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Pavan"],"technology_type":["Glycoproteomics","Mass Spectrometry"],"disease":["Acute Leukemia","Disease Free"],"software":[""],"submitter_keywords":["Fc γ (gamma) receptor iiia","High mannose n-linked glycans","Monocytes","Fcγriiia","Cd16a","Immunotherapy","Igg","Parallel reaction monitoring","Glycosylation","N162","Oligomannose"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD071784"],"tissue":["Blood Cell","Monocyte","Cell Culture","Blood"],"sample_protocol":["An Orbitrap Eclipse Tribrid mass spectrometer coupled with an EASY nLC 1200 system (Thermo Fisher Scientific, Waltham, MA) was used for both data dependent (DDA) and targeted nano-liquid chromatography-tandem mass spectrometry (nLC-MS/MS). Chromatographic separation was performed with  an Acclaim PepMap 100 (75 μm x 2 cm) trapping column and a PepMap RSLC C18 analytical column (2 μm, 100 Å, 75 μm × 15 cm)  with the following gradient: initial conditions 2% B, 2–6% B from 0 to 5 min, 6–35% B from 5 to 75 min, 35–60% B from 75 to 80 min, 60–95% B for 30 s, and 95% B for 9.5 min (solvents A and B consisted of 1% acetonitrile/99% water +0.1% formic acid and 80% acetonitrile/20% water + 0.1% formic acid, respectively). For all nLC-MS/MS experiments, four technical replicates (n=4) were performed unless otherwise noted. All MS1 spectra were acquired using a nano spray ionization source in positive mode applying 1900 V; transfer tube temperature: 275 ⁰C, RF lens 30%, and the Orbitrap was used as the mass analyzer with a resolution of 120,000 and quadrupole isolation set to ‘on’. The mass range was set to ‘normal’ (375-2000 m/z), and data was acquired in profile mode.  CD16a Titration Curves: Initially, 200 ng of THP-1 cell lysate digest spiked with different amounts of CD16a were analyzed via nano-liquid chromatography-tandem mass spectrometry parallel reaction monitoring (nLC-MS/MS-PRM) method targeting a set of CD16a (FcγRIIIA V/F158) site Asn162 glycopeptide precursors from a list of previously described glycoforms16 to assess method performance. For the relative quantification of targeted glycoforms, a parallel reaction monitoring method was designed to acquire data alternatively in MS1 and MS2 modes targeting selected precursor within a retention time window (Supplementary Table 1) with the following parameters: MS1 settings were as described above with the following changes: AGC target set as standard; absolute AGC target 4x105, maximum injection time in ‘auto’ mode and 1 μscan. For MS2 scans, the isolation window for the quadrupole was 2 m/z, the activation type was HCD and 35% collision energy, orbitrap resolution: 50000, normal mass range, auto scan range mode, custom AGC target, 200 normalized AGC target (%), absolute AGC value of 1x105,100 ms for maximum injection time, 1 μscan, data type in profile mode and number of spectra (N) = 30. Defining Human Monocyte CD16a Glycopeptide Precursors: Given that the prior list of glycopeptide precursors was assembled from recombinant CD16a, we sought to determine if additional glycopeptides/glycoforms were present in THP-1-CD16+ cells, via an unbiased method. To achieve this, immunoaffinity-enriched CD16a from PMA-treated THP-1 cells with stable expression of human FcγRIIIa (THP1+CD16a cells) were analyzed via nLC-MS/MS using a data dependent method specifically designed to maximize the identification of glycopeptides, to sample CD16a glycoforms in an unbiased manner. The following parameters were set for glycopeptide discovery using a modified data dependent method to maximize the identification of glycopeptides. The MS1 settings were as described above with the following changes: custom AGC target; 200 for normalized AGC target (%), absolute AGC target 8 x 105, maximum injection time in ‘auto’ mode and 2 μscans. In MS2 scans, the isolation window for the quadrupole was 1.2 m/z units and the activation was HCD with a collision energy of 35%, AGC target set as standard and a maximum injection time of 35 ms, top speed of 3 sec, charge