{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD047714/filetosample.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD047714/checksum.txt"],"Pdf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD047714/LCMSmethod-L2.pdf"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD047714/mqpar.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD047714/PI22-26697-L2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD047714/PI22-26696-L2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD047714/PI22-26698-L2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD047714/PI22-26699-L2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD047714/PI22-26700-L2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD047714/PI22-26835-L2.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD047714/Contaminats_2019.03.03.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD047714/VectorBase-57_AaegyptiLVP_AGWG_AnnotatedProteins.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD047714/Search.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["jribeiro@niaid.nih.gov"],"submitter":["Thiago Silva"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["A comprehensive proteomics analysis of the hemolymph composition of sugar-fed aedes aegypti female and male mosquitoes"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD047714"],"tissue":["Hemolymph"],"sample_protocol":["Three independent pools containing hemolymph samples from 40 mosquitoes/each (4-6 days old sugar-fed male or female) were obtained by perfusion and prepared as follows. Mosquitoes were immobilized on ice and placed individually under a stereoscope on a slide on the lid of a Petri dish filled with ice. Carefully, using fine tip forceps, a very small superficial incision was made in the lateral region of the VI-VII abdominal segment. Then, with the mosquito positioned sideways, a heat-stretched capillary needle filled with sterile PBS was gently inserted into the thorax. The pierced mosquito was lifted via a micromanipulator, and a total of approximately 10 µL of sterile PBS was gently injected in the thorax. Perfused hemolymph was collected through the abdominal incision with a pipette and transferred immediately to a Protein LoBind tube (Eppendorf) on ice. If any turbidity on the hemolymph being collected from the mosquito was observed, indicative of high contamination from fat body or other tissues, the sample was discarded and not added to the pool. To obtain cell free hemolymph for proteomics analysis, samples were immediately centrifuged at 1,000 x g for 10 minutes at 4oC, the supernatant was saved, and the pellet was discarded. An aliquot of each pool was used to measure protein concentration (Pierce Micro BCA protein assay kit, cat # 23235) and run a gel as described below. The remaining was stored at a -80oC freezer until use for mass spectrometry runs. To assess the protein profile of the pools, a 5µL aliquot of each was run on a 4-12% NuPAGE Bis-Tris mini gel (Thermo Fisher #NP0322BOX), under denaturing and reducing conditions, using MES buffer (Thermo Fisher #NP000202).  After running, gels were stained using Pierce Silver Stain for mass spectrometry kit (Thermo Fisher # 24600) following manufacturer’s instructions."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Pooled hemolymph samples (10µg of protein quantified by BCA assay) were thawed on ice and the urea concentration was adjusted to 5M by the addition of 8M urea, 50mM HEPES at pH 8.5. To attain a final volume of 0.25ml, adjustments were made using HEPES-buffered 5M urea solution. For reduction, DTT was added to a final concentration of 5mM, followed by incubation at 37°C for 40 minutes. The samples were treated with 15mM iodoacetamide and incubated for 30 minutes RT. The urea concentration was lowered to 2M by adding 50mM HEPES pH 8.0, and then 200ng of LysC protease was added. After a 3 hrs incubation at 37°C , 800ng of trypsin was added. The samples were incubated for 15 hours at 37°C, then acidified to pH 2.0 with trifluoroacetic acid (TFA), desalted and concentrated on an Oasis HLB micro-elution plate. The samples were eluted with a solution 1:1 of 0.1% TFA and acetonitrile and dried under vacuum. The residue was dissolved in 15µl of injection solvent, 0.1% formic acid, 3% acetonitrile, and peptide quantitation was done by fluorescent assay (Pierce Quantitative Fluorometric Peptide Assay).  The LC-MS experiments were performed using the Orbitrap Fusion Lumos mass spectrometer connected to an EASY nLC 1200 nano-liquid chromatography system (Thermo Fisher Scientific). The peptide samples were loaded to a PepMap C18 trap column (3µm particle, 100Å pore, 75µm inner diameter, 2cm length) and separated using an EASY-Spray analytical column (PepMap C18, 2µm particle, 100Å pore, 75µm inner diameter, 25cm length) by a 120-min acetonitrile gradient (from 0 to 24% acetonitrile for the first 80 min, then 24 to 48 % for the next 40 min) at the flow rate of 200 nL/min. The mobile phase solvent contained 0.1% formic acid. The analytical column was kept at 50°C. The data acquisition was done with a standard data-dependent acquisition scheme, where the survey MS1 scan was done every 3 seconds with the Orbitrap mass analyzer at the 120,000-resolution setting, and MS2 scans were done for multiply charged precursor ions isolated with m/z 1.6 window using the Quadrupole and fragmented by HCD at the normalized collision energy of 25% then scanned with the Orbitrap mass analyzer at the 15,000-resolution setting. The dynamic exclusion period was set at 60 sec, and the EASY-IC internal calibration was performed at the start of each experiment.  Protein annotation, identification and quantification  Mass spectrometry raw files were analyzed using the MaxQuant software version 2.4.0.0 (Max‐Planck‐Institute of Biochemistry, https://www.maxquant.org) against Aedes aegypti FASTA database (VectorBase‐57_AaegyptiLVP_AGWG_AnnotatedProteins.fasta from https://vectorbase.org/) with the default parameters.  