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From the overnight culture, 1 mL of cells were pelleted at 3,500 x g for 10 min and washed twice with 1 mL M9 minimal media to remove any trace of LB media. Pelleted cells were reconstituted in 1 mL minimal media, and then 100 µL was added to 100 mL minimal media (iron-limited media; LIM) and minimal media supplemented with 10 µM iron Fe2(SO4)3 (iron-replete) in quadruplicate. Cultures were grown at 37 °C with 200 RPM shaking and collected at 24 h (late stationary) by pelleting cells at 4,000 x g for 10 minutes and decanting supernatant.   Cell pellets were washed twice with 5 mL phosphate-buffered saline (PBS) and then processed as previously described with some noted deviations. Briefly, cells were resuspended in 100 mM Tris-HCl, pH 8.5, with 2% sodium dodecyl sulphate (SDS; final concentration), proteinase inhibitor and phosSTOP tablets. Cells were lysed using probe sonication (30 s on/ 30 s off in an ice bath, 30% power), reduced with 10 mM dithiothreitol at 95 °C for 10 min (800 rpm), alkylated using 55 mM iodoacetamide for 20 min (room temperature, in the dark) then precipitated using chloroform-methanol precipitation to improve downstream phosphopeptide yield. The pellet was dried in a speedvac at 45 °C for 10 min.  Protein pellets were resuspended in 8 M urea/ 40 mM HEPES buffer and protein concentration was determined using BSA-tryptophan assay. A total of 1 mg protein was digested overnight at room temperature for each replicate of each condition using a 1:50 ratio of trypsin/lysC to protein. Digested samples were dried completely in a SpeedVac at 45 °C, then desalted using PierceTM Peptide Desalting Spin Columns (Thermo Fischer Scientific, 89852) according to the manufacturer’s instructions. Briefly, samples were reconstituted in 0.3 mL 0.1% trifluoroacetic acid (TFA), loaded onto desalting spin columns by centrifuging at 3,000 x g for 1 min, then washed three times with 0.3 mL 0.1% TFA and centrifuged at 3,000 x g for 1 min. Peptides were eluted using 0.3 mL 50% acetonitrile (ACN) 0.1% TFA and collected by centrifuging at 3,000 x g for 1 min. Elution was repeated and combined with initial elution. Desalted peptides were then split, 10% (approx. 100 µg) was aliquoted, dried to completion in speedvac at 45 °C and stored at -80 °C (total proteome samples). The remaining 900 µg were dried to completion in a speedvac at 45 °C then subjected to phosphopeptide enrichment. Phosphopeptide enrichment was performed as previously described using the High Select™ Phosphopeptide Enrichment Kit (Thermo Fisher Scientific, cat no A32992) according to the manufacturer’s instructions, except where indicated otherwise. Briefly, samples were reconstituted in 0.2 mL Binding/Wash buffer, and sample pH was confirmed to be 2.5 using Fischer Scientific 0.0 – 3.0 pH paper (cat no 13-640-511) to improve recovery of acid labile phosphopeptides (pHis and pAsp)44.  Fe-NTA (nitrilotriacetic acid) column was equilibrated by washing twice with 0.2 mL Binding/Wash buffer and centrifuging at 1,000 x g for 30 sec. Samples were incubated with a Fe-NTA column for 15 min (shortened from 30 min) to reduce time in the acidic buffer. The column was washed three times using 0.2 mL Binding/Wash buffer and once with 0.2 mL with MilliQ water by centrifuging at 1,000 x g for 30 sec and then eluted using 0.2 mL Elution buffer, centrifuging at 1,000 x g for 30 sec to collect. Eluted phosphopeptides were dried completely in a speedvac at 45 °C. Total proteome and phosphoenriched samples were reconstituted in 40 µL 0.1% formic acid (FA) and loaded onto Evotips according to the manufacturer’s instructions. For total proteome, 5 µg was loaded per tip; for phosphoenriched samples, 90% of the sample volume was loaded per tip (36 µL). Tips were washed with 40 µL Buffer A by centrifuging at 800 x g for 1 min then 0.2 mL Buffer A were added to tips and pulsed on the centrifuge to remove air bubbles. Samples were separated and analyzed using Evosep One liquid chromatography system coupled with Thermo Scientific Orbitrap Exploris 240 using an 88 min method for total proteome and 44 min method for phosphoenriched samples. Mass spectrometry analysis was performed in data-dependent, positive ion mode using a 15 cm PepSep column with 150 µm diameter and 1.9 µM beads (Evosep, EV1106). The precursor range was set at 350-1800 m/z, 60,000 resolution, 50 msec injection time and an automatic gain control target of 3e6. Dynamic exclusion was set to 10 sec, and charge states 2-8 were included. The fragment ion isolation window was 1 m/z with higher-energy collisional dissociation (HCD) fragmentation energy of 34 eV with 15,000 resolution and a dynamic injection time. First mass was set at 110 m/z for MS2 scans, and the automatic gain control target was set to 2e6."