states 2-7, and dynamic exclusion ‘on’. The detection of ≥2 glycan oxonium ion peaks (m/z 138.0550, 144.0655, 168.0655, 186.0761, 204.0867, 274.0921, 292.1027, 366.1395, 512.1974; with 25 ppm mass tolerance) in the HCD spectrum triggered an EThcD MS2 scan and a sceHCD scan. EThcD was performed with the next settings: ETD with 20% supplemental activation, 30,000 resolution, mass range set as ‘high’, first scan set at 130 m/z, 1 μscan, custom AGC target, 200 normalized AGC target (%), maximum injection time set as ‘auto’ and data type in profile mode. Stepped collision energy HCD (sceHCD) was performed with 15, 30, and 40% collision energies, 15,000 resolution, 1 μscan, custom AGC target, 200 normalized AGC target (%), and 100 ms maximum injection time, and spectra were acquired in profile mode. PRM of CD16a Glycopeptides from Primary Human Monocytes and PBMCs: Following definition of CD16a glycoforms from primary cells, PRM analyses were conducted via a modified nano-liquid chromatography-tandem mass spectrometry parallel reaction monitoring (nLC-MS/MS-PRM) method targeting CD16a sites N45, N74, and N162 glycopeptides with the same settings as above (see ‘CD16 Titration Curves’ section), with a modified set of precursors."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Proteome Discoverer 2.4 (Thermo Fisher Scientific) with an integrated Byonic v4.0.12 node (Protein Metrics Inc, Cupertino, CA, USA) were used for data analysis for glycopeptide identification from human FcγRIIIa and to stablish the precursors to target with the PRM method. For the analysis of FcγRIIIa enriched from THP-1 cells, monocytes and PBMCs only the F158 variant was analyzed, with data dependent strategy or targeted method. The reviewed human protein sequence database from UniProt (Homo sapiens Release 2023_03), with the inclusion of FcγRIIIa isoforms V158 and F158, and an N-glycan database consisting of 309 mammalian glycans were used for data searching. Parameters considered for the search include: 1 N-glycan per peptide (variable) and carbamidomethylation of cysteine (fixed), precursor tolerance: 10 ppm, fragment tolerance: 20 ppm, maximum number of missed cleavages: 6, cleaved residues: DEFLWY, common modifications max: 2, rare modification max: 1, false discovery rate (FDR): 1%. Following the Byonic analyses, glycopeptide assignments were filtered (Byonic score ≥200) and manually curated.  Skyline 29 (Skyline-daily version 24.1.1.202, University of Washington, USA) was used for quantification of selected glycopeptides from the PRM results. For identification of glycopeptides containing site N162, transitions from HexNAc (m/z 204.0867), HexNAc-H2O (m/z 186.0761), HexNAc-2H2O (m/z 168.0655), Hex-HexNAc (m/z 366.1395) ions, Y1 ion (peptide+HexNAc) and b/y-ions were used, while the Y1 ion (peptide+HexNAc) was used for quantification. On the other hand, due to their low relative abundance, for identification of glycopeptide harboring N45 transitions from HexNAc, HexNAc-H2O, HexNAc-2H2O, Hex-HexNAc ions, and at least one b- or y-ions were used, while the HexNAc ion was used for quantification. For glycopeptides harboring site N74, HexNAc, HexNAc-H2O, HexNAc-2H2O, Hex+HexNAc ions were used for identification and HexNAc ion for quantification. For Skyline analysis, the sequence of human CD16a (FcγRIIIa F158 or V158) from UniProt was utilized for the protein database. The peptide settings were as follows, enzyme specificity WFYLE, except when followed by P, for peptide modification: carbamidomethyl (C) and identified N-glycan compositions, a library was created from a survey search from Byonic (data dependent search), and target peptides manually edited including sequence and glycan compositions. The transition setting included: monoisotopic precursor mass and product ion mass, precursor charges were set as +3, +4 and +5, and ion charges were +1 and +2, ion type were y, b, and the precursor was also included. Y1 (peptide+ HexNAc) was included as a special ion. Ion match tolerance was 0.05 m/z. Subsequently, all