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Silva"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Infection","Plasmodium","Mosquito","Proteome","Salivary gland","Saliva"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD057587"],"tissue":["Saliva"],"sample_protocol":["For the proteome, we performed infections with a transgenic GFP P. berghei parasite strain (ANKA GFPcon 259cl2). For all the other assays, we used P. berghei (Pb) ANKA transgenic line expressing mCherry and luciferase markers under the control of the hsp70 and eef1a promotors, respectively (73). Parasitemia was quantitatively assessed by light microscopy using methanol-fixed, 10% Giemsa-stained blood smears. For mosquito infections, female mosquitoes (4-5 days old) were fed on infected mice once flagellation reached 3-4 ex flagellations per 40 x field. After feeding, infected mosquitoes were kept at 19°C, 80% humidity, and a 12-hour light-dark cycle. Mosquitoes with a productive infection in the salivary glands were sorted using a fluorescent scope (Leica M205 FCA coupled to a camera DFC 7000 G5 for multi-color fluorescence imaging).  Female An. gambiae mosquitoes were infected with P. falciparum NF54 via membrane feeding using reconstituted human blood (74). The asexual blood-stage cultures were maintained in vitro using O+ erythrocytes at a 4% hematocrit, as previously described (74). For mosquito infections, a suspension of human RBCs was mixed with human serum (Interstate blood bank) at 50% hematocrit and diluted to 0.05% gametocytemia before being fed to the mosquitoes. Post-infection, the mosquitoes were kept at 25°C and 80% humidity and provided with a 10% (w/v) sucrose solution. For saliva collection, forced salivation was used on 50 female mosquitoes. Four independent infections with P. berghei or P. falciparum were performed for this assay; either of these parasites was paired with an uninfected sample. The mosquitoes were water-deprived for approximately 1–2 hours before collection. After sedation on ice, the mosquitoes' mouthparts were inserted into 10 μl tips containing 8 μl of PBS supplemented with 2% pilocarpine (Sigma-Aldrich). The mosquitoes were then allowed to salivate for 30 minutes at 28°C. The saliva solutions were subsequently pooled into Protein Lo-Bind tubes (Eppendorf) and stored at -80°C until further use.  The samples dissolved in SDS-PAGE sample buffer were run on an SDS-PAGE minigel. The gels were stained with Coomassie blue (ProtoBlue Safe, National Diagnostics) overnight. For the saliva samples the top gel slices were excised and cut in two pieces. Next, the excised slices were cut into small pieces, and subjected to in-gel trypsin digestion. Briefly, the gel pieces were destained with 50% acetonitrile in 100mM AMBI, reduced with 5mM DTT, and alkylated in 11mM iodoacetamide. The pieces were then dehydrated with 50%, followed by 100%, acetonitrile. Afterward, 10 ng/µL mass-spec-grade trypsin (Promega) was added, allowing the trypsin solution to soak into the gel. Following overnight digestion at 30°C, the peptides were extracted with acetonitrile in formic acid and subjected to LC-MS/MS analysis. LC-MS/MS data were acquired using an Orbitrap Fusion Lumos mass spectrometer equipped with an EASY-Spray Ion Source and an EASY-nLC 1200 liquid chromatography system (Thermo Fisher Scientific). The mobile phase consisted of water with 0.1% formic acid. Peptides (5 μL) were loaded onto a trap column (PepMap 100 C18, 3 μm particle size, 2 cm length, 75 μm inner diameter, Thermo Fisher Scientific), and separated on an analytical column (PepMap 100 C18, 2 μm particle size, 25 cm length, 75 μm inner diameter, Thermo Fisher Scientific) using a linear gradient: 0–40% acetonitrile over 80–100 minutes, 40–80% for 5 minutes, holding at 80% for 5 minutes, 80–0% for 5 minutes, and holding at 0% for 5 min. Throughout this 120-min data acquisition, the flow rate was set at 300 nL/min, with the analytical column maintained at 50 °C. Data acquisition followed a standard data-dependent acquisition strategy. MS1 scans were performed every 2 seconds using the Orbitrap mass analyzer at a resolution of 120,000. MS2 scans were performed on multiply charged precursor ions, isolated with a 1.6 m/z window using a quadrupole, and fragmented by CID at 35% collision energy, analyzed with the Linear Ion Trap. A dynamic exclusion period of 30 seconds was applied, and EASY-IC internal calibration was used for Orbitrap scans."