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Nita-Lazar"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Escherichia coli","Neutrophils","Secretome","Lps","Francisella tularensis"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072780"],"tissue":["Primary Cell"],"sample_protocol":["Human PMNs were lysed in 8 M urea supplemented with protease and phosphatase inhibitors (ThermoFisher, USA). Lysates were stored at -80°C. Protein concentration of lysates were measured using the BCA assay (ThermoFisher, USA), following the manufacturer’s instructions. Proteins were reduced with 10 mM Tris(2-carboxyethyl)phosphine (TCEP) at 37°C for 45 min, followed by alkylation with 20 mM chloriacetamide (CAM) at 25°C for 30 min. Urea concentration was diluted to <1 M using 50 mM ammonium bicarbonate. Samples were digested with sequencing-grade trypsin (Promega, USA) at a 1:25 enzyme-to-protein ratio for 18 h at 37°C. Digestion was stopped by acidification with 10% formic acid to reach pH ~3. Samples were centrifuged and supernatants were dried via SpeedVac. Peptides were cleaned using C18 ZipTips (Millipore, USA), following a dual buffer protocol (0.1% formic acid / 80% acetonitrile). Dried peptides were resuspended in 0.1% formic acid and quantified using a Nanodrop spectrophotometer, then samples were diluted to 0.2 µg/µL for LC-MS/MS injection. All steps were performed with MS-grade water.   Secretome. Protein extraction and sample preparation. Supernatants free of cells were collected and dried to completeness overnight in a speed-vac at room temperature. Briefly, the resulting pellet was resuspended in sample buffer and loaded into NuPAGE 4–12% Bis-Tris gels (Thermo Fisher Scientific, USA). Samples were submitted to gel electrophoresis for 10 min at 200 V, 3 A, and 300 W, until proteins entered the resolving gel without extensive separation. Gels were subsequently stained with Coomassie Blue and destained overnight. Protein-containing regions were excised and cut into small pieces for in-gel digestion. Gel pieces were destained with water and dehydrated in 100% acetonitrile (ACN) until gel particles became white-opaque, followed by drying in a speed-vac. Proteins were reduced with 10 mM dithiothreitol (DTT) in 100 mM ammonium bicarbonate (ABC) at 56 °C for 30 min and alkylated with 55 mM iodoacetamide (IAA) in 100 mM ABC for 30 min at room temperature in the dark. After sequential washes with ABC and ACN, gel pieces were dried and rehydrated with sequencing-grade trypsin (Promega, USA) (10 ng/µL in 10 mM ABC), allowed to swell at 4 °C for the first hour, with additional ABC to cover all gel pieces, and then proceed to digestion overnight at 37 °C. Peptides were extracted stepwise with 50% ACN/ 5% TFA, 75% ACN/ 0.1% TFA, and 100% ACN, pooled, and dried to completeness in a speed-vac. Dried peptide extracts were stored at −80 °C until LC-MS/MS analysis. Dried peptides were resuspended in 0.1% formic acid and quantified using a Nanodrop spectrophotometer, then samples were diluted to 0.2 µg/µL for LC-MS/MS injection. All steps were performed with MS-grade water."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw MS data were processed using Spectronaut™ (v19.5, Biognosys), direct DIA analysis (no spectral library required), against the UniProt Homo sapiens reference proteome (2024-03-15). The resulting quantitative data were exported normalized and further analyzed in R (v4.3.1). Data curation included log2 transformation, proteins were retained if they were quantified in at least 2 of 3 biological replicates for each condition (treatment and time) and missing values were imputed using median of the condition (for global proteomics) or MinProb (Secretome). PCA visualizations were generated using ‘ggplot2’ and ‘plotly’ packages. Hierarchical clustering heatmaps of proteins were generated using ‘pheatmap’ package, displaying z-scored intensities grouped by treatment, donor and time. Differentially expressed proteins (DEPs) were identified using ‘limma’ package. At each time point (0.5h, 1h, 3h, 6h), linear models were fitted per protein with treatment as a fixed effect and donor as a blocking factor. DEP were subjected to functional enrichment analysis using the ‘clusterProfiler’ package. Gene Ontology (GO) Biological Process and KEGG pathway enrichment were conducted using hypergeometric testing with human gene annotation from ‘org.Hs.eg.db’. Enrichment background was defined as the set of proteins retained after filtering."],"omics_type":["Proteomics"],"labhead":["Aleksandra Nita-Lazar"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Functional Cellular Networks Section, Laboratory of Immune System Biology, NIAID, NIH"],"species":["Homo Sapiens (human)"],"publication":["41819446 Pittaluga Villarreal JR, Kim D, Yoon SH, Bhushan V, Issara-Amphorn J, Pederson J, Manes NP, Nita-Lazar A. Structural diversity of lipid A modulates neutrophil proteome and secretome responses. J Proteomics. 