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8 results for “Chemosensory proteins”
Data from: Effect of host plant and immune challenge on the levels of chemosensory and odorant-binding proteins in caterpillar salivary glands
More than half of the proteome from mandibular glands in caterpillars is represented by chemosensory proteins. Based on sequence similarity, these proteins are putative transporters of ligands to gustatory receptors in sensory organs of insects. We sought to determine whether these proteins are inducible by comparing, both qualitatively and quantitatively, the salivary (mandibular and labial) proteomes from caterpillars (Vanessa cardui) reared on different plants and artificial diet containing either bacteria or bacterial cell-walls. We included a treatment where the caterpillars were switched from feeding on artificial diet to plant material at some point in their development. Additionally, we evaluated the degree of overlap between the proteomes in the hemolymph-filled coelom and salivary glands of caterpillars reared on plant material. We found that the quality and quantity of the identified proteins differed clearly between hemolymph-filled coelom, labial and mandibular glands. Our results indicated that even after molting and two-day feeding on a new diet, protein production is affected by the previous food source used by the caterpillar. Candidate proteins involved in chemosensory perception by insects were detected: three chemosensory (CSPs) and two odorant-binding proteins (OBPs). Using the relative amounts of these proteins across tissues and treatments as criteria for their classification, we detected hemolymph- and mandibular gland-specific CSPs and observed that their levels were affected by caterpillar diet. Moreover, we could compare the protein and transcript levels across tissues and treatment for at least one CSP and one OBP. Therefore, we have identified specific isoforms for testing the role of CSPs and OBPs in plant and pathogen recognition. We detected catalase, immune-related protein and serine proteases and their inhibitors in high relative levels in the mandibular glands in comparison to the labial glands. These findings suggest that the mandibular glands of caterpillars may play an important role protecting the caterpillar from oxidative stress, pathogens and aiding in digestion. Contamination with hemolymph proteins during dissection of salivary glands from caterpillars may occur but it is not substantial since the proteomes from hemolymph, mandibular and labial glands were easily discriminated from each other by principal component analysis of proteomic data.
Data from: Comparative genomics of chemosensory protein genes reveals rapid evolution and positive selection in ant-specific duplicates
Gene duplications can have a major role in adaptation, and gene families underlying chemosensation are particularly interesting due to their essential role in chemical recognition of mates, predators and food resources. Social insects add yet another dimension to the study of chemosensory genomics, as the key components of their social life rely on chemical communication. Still, chemosensory gene families are little studied in social insects. Here we annotated chemosensory protein (CSP) genes from seven ant genomes and studied their evolution. The number of functional CSP genes ranges from 11 to 21 depending on species, and the estimated rates of gene birth and death indicate high turnover of genes. Ant CSP genes include seven conservative orthologous groups present in all the ants, and a group of genes that has expanded independently in different ant lineages. Interestingly, the expanded group of genes has a differing mode of evolution from the orthologous groups. The expanded group shows rapid evolution as indicated by a high dN/dS (nonsynonymous to synonymous changes) ratio, several sites under positive selection and many pseudogenes, whereas the genes in the seven orthologous groups evolve slowly under purifying selection and include only one pseudogene. These results show that adaptive changes have played a role in ant CSP evolution. The expanded group of ant-specific genes is phylogenetically close to a conservative orthologous group CSP7, which includes genes known to be involved in ant nestmate recognition, raising an interesting possibility that the expanded CSPs function in ant chemical communication.
Data from: Effect of host plant and immune challenge on the levels of chemosensory and odorant-binding proteins in caterpillar salivary glands
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Data from: Comparative genomics and transcriptomics in ants provide new insights into the evolution and function of odorant binding and chemosensory proteins
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Data from: Comparative genomics of chemosensory protein genes reveals rapid evolution and positive selection in ant-specific duplicates
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Tissue-specific transcriptomics, chromosomal localization, and phylogeny of chemosensory and odorant binding proteins from the red flour beetle Tribolium castaneum reveal subgroup specificities for ol
GEO Series GSE63162. Tribolium castaneum. 16 samples. Type: Expression profiling by high throughput sequencing.