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Saliva P. berghei: LC-MS/MS data were processed using MaxQuant software (v2.0.3.0.) (24). Raw data files from each sample were loaded as fractions and searched against the Anopheles gambiae PEST annotated protein database (VectorBase, release 51) and Plasmodium berghei ANKA protein database (PlasmoDB, release 51), with the MaxQuant contaminants database included. Peptide identification allowed for fixed cysteine carbamidomethylation and variable modifications of N-terminal acetylation and methionine oxidation. A 1% false discovery rate (FDR) was applied, and the match between runs feature was enabled. Protein quantification was performed using iBAQ intensity to generate LFQ intensity, which was reported as log2 values in tables and figures. Only proteins with at least three unique peptides were included, and contaminants were excluded from further analysis.  Statistical analyses were performed using Perseus software (75). Protein intensities were log2-transformed and normalized by median centering. Only proteins with LFQ values greater than zero were included in the analysis. Missing values were imputed using a random normal distribution, with the mean set to the observed distribution mean minus 1.8 standard deviations and the standard deviation set to 0.3 times the observed standard deviation. Differential expression was assessed using Student’s t-test with permutation-based FDR control. Heatmaps were generated on Perseus, and PCA plots were generated using GraphPad. Protein annotation: For protein annotation, we employed an in-house program that analyzes BLASTp and rpsBLAST results across various databases, including UniProtKB, Conserved Domain Database (CDD), REFSEQ-Invertebrate, Diptera, and FlyBase. This program evaluates approximately 400 keywords and their order of appearance in the protein matches, considering e-values and sequence coverage. Signal peptides were predicted using SignalP 5.0. Protein abundance was quantified using intensity-based absolute quantification (iBAQ). Relative abundances within each pool were calculated by dividing individual iBAQ values by the total sum of iBAQ values for that pool (25, 26, 76). Saliva P. falciparum: LC-MS/MS data were processed using MaxQuant software (v2.0.3.0.) (24). Raw data files from each sample were loaded as fractions and searched against the Anopheles gambiae PEST annotated protein database (VectorBase, release 51) with the MaxQuant contaminants database included. For Plasmodium falciparum samples, the P. falciparum NF54 protein database (release 51) was used. Peptide identification allowed for fixed cysteine carbamidomethylation and variable modifications of N-terminal acetylation and methionine oxidation. A 1% false discovery rate (FDR) was applied, and the match between runs feature was enabled. Protein quantification was performed using iBAQ intensity to generate LFQ intensity, which was reported as log2 values in tables and figures. Only proteins with at least three unique peptides were included, and contaminants were excluded from further analysis.  Statistical analyses were performed using Perseus software (75). Protein intensities were log2-transformed and normalized by median centering. Only proteins with LFQ values greater than zero were included in the analysis. Missing values were imputed using a random normal distribution, with the mean set to the observed distribution mean minus 1.8 standard deviations and the standard deviation set to 0.3 times the observed standard deviation. Differential expression was assessed using Student’s t-test with permutation-based FDR control. Heatmaps were generated on Perseus, and PCA plots were generated using GraphPad. Protein annotation: For protein annotation, we employed an in-house program that analyzes BLASTp and rpsBLAST results across various databases, including UniProtKB, Conserved Domain Database (CDD), REFSEQ-Invertebrate, Diptera, and FlyBase. This program evaluates approximately 400 keywords and their order of appearance in the protein matches, considering e-values and sequence coverage. Signal peptides were predicted using SignalP 5.0. Protein abundance was quantified using intensity-based absolute quantification (iBAQ). Relative abundances within each pool were calculated by dividing individual iBAQ values by the total sum of iBAQ values for that pool (25, 26, 76)."],"omics_type":["Proteomics"],"labhead":["Joel Vega Rodriguez"],"instrument_platform":[""],"labhead_affiliation":["Molecular Parasitology and Entomology Unit,Laboratory of Malaria and Vector Research, National Institutes of Health. USA."],"submission_type":["PARTIAL"],"species":["Plasmodium Falciparum Nf54","Plasmodium Berghei Anka","Anopheles Gambiae Str. Pest"],"publication":["41266344 Alves E Silva TL, Kanatani S, Barletta Ferreira AB, Schwartz CL, Liffner B, Talyuli OAC, Olivas J, Nagata BM, Pala ZR, Pascini T, Alves DA, Zhao M, Suzuki M, Dorner LP, Frischknecht F, Coppens I, Barillas-Mury C, Absalon S, Ribeiro JMC, Sinnis P, Vega-Rodriguez J. High-resolution proteomics unveils salivary gland disruption and saliva-hemolymph protein exchange in Plasmodium-infected mosquitoes. Nat Commun. 