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Integrated analysis of the sialotrancriptome and sialoproteome of the rat flea Xenopsylla cheopis.

ABSTRACT: . Here we provide a deeper insight into Xenopsylla cheopis salivary glands contents pairing transcriptome and proteomic approaches. Sequencing of 99 pairs of salivary glands from adult females X. cheopis yielded a total of 7,432 coding sequences functionally classified into 25 classes, in which the secreted class was found to be the most abundant one. The translated transcripts also served as a reference database for the proteomic study, which identified peptides from 610 different proteins.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Xenopsylla Cheopis

TISSUE(S): Salivary Gland

SUBMITTER: Stephen Lu

LAB HEAD: Jose Marcos Ribeiro

PROVIDER: PXD028695 | Pride | 2023-05-10

REPOSITORIES: Pride

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			Action	DRS
	PI21-24890-1L.raw	Raw
	PI21-24890-1L.sqt	Other
	PI21-24892-1L.raw	Raw
	PI21-24892-1L.sqt	Other
	PI21-24976-C1.raw	Raw

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Publications

Integrated analysis of the sialotranscriptome and sialoproteome of the rat flea Xenopsylla cheopis.

Lu Stephen S Andersen John F JF Bosio Christopher F CF Hinnebusch B Joseph BJ Ribeiro José M C JMC

Journal of proteomics 20220104

Over the last 20 years, advances in sequencing technologies paired with biochemical and structural studies have shed light on the unique pharmacological arsenal produced by the salivary glands of hematophagous arthropods that can target host hemostasis and immune response, favoring blood acquisition and, in several cases, enhancing pathogen transmission. Here we provide a deeper insight into Xenopsylla cheopis salivary gland contents pairing transcriptomic and proteomic approaches. Sequencing of ...[more]

PMID: 34990822

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A substrate-like thrombin inhibitor from the saliva of the flea Xenopsylla cheopis is resistant to cleavage by the enzyme

Project description:XC-43 is a small peptide identified in the sialome of the flea Xenopsylla cheopis and act as a fast, tight-binding inhibitor of thrombin with a dissociation constant of less than 10 pM. The crystal structure of XC-43 in complex with thrombin shows that despite its substrate-like binding mode, XC-43 is not detectably cleaved by thrombin and that it interacts with the thrombin surface from the enzyme catalytic site through the fibrinogen-binding exosite I. The low rate of hydrolysis is verified in solution experiments with XC-43 which show the substrate to be largely intact after two hours of incubation with thrombin at 37°C. The potential of XC-43 as an anticoagulant is suggested by increased arterial occlusion time, tail bleeding time, and blood coagulation parameters in rat models of thrombosis.

2022-02-16 | PXD028851 | Pride

Triatoma sordida salivary glands LC-MSMS

Project description:Triatoma sordida salivary glands secrete a number of complex bioactive proteins during feeding that affect hemostatic and immunological systems from vertebrate hosts. In this study, salivary glands and saliva were collected from 5th instar nymphs and adult triatomines. Liquid chromatography tandem-mass spectrometry (LC-MS/MS) was used to identify T. sordida salivary proteins. A total of 133 proteins was identified. Lipocalins, Hemiptera specific families, CRiSP/Antigen-5 and Kazal-type protein inhibitors proteins match to 42.01%, 14.32%, 5.86% and 1.91% of the total spectrum count, respectively. These proteins are involved in several physiological roles, including anti-coagulant, immunity and anti-microorganism. Salivary proteins contribute to successful feeding.

2022-02-15 | PXD028350 | Pride

Integrated analysis of sialotranscriptome and sialoproteome of the brown dog tick Rhipicephalus sanguineus (s.l.): insights into gene expression during blood feeding

Project description:Tick salivary glands secrete a complex saliva into their hosts which modulates vertebrate hemostasis, immunity and tissue repair mechanisms. In this work, we explored using transcriptomic and proteomic analysis the sialome of Rhipicephalus sanguineus (s.l.) adult female ticks feeding on a rabbit. Instead of grouping the ticks by days of feeding, we instead grouped them into six groups based on their weights which better demarks their feeding physiological state. We also included an unfed group. All groups had three replicates except for the unfed group that had two replicates. A total of 687 million reads from 20 libraries were assembled from which 71,643 coding sequences were extracted, 28,921 of which had a TPM (transcripts per million) of 10 or larger in at least one library. The translated transcripts served as a target database for a proteomic study, which identified 2,125 polypeptides. The correlations between transcriptional and translational results in the different groups were evaluated.