Confocal microscopy data associated with "The conserved aphid saliva chemosensory protein effector Mp10 targets plant AMSH deubiquitinases at cellular membranes to suppress pattern-triggered immunity"
<p><strong>Confocal microscopy data as described in "The conserved aphid saliva chemosensory protein effector Mp10 targets plant AMSH deubiquitinases at cellular membranes to suppress pattern-triggered immunity".</strong></p> <p> </p> <p>Data relate to Figure 2 (“Mp10 interacts with AMSH deubiquitinases in yeast and plants”) involving FLIM-FRET imaging data to determine the interaction between eGFP-tagged <em>Myzus persicae </em>Mp10 and mCherry-tagged <em>Nicotiana benthamiana </em>AMSH proteins in plant cells; and Figure 6 (“Mp10 affects the abundance and localisation of cell-surface receptor-like kinases) involving confocal microscopy showing the effect of Mp10-expression on the localisation of the GFP-tagged FLS2 receptor-kinase protein, and it’s colocalization with RFP-tagged markers of the plasma membrane and the tonoplast in plant cells.</p> <p>Constructs encoding fluorescent protein fusions were transformed into <em>Agrobacterium tumefaciens </em>GV3101, and mixed Agrobacterium cultures were infiltrated into mature leaves of <em>N. benthamiana </em>plants to co-express the desired combinations of proteins. All image data was gathered from lower epidermal leaf cells of infiltrated leaves 2-3 days post infiltration.</p> <p> </p> <p><strong>FLIM-FRET assays.</strong></p> <p>eGFP-tagged Mp10, or eGFP-alone, was co-expressed with mCherry-tagged AMSH proteins, or mCherry fused to aquaeorin in <em>N. benthamiana</em> via agroinfiltration as described above. Lower epidermal cells of leaf sections were imaged 2-3 days after infiltration using a Leica Stellaris 8. Images were captured detecting fluorescence from eGFP (WLL laser, ex.488 nm, em 509-534 nm.) mCherry (lWLL aser, ex. 587 nm em 603-625 nm.) and chlorophyll (WLL laser, ex 587 nm. em 687-712 nm.). Regions of cells showing expression of both eGFP- and mCherry- tagged proteins but lacking chlorophyll were selected for FLIM analysis to avoid bleed through of chlorophyll fluorescence into the eGFP chanel. Fluorescence lifetime data of EGFP were collected from these regions in FLIM mode (WLL laser ex. 488nm, em 525-530 nm.), data were collected at 128x128 resolution until 1000 photons per pixel were collected for the most intense regions of the image. Instrument response function was captured using erythrosine on each day of data collection. FLIM data were analysed using Leica LASX FLIM FCS software. Fluorescence lifetime decay curves of free eGFP control samples were modelled as a 2-component exponential function, and all samples from each experimental set were modelled against the fluorescence lifetime from the corresponding control samples to derive values for fluorescent lifetime and %FRET efficiency for each image collected. %FRET efficiency was mapped to the images and phasor plots were generated for regions with the highest and lowest FRET efficiency, showing that the FRET signal was associated with a clockwise shift on the phasor plot consistent with <em>bona-fide </em>FRET. Full experimental metadata for each image set are included within the .lif files.</p> <p> </p> <p><strong>FLS2-GFP localisation experiments.</strong></p> <p>Confocal microscopy analysis was performed on a Leica TCS SP8X confocal DM6 microscope with a 63x water-immersion objective, using Leica Application Suite X (LAS X) software (3.5.7.23225). eGFP and chlorophyll signals were excited by a 488 nm Argon laser with emission, respectively, at 495–545 nm and 690-710 nm. RFP signal was excited by a 590 nm white light laser (WLL) with emission at 605–650 nm. Full experimental metadata for each image set are included within the .lif files.</p> <p> </p> <p>Leica Image Files (.lif) that contain multiple images including metadata associated with image acquisition and processing.</p> <p> </p> <p>FLIM030823.lif</p> <p>FLIM130724.lif</p> <p>FLIM140623.lif</p> <p>FLIM160623.lif</p> <p>FLIM240523.lif</p> <p>FLIM250523.lif</p> <p>Files include FLIM-FRET data as shown in Figure 2 parts D-L.</p> <p>FLIM-data-files.xlsx includes a description of the individual image filenames, and the combinations of fluorophore imaged in each.</p> <p> </p> <p>Fig6cSlFLS2-gfp_Mp10-RFP.lif</p> <p>Fig6c-SlFLS2-GFP_EV-RFP.lif</p> <p>Correspond to Figure 6 C showing co-expression of RFP-tagged Mp10 (or free RFP control) co-expressed with GFP-tagged FLS2</p> <p> </p> <p>20230828_SlFLS2-GFP_Flag-Mp10_Flag-alone_Remorin-RFP-3-3-1x.lif</p> <p>20230828_SlFLS2-GFP_Flag-Mp10_Flag-alone_Remorin-RFP-3-3-3x.lif</p> <p>20230828_SlFLS2-GFP_Flag-Mp10_Flag-alone_Remorin-RFP-4-2-3x.lif</p> <p>0230828_SlFLS2-GFP_Flag-Mp10_Flag-alone_Remorin-RFP4-2-1x.lif</p> <p>Correspond to Figure 6 D showing co-expression of FLAG-tagged Mp10 (or free FLAG control) co-expressed with GFP-tagged FLS2 together with RFP-tagged plasma membrane marker Remorin</p> <p> </p> <p>20230911_SlFLS2-GFP_Flag-Mp10_Flag-alone_StSUC4-RFP-14-5-1x.lif</p> <p>20230911_SlFLS2-GFP_Flag-Mp10_Flag-alone_StSUC4-RFP-14-5-3x.lif</p> <p>20230911_SlFLS2-GFP_Flag-Mp10_Flag-alone_StSUC4-RFP-16-1-1x.lif</p> <p>20230911_SlFLS2-GFP_Flag-Mp10_Flag-alone_StSUC4-RFP-16-1a-3x.lif</p> <p>20230911_SlFLS2-GFP_Flag-Mp10_Flag-alone_StSUC4-RFP-16-1b-1x.lif</p> <p>Correspond to Figure 6 E showing co-expression of FLAG-tagged Mp10 (or free FLAG control) co-expressed with GFP-tagged FLS2 together with RFP-tagged tonoplast marker SUC4.</p> <p> </p> <p>We are grateful to the John Innes Centre (JIC) Bioimaging Platform for training and technical support</p> <p>This work was funded by UK Research and Innovation (UKRI) Biotechnology and Biological Sciences Research Council (BBSRC) grants to SAH (BB/V008544/1 and BB/N009169/1), Additional Support was provided by the BBSRC Institute Strategy Programmes (BBS/E/J/000PR9797 and BBS/E/JI/230001B) awarded to the John Innes Centre (JIC). The JIC is grant-aided by the John Innes Foundation.</p> <p> </p>
Comparison and functional analysis of odorant-binding proteins and chemosensory proteins in two closely related thrips species, Frankliniella occidentalis and Frankliniella intonsa (Thysanoptera: Thri
GEO Series GSE213075. Frankliniella intonsa; Frankliniella occidentalis. 9 samples. Type: Expression profiling by high throughput sequencing.
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