kağıthane, Istanbul, 34408, Turkey.
Background: Modulation of protein synthesis according to the physiological cues is maintained through tight control of Eukaryotic Elongation Factor 2 (eEF2), whose unique translocase activity is essential for cell viability. Phosphorylation of eEF2 at its Thr56 residue inactivates this function in translation. In our previous study we reported a novel mode of post-translational modification that promotes higher efficiency in T56 phosphorylation.
View Article and Find Full Text PDFmBio
January 2025
Department of Microbiology and Molecular Genetics, University of California, Davis, California, USA.
Orthoflaviviruses are positive-sense single-stranded RNA viruses that hijack host proteins to promote their own replication. Zika virus (ZIKV) is infamous among orthoflaviviruses for its association with severe congenital birth defects, notably microcephaly. We previously mapped ZIKV-host protein interactions and identified the interaction between ZIKV non-structural protein 4A (NS4A) and host microcephaly protein ankyrin repeat and LEM domain-containing 2 (ANKLE2).
View Article and Find Full Text PDFDevelopment
January 2025
Department of Biological Chemistry and Pharmacology, The Ohio State University Medical Center, Columbus OH, USA.
Zebrafish have a high capacity to regenerate their hearts. Several studies have surveyed transcriptional enhancers to understand how gene expression is controlled during heart regeneration. We have identified REN or the runx1 enhancer that during regeneration regulates the expression of the nearby runx1 gene.
View Article and Find Full Text PDFChem Biodivers
January 2025
Biruni Universitesi, Molecular Biology and Genetics, Biruni Uni, İstanbul, TURKEY.
Regulation of protein production in response to physiological signals is achieved through precise control of Eukaryotic Elongation Factor 2 (eEF2), whose distinct translocase function is crucial for cell survival. Phosphorylation of eEF2 at its Thr56 (T56) residue inactivates this function in translation. Using genetically modified paralogue of a colon cancer cell line, HCT116 which carries a point mutation at Ser595-to-Alanine in the eEF2 gene we were able to create a constitutively active form of eEF2.
View Article and Find Full Text PDFInt J Microbiol
January 2025
Laboratory of Animal Hygiene, School of Veterinary Medicine, Kitasato University, Higashi 23-35-1, Towada Aomori 034-8628, Japan.
-a facultative intracellular pathogen of macrophages-causes bronchopneumonia in foals and patients who are immunocompromised. Virulent strains of possess a virulence-associated plasmid, which encodes a 15- to 17-kDa surface protein called virulence-associated protein A (VapA). VapA expression is regulated by temperature and pH.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!