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Developmental Control of Gene Copy Number by Repression of Replication Initiation and Fork Progression

Project description:This SuperSeries is composed of the following subset Series: GSE31895: ChIP with anti-orc2 antibody to identify regions of orc binding in third instar salivary glands of WT and SuUR mutant Drosophila GSE31896: RNAPolII ChIP to find differences between third instar salivary glands of WT and SuUR GSE31897: ChIP with anti-H3K27me3 to compare binding in salivary glands of WT and SuUR Drosophila GSE31898: CGH to ascertain levels of gDNA in third instar salivary glands of various mutant Drosophila GSE31899: ChIP-Seq of ORC2 bound to third instar salivary gland DNA in WT and mutant Drosophila, analyzed by Illumina sequencing GSE33017: Expression profile of third instar larval salivary gland tissue Refer to individual Series

2011-10-17 | E-GEOD-31900 | biostudies-arrayexpress

ChIP-Seq of ORC2 bound to third instar salivary gland DNA in WT and mutant Drosophila, analyzed by Illumina sequencing

Project description:We analyzed ORC2 ChIP-Seq from hand dissected salivary glands of wandering third instar larvae from OrR or SuUR Drosophila. Goals were to ascertain the difference in binding profile between salivary glands expressing and not expressing the Supressor of UnderReplication protein. One replicate is included for each of OrR (WT) or SuUR salivary glands.

2011-10-18 | E-GEOD-31899 | biostudies-arrayexpress

Chromatin immunoprecipitation of the MSL-1 and MSL-3 vs a mock IP in Drosophila and transcription profiling of X linked genes in WT male or female III instar larvae to provide X chromosome wide profiling of MSL-1 distribution and dosage compensation in Drosophila

Project description:Dosage compensation ensures that males and females, despite unequal number of X chromosomes, equalize for X linked gene expression. In Drosophila, it is achieved by a two-fold up-regulation of most of the genes present on the male X chromosome, and requires the association of the Dosage Compensation Complex (DCC) on the X chromosome. One of the main intriguing aspects of dosage compensation is how this complex is able to target specifically hundreds of sites only on the X chromosome in order to ensure dosage compensation. In order to better understand the targeting of the DCC and the dosage compensation mechanism, we have then decided to analyze the distribution of the DCC as well as the expression levels in male and female in a more complete and precise manner, using microarrays. In this experiment, we present the data used to analyse the distribution of the MSL-1 and MSL-3 protein (part of the DCC complex) on the X chromosome in WT embryos aged from 0H-14H, as well as the distribution of MSL-1 in embryos aged from 4-6H and in male III instar salivary glands. The DNA amplified from the specific immunoprecipitation (MSL-1 or MSL-3 IP) were labelled using Cy5-dCTP and hybridized against DNA amplified from a non specific immunoprecipitation (mock IP), labeled with Cy3 dye. In parralel we present the data used to analyse the expression profile of X-linked genes in WT male or female III instar larvae salivary glands. The cDNA amplified from the RNA extracted from the male or female salivary glands were labelled using Cy5-dUTP and hybridized against the reference sample, labelled with Cy3-dUTP (pool RNA from ON embryos, adultes, and salivary glands mixed at a ratio 1:1:1.and amplified as the RNA from salivary glands). We used for this study a cDNA array developed by the Genecore facility in EMBL, covering the DGC1 and DGC2 cDNA libraries from the Berkeley Drosophila Genome Project, which represents more than 70% of the coding Drosophila genome.

2006-04-01 | E-MEXP-554 | biostudies-arrayexpress

RNAPolII ChIP to find differences between third instar salivary glands of WT and SuUR

Project description:ChIP was performed to identify regions of gDNA bound by RNA polymerase II in third instar salivary glands of Drosophila WT and SuUR mutants. This demonstrated that RNAPolII does not localize to regions that are under-replicated in SuUR mutant third instar salivary glands. Comparison of RNAPolII ChIP from third instar salivary glands relative to control IgG pulldown for two different Drosophila strains

2011-10-17 | E-GEOD-31896 | biostudies-arrayexpress

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2008-06-19 | E-GEOD-8623 | biostudies-arrayexpress

RNA Seq Profiling of Murine Salivary Glands in the Presence or Absence of Active MCMV Infection

Project description:Recent work indicates that salivary glands are able to constitutively recruit CD8+ T cells and retain them as tissue resident memory T cells (TRM), independently of local infection, inflammation or antigen. To understand the mechanisms supporting T cell recruitment to the salivary gland, we compared T cell migration to the salivary gland in mice infected or not with murine cytomegalovirus (MCMV), a herpesvirus that infects the salivary gland and promotes the accumulation of salivary gland TRM. We found that acute MCMV infection increased rapid T cell recruitment to the salivary gland, but that equal numbers of activated CD8+ 44 T cells eventually accumulated in both infected and uninfected glands. T cell recruitment to uninfected salivary glands depended on chemokines and the integrin α4. Several chemokines were expressed in the salivary glands of both infected and uninfected mice and many of these could promote the migration of MCMV-specific T cells in vitro. MCMV infection increased expression of chemokines that interact with the receptors CXCR3 and CCR5, but neither receptor was needed for T cell recruitment to the salivary gland during MCMV infection. Unexpectedly however, the chemokine receptor CXCR3 was critical for T cell accumulation in uninfected salivary glands. Together, these data suggest that CXCR3 and the integrin α4 mediate T cell recruitment to uninfected salivary glands, but that redundant mechanisms mediate T cell recruitment after MCMV infection.

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