Briefly, digestion was set Trypsin/P with Max. missed cleavage of 2.  Cysteine carbamidomethylation was set as a fixed modification, while N‐terminal acetylation and methionine oxidations as variable modifications.  The ‘matching between runs’ feature was enabled. For stringency, only proteins containing at least three unique peptides were considered.  For stringency, only proteins containing at least three unique peptides were considered. MS1‐based label‐free quantification (LFQ) was done using the maxLFQ algorithm with a minimum ratio count of 2. All statistical analyses were performed with the Perseus software. Initially, protein groups identified only by site, matching contaminants, or reverse database were filtered out. Protein intensities based on LFQ were Log2 transformed, and each sample (pool containing hemolymph from 40 mosquitoes) was centered by subtracting the median of the protein distribution. We considered only proteins with computed LFQ greater than zero in at least 4 pools for the characterization of protein composition and statistical analysis. Missing values for low-abundant proteins were imputed based on the normal distribution for each sample using the random forest imputation method. Differential expression was assessed using a t-test with 250 permutations as a form of truncation, and p-values were adjusted for multiple testing using the Benjamini-Hochberg procedure, with a false discovery rate (FDR) threshold set at 0.05. Comparison of abundance of proteins within the same pool was based on their intensity-based absolute quantification (iBAQ), calculated using MaxQuant software."],"omics_type":["Proteomics"],"labhead":["Jose Marcos Chaves Ribeiro"],"instrument_platform":[""],"labhead_affiliation":["National Institutes of Health"],"submission_type":["PARTIAL"],"species":["Aedes Aegypti"],"submitter_mail":["thiagoluiz.alvesesilva@nih.gov"],"publication":["38576391 Alvarenga PH, Alves E Silva TL, Suzuki M, Nardone G, Cecilio P, Vega-Rodriguez J, Ribeiro JMC, Andersen JF. Comprehensive Proteomics Analysis of the Hemolymph Composition of Sugar-Fed <i>Aedes aegypti</i> Female and Male Mosquitoes. J Proteome Res. 2024 23(4):1471-1487 10.1021/acs.jproteome.3c00918"],"submitter_affiliation":["National Institutes of Health"],"submitter_country":["Brazil"],"pubmed_abstract":["In arthropods, hemolymph carries immune cells and solubilizes and transports nutrients, hormones, and other molecules that are involved in diverse physiological processes including immunity, metabolism, and reproduction. However, despite such physiological importance, little is known about its composition. We applied mass spectrometry-based label-free quantification approaches to study the proteome of hemolymph perfused from sugar-fed female and male <i>Aedes aegypti</i> mosquitoes. A total of 1403 proteins were identified, out of which 447 of them were predicted to be extracellular. In both sexes, almost half of these extracellular proteins were predicted to be involved in defense/immune response, and their relative abundances (based on their intensity-based absolute quantification, iBAQ) were 37.9 and 33.2%, respectively. Interestingly, among them, 102 serine proteases/serine protease-homologues were identified, with almost half of them containing CLIP regulatory domains. Moreover, proteins belonging to families classically described as chemoreceptors, such as odorant-binding proteins (OBPs) and chemosensory proteins (CSPs), were also highly abundant in the hemolymph of both sexes. Our data provide a comprehensive catalogue of <i>A. aegypti</i> hemolymph basal protein content, revealing numerous unexplored targets for future research on mosquito physiology and disease transmission. It also provides a reference for future studies on the effect of blood meal and infection on hemolymph composition."],"pubmed_title":["Comprehensive Proteomics Analysis of the Hemolymph Composition of Sugar-Fed <i>Aedes aegypti</i> Female and Male Mosquitoes."],"pubmed_authors":["Alvarenga Patricia H PH, Alves E Silva Thiago Luiz TL, Suzuki Motoshi M, Nardone Glenn G, Cecilio Pedro P, Vega-Rodriguez Joel J, Ribeiro Jose M C JMC, Andersen John F JF"],"additional_accession":[]},"is_claimable":false,"name":"A comprehensive proteomics analysis of the hemolymph composition of sugar-fed Aedes aegypti female and male mosquitoes","description":"In arthropods, hemolymph carries immune cells and solubilizes and transport nutrients, hormones, and other molecules that are involved in diverse physiological processes including immunity, metabolism and reproduction. However, despite such physiological importance, little is known about its composition. We applied mass spectrometry-based label free quantification approaches to study the proteome of hemolymph perfused from sugar-fed female and male Aedes aegypti mosquitoes. A total of 1,403 proteins were identified, 447 of them predicted to be extracellular. In both sexes almost half of these extracellular proteins were predicted to be involved in defense/immune response, and their relative abundance (based on their intensity based absolute quantification, iBAQ) were 37.9% and 33.2%, respectively. Interestingly, among them 102 serine proteases/serine protease-homologs were identified, almost half of them containing CLIP regulatory domains. Moreover, proteins belonging to families classically described as chemoreceptors, like odorant-binding proteins (OBPs) and chemosensory proteins (CSPs) were also highly abundant in the hemolymph of both sexes. Our data provide a comprehensive catalogue of Ae. aegypti hemolymph basal protein content, revealing numerous unexplored targets for future research on mosquito physiology and disease transmission. It also provides a reference for future studies on the effect of blood meal and infection on the hemolymph 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