Project description:. 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.

2023-05-10 | PXD028695 | Pride

L3-L4 Developmental Transcriptome of the human parasitic nematode Brugia malayi and its Wolbachia endosymbiont

Project description:Lymphatic filarial nematodes maintain a mutualistic association with the intracellular bacterium Wolbachia. Wolbachia populations expand following infection of the mammalian host, to support larval growth and development. Utilizing transcriptomic data from Brugia malayi over the first two weeks post-infection, we present an analysis of the biochemical pathways that are involved in Wolbachia population growth and regulation in support of larval development. In Wolbachia, we observe coordinated regulation of carbon metabolism with an alternating pattern of glycolysis and TCA cycle pathways reminiscent of the ‘Warburg effect’. Wolbachia's purine, pyrimidine and haem biosynthesis and Type IV secretion pathways are also upregulated and correlate with the upregulation of the nematode’s DNA replication pathway. In the nematode we observe up-regulation of the autophagy pathway, a key regulator of Wolbachia populations. These findings support a key role for nucleotide and haem provisioning from Wolbachia in support of the larval growth and development of its nematode host.

2021-06-30 | GSE132848 | GEO

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

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