2025 16(1):10205 10.1038/s41467-025-64837-6"],"submitter_mail":["thiagoluiz.alvesesilva@nih.gov"],"submitter_affiliation":["National Institutes of Health"],"submitter_country":["Brazil"],"pubmed_abstract":["Plasmodium sporozoites, the infective stage of malaria, must invade the mosquito salivary glands (SGs) before being transmitted to a vertebrate host. However, the physiological and biochemical effects of this invasion remain largely unexplored. We examined the impact of Plasmodium infection on Anopheles gambiae salivary glands using high-resolution proteomics, gene expression, and morphological analysis. The data reveal differential expression of various proteins, including the enrichment of hemolymph-derived humoral proteins in infected salivary glands. These proteins diffuse into the SGs due to structural damage caused by the sporozoites during invasion, while saliva proteins diffuse out into the circulation. Moreover, proteomic analysis of saliva from P. berghei- or P. falciparum-infected mosquitoes revealed changes in composition, with a pronounced reduction of immune proteins relative to uninfected mosquitoes. This reduction is likely due to the association of these proteins with the surface of sporozoites and/or changes in the saliva's physical properties within the invaded salivary secretory cavities. The saliva protein profiles from mosquitoes infected with both Plasmodium species are remarkably similar, suggesting a conserved interaction between sporozoites and salivary glands. Our results provide a foundation for understanding the molecular interactions between Plasmodium sporozoites and mosquito salivary glands."],"pubmed_title":["High-resolution proteomics unveils salivary gland disruption and saliva-hemolymph protein exchange in Plasmodium-infected mosquitoes."],"pubmed_authors":["Alves E Silva Thiago Luiz TL, Kanatani Sachi S, Barletta Ferreira Ana Beatriz AB, Schwartz Cindi L CL, Liffner Benjamin B, Talyuli Octavio A C OAC, Olivas Janet J, Nagata Bianca M BM, Pala Zarna Rajeshkumar ZR, Pascini Tales T, Alves Derron A DA, Zhao Ming M, Suzuki Motoshi M, Dorner Lilian P LP, Frischknecht Friedrich F, Coppens Isabelle I, Barillas-Mury Carolina C, Absalon Sabrina S, Ribeiro Jose M C JMC, Sinnis Photini P, Vega-Rodriguez Joel J"],"additional_accession":[]},"is_claimable":false,"name":"High-Resolution Proteomics Unveils Salivary Gland Disruption and Saliva-Hemolymph Protein Exchange in Plasmodium-Infected Mosquitoes","description":"Plasmodium sporozoites, the stage that initiates a malaria infection, must invade the mosquito salivary glands before transmitting to a vertebrate host. However, the effects of sporozoite invasion on salivary gland physiology and saliva composition remain largely unexplored. We examined the impact of Plasmodium infection on Anopheles gambiae salivary glands using high-resolution proteomics, gene expression, and morphological analysis. The data revealed differential expression of various proteins, including the enrichment of humoral proteins in infected salivary glands originating from the hemolymph. These proteins diffused into the SGs due to structural damage caused by the sporozoites during invasion. Conversely, saliva proteins diffused out into the circulation of infected mosquitoes. Moreover, infection altered saliva protein composition, as shown by proteomes from saliva collected from mosquitoes infected by P. berghei or P. falciparum, revealing a significant reduction of immune proteins compared to uninfected mosquitoes. This reduction is likely due to the association of these proteins with the surface of sporozoites within the mosquito salivary secretory cavities. The saliva protein profiles from mosquitoes infected with both Plasmodium species were remarkably similar, suggesting a conserved interaction between sporozoites and salivary glands. Our results provide a foundation for understanding the molecular interactions between Plasmodium sporozoites and mosquito salivary glands.","dates":{"publication":"2026-07-06","submission":"2024-11-06"},"accession":"PXD057587","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:28550","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:441772","NEWT:48106","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:300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