2026 328:105643 10.1016/j.jprot.2026.105643"],"submitter_mail":["nitalazarau@niaid.nih.gov"],"submitter_affiliation":["NIAID"],"submitter_country":["United States"],"pubmed_abstract":["Neutrophils (PMNs) are central effector cells of the innate immune system, deploying antimicrobial functions such as degranulation, ROS production, and release of antimicrobial mediators. However, the neutrophil reprogramming in response to structurally distinct lipopolysaccharide (LPS) stimuli remains incompletely defined. Here, we integrated functional profiling with quantitative high-resolution proteomics to compare human PMN responses to two LPS preparations differing primarily in lipid A acylation: hexaacylated LPS from Escherichia coli (ECO-LPS) and tetra-acylated LPS from Francisella tularensis (FT-LPS). Principal component analysis (PCA) revealed that inter-donor variability was the dominant source of variation. ECO-LPS induced clear activation phenotypes and robust, time-dependent proteome remodeling, including early loss of L-selectin and progressive depletion of granule-associated proteins concomitant with increased abundance of inflammatory signaling proteins. In contrast, FT-LPS treated PMNs were indistinguishable from controls at the cellular proteome level. In the secretome, ECO-LPS treatment caused enrichment of neutrophil degranulation and granule lumen components, consistent with intracellular depletion of granules. FT-LPS elicited limited secretory changes, suggesting a restrained activation or primed state without coordinated intracellular remodeling. Together, our results demonstrate that lipid A acylation is a key determinant of neutrophil activation state and provide a resource for defining proteomic signatures associated with LPS sensing. SIGNIFICANCE: Neutrophils are essential first- responder cells of the innate immune system, and their activation is classically studied using targeted sets of surface markers and functional readouts, while the proteome- and secretome-level dynamics remain less well defined. By applying quantitative DIA proteomics to both the intracellular proteome and the secretome of primary human neutrophils, this study reveals how lipid A structure dictates the depth and coordination of neutrophil activation. The data demonstrate that hexaacylated LPS drives coordinated depletion of degranulation-associated proteins with a concomitant appearance in the secretome. In contrast, tetra-acylated LPS fails to induce comparable intracellular remodeling and instead produces only subtle secretory responses consistent with restrained activation. These findings refine our mechanistic understanding of how structurally distinct endotoxins differentially regulate neutrophil effector functions, emphasize the donor-intrinsic proteomic variation, and provide a reference that can guide future studies of attenuated innate sensing and neutrophil-focused therapeutic approaches."],"pubmed_title":["Structural diversity of lipid A modulates neutrophil proteome and secretome responses."],"pubmed_authors":["Pittaluga Villarreal Jose R JR, Kim Doeun D, Yoon Sung Hwan SH, Bhushan Vanya V, Issara-Amphorn Jiraphorn J, Pederson Jacob J, Manes Nathan P NP, Nita-Lazar Aleksandra A"],"additional_accession":[]},"is_claimable":false,"name":"Structural  Diversity of Lipid A Modulates Neutrophil Proteome and Secretome Responses","description":"We applied quantitative high-resolution proteomics to systematically evaluate how the human PMN proteome is shaped in response to two LPS preparations that differ primarily in the number of acyl chains associated with their lipid A (E. coli and F. tularensis LPS). To capture both stimulus-specific effects and response kinetics, PMNs were analyzed at multiple time points, allowing assessment of treatment-dependent differences and proteomic changes over time within each condition. We characterized the PMN secretome following exposure to these agents, enabling the comparison of process between intracellular proteomic and protein release. Together, this integrated cellular proteome and secretome approach provides a comprehensive framework to define how structurally distinct LPS molecules modulate PMN functional programs over time. While PMN responses to LPS have been extensively investigated, their temporal proteomic and secretory landscapes in primary human PMNs, particularly in response to LPS with divergent lipid A architectures, remain incompletely characterized.","dates":{"publication":"2026-04-27","submission":"2026-01-08"},"accession":"PXD072780","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:3715","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:299467","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:10804","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012"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