Project description:Paleoproteomics is the proteomics analysis of ancient proteins, which may be better preserved than DNA in fossil inclusions and particularly in amber fossilized tree resin. However, only yeast proteins have been previously suggested as identified by paleoproteomics analysis conducted in fossil amber. In this study, we developed and applied a paleoproteomics approach to study fossil arthropod inclusions in five Burmese (also known as Burmite and Kachin) amber (Cretaceous, ca. 99 mya) pieces. The results of morphological analysis supported the first report of fossil scavenger mite (Holothyrida, Neothyridae) together with co-inclusions of putative lacewing larva (Neuroptera, Chrysopidae) and thrip Frankliniella sp. (Thysanoptera, Thripidae), the identification of Cornupalpatum sp. (Ixodidae), and two mites Prostigmata (Acari, Trombidiformes, Tetranychidae). A control amber fragment derived from the piece with mite-lacewing-thrip co-inclusions was included in the analysis. The paleoproteomics analysis was conducted by Mass Spectrometry (MS) and Liquid Chromatography-Tandem Mass Spectrometry by searching results from all fossil amber pieces against a compile database containing all sequences from Acari, Insecta and Enterobacterales taxonomies in Uniprot together with contaminants database supplemented with human keratins and bovine trypsin. Identified proteins were selected for analysis based on those identified by MS with more than two peptides per protein and at least one peptide with 1% FDR. Paleoproteomics identified protein orthologs present in fossil amber inclusions of ca. 99 mya in arthropods and other organisms. These results provide a paleoproteomics approach to complement morphological studies in amber inclusions.
2026-03-23 | PXD066794 | Pride
Project description:microRNAof expression in Hyalomma anatolicum anatolicum (Acari: Ixodidae) ticks
| PRJNA698374 | ENA
Project description:microRNA expression in Hyalomma anatolicum anatolicum (Acari: Ixodidae) ticks
Project description:Paleoproteomics approaches the study of proteins by proteomics analysis in fossil samples. Recently, a protocol was developed and validated for paleoproteomics characterization of fossil arthropod parasitiformes in amber inclusions. In this study, the paleoproteomics approach was applied to arthropod fossil amber inclusions to characterize fossil holobiont with possible interactions between different organisms. The study targeted two arachnid fossil inclusions in Burmese amber (also known as Burmite or Kachin amber Cretaceous, ca. 99 mya). Although details of the dorsal and ventral idiosoma are equivocal, the results supported that fossils appear to belong to mites Prostigmata (Acari:Trombidiformes:Tetranychidae). Paleoproteomics analysis included peptide false-discovery rate (FDR), E-value of identified sequences in the UniProt databases with betweenness - PageRank centrality range (PR > 0.40) in phylogenetic analysis, and protein assigned score (PAS = E-value x PR). The analysis identified six Ubiquitin-like, Ig-like domain-containing and Peroxiredoxin-like proteins associated with mite species, thus supporting morphological findings. Ubiquitin-like proteins were also identified in ticks with similar sequence and structure to mite-derived protein. Other identified peptides were assigned to Ubiquitin-like proteins in birds and a parasitic nematode. The results suggested ancient holobiont composition with mite-bird-parasite interactions. The results are supported by ancient and modern interactions between these organisms. Despite current paleoproteomics limitations under investigation, these results advanced the characterization of fossil proteins relevant for the molecular evolution of Parasitiformes and the fossil holobiont in acari-host-parasite interactions.