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The .RAW files were processed using MaxQuant v2.4.0.0102 with default parameters except where noted. The peptides identified were searched with the built-in Andromeda103 search engine against K. pneumoniae subsp. pneumoniae K52 serotype (5126 protein sequences from UP000000265 proteome ID; accessed Dec. 2, 2022) from UniProt104. Phosphorylation was included as a variable modification using a modified version of the default phospho STY parameters, which included the addition of pHis and pAsp modifications (neutral loss of H3O4P; mass 97.9768950 Da) and a diagnostic peak for pHis (C5H8O3N3P immonium ion with a mass of 190.037604 m/z after protonation). Phosphopeptide abundance was normalized to the total proteome. Modified and unmodified peptides were included for protein quantification using label-free quantification (LFQ) (ratio count set to 1)74. Other modifications included were carbamidomethylation of cysteine as a fixed modification and methionine oxidation and N-acetylation of proteins as variable modifications. Digestion parameters were set to trypsin specificity with a maximum of 2 missed cleavages. The minimum number of peptides needed to identify a protein was set to 2, and match between runs was enabled with a match window time of 0.7 min and alignment time window of 20 min74. The phospho (STYDH) modifications identified in the “ProteinGroups” file were processed using Perseus v2.0.10.0105, including 1, 2 and 3 phosphorylation multiplicities. Phosphorylated peptides matching contaminants or reverse database were removed, and the remaining phosphopeptides were organized into class I (localization probability >75%), class II (>50%) and III (<50%). Phosphopeptide LFQ intensities were converted to log scale (log2), then samples were filtered to remove peptides identified in less than 3 replicates (valid-value filter of 3 in at least one group). Missing values were replaced with imputation using a 0.3 standard deviation width of the Gaussian distribution and a 1.8 standard deviation down shift. A student’s t-test was used to identify significant changes in protein abundance across different conditions, with a p-value of less than or equal to 0.05, a Benjamini–Hochberg false discovery rate (FDR) of 5%, and an S0 value of 1."],"omics_type":["Proteomics"],"labhead":["Jennifer Geddes-McAlister"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Molecular and Cellular Biology, University of Guelph, Canada"],"species":["Klebsiella Pneumoniae Subsp. Pneumoniae"],"publication":["Not available"],"submitter_mail":["reitzelc@uoguelph.ca"],"submitter_affiliation":["University of Guelph"],"submitter_country":["Canada"],"additional_accession":[]},"is_claimable":false,"name":"Phosphoproteome modulation by zinc and iron in Klebsiella pneumoniae reveals new virulence mechanisms and antibacterial targets","description":"Klebsiella pneumoniae is a Gram-negative bacterium causing 10-20% mortality in immunocompromised individuals and is known to rapidly develop resistance towards existing antibiotics. This underscores a need for novel antimicrobials or strategies for resensitization. Bacterial adaptation to iron and zinc, which are key nutrients linked to growth, division, and virulence, offers promising targets for antibiotic intervention. In this thesis, mass spectrometry-based phosphoproteomics was used to profile K. pneumoniae in iron/zinc-replete and -limited media, identifying 574 phosphopeptides from 358 phosphoproteins. Two candidates, SbmA and TolQ, were selected for disruption based on hypothesized roles in iron acquisition and membrane stabilization, respectively. Through iron quantification assays, growth curves, electron microscopy, antibiotic susceptibility testing and infection assays, we identified a previously uncharacterized role for SbmA in iron acquisition and identified reduced growth, viability, increased β-lactam susceptibility, and enhanced immune clearance for ΔtolQ. High-throughput drug screening revealed two compounds that target SbmA or TolQ, reducing bacterial growth and enhance immune clearance. Together, these findings highlight phosphoproteomics as a powerful tool for identifying nutrient-regulated targets and position TolQ and SbmA as promising candidates for antimicrobial development.","dates":{"publication":"2026-04-15","submission":"2025-12-20"},"accession":"PXD072239","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","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: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","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: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:7719","NEWT:5530","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:49928","NEWT:3349","NEWT:160621","NEWT:212790","NEWT:110368","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: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:270643","NEWT:3715","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","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: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:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","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:108458","NEWT:5936","NEWT:321967","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:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","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:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","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: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: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","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:64657","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","NEW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