transitions were manually inspected, and those that exceed +/-10 ppm error tolerance were discarded. Orbitrap was set as the analyzer for MS1 and MS2 filtering with resolving power 120,000 at 400 m/z for MS1 and 60,000 at 400 m/z for MS2. All assignments were manually curated considering peak shape of transitions from the same glycoform and retention time. The area under the curve (AUC) of the selected transition for quantification from each glycopeptide was exported from Skyline. Retention times were measured between runs to ensure consistency between replicates. Finally, AUCs from each glycopeptide containing a common asparagine residue were summed, and the summed area was used as the denominator to determine the relative abundance of each glycoform sharing the same N-glycosylation site."],"omics_type":["Proteomics"],"labhead":["Kevin Brown Chandler"],"instrument_platform":[""],"labhead_affiliation":["Assistant Professor  Department of Cellular and Molecular Medicine Florida International University | Herbert Wertheim College of Medicine"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["42026724 Pavan CH, Desai J, Medina Navarro V, Chandler KB. Assessing High-Affinity &lt;i&gt;N&lt;/i&gt;-Glycoforms of the Human Fcγ Receptor IIIa (CD16a) via Parallel Reaction Monitoring Mass Spectrometry. J Proteome Res. 2026 10.1021/acs.jproteome.5c01234"],"submitter_mail":["cpavan@fiu.edu"],"submitter_affiliation":["Florida International University"],"submitter_country":["United States"],"pubmed_abstract":["The Fc γ-receptor IIIa (FcγRIIIa), or CD16a, is a receptor for the Fc region of IgG that plays an essential role in the regulation of antibody effector functions. Dysregulated CD16a activity contributes to tissue damage and chronic inflammation or, conversely, compromises the removal of immune complexes. CD16a glycoforms with high-mannose <i>N</i>-linked glycans at site N162 demonstrate higher affinity for IgG compared to other forms. Here, we developed a targeted nanoliquid chromatography tandem mass spectrometry parallel reaction monitoring (PRM) method for the site-specific study of CD16a <i>N</i>-glycosylation. The method was applied to assess changes in site N162 <i>N</i>-glycosylation in a model of monocyte differentiation and in CD16a from human primary monocytes and peripheral blood mononuclear cells. Site N162 <i>N</i>-glycosylation was similar across the surveyed cell types. An increase in the proportion of high-mannose <i>N</i>-glycan compositions at site N162 was observed, corresponding to high-affinity glycoforms of CD16a, in a model of monocyte differentiation. Here, the feasibility of using targeted glycopeptide PRM to study CD16a glycosylation in primary cells has been demonstrated. This strategy is well-suited for adaptation to clinical studies focused on the role of CD16a glycosylation in physiology, immunotherapy, and immune disorders. Data are available via ProteomeXchange with the identifier PXD071784."],"pubmed_title":["Assessing High-Affinity &lt;i&gt;N&lt;/i&gt;-Glycoforms of the Human Fcγ Receptor IIIa (CD16a) via Parallel Reaction Monitoring Mass Spectrometry."],"pubmed_authors":["Pavan Carlos H CH, Desai Jay J, Medina Navarro Valentina V, Chandler Kevin Brown KB"],"additional_accession":[]},"is_claimable":false,"name":"Parallel Reaction Monitoring to Assess High-Affinity N-Glycoforms of the Human Fcγ Receptor IIIa (CD16a)","description":"Fc γ-receptor IIIa (FcγRIIIa, or CD16a) is a receptor for the Fc region of IgG antibodies and plays an essential role in the regulation of antibody effector functions. While the activation of CD16a plays a role in a healthy immune response, dysregulated CD16a activity may contribute to tissue damage and chronic inflammation by over-activating immune cells or, conversely, by compromising the removal of immune complexes. Functionally distinct glycosylated forms of CD16a exist, with CD16a glycoforms modified with high mannose N-linked glycans at site N162 demonstrating a higher binding affinity for IgG compared to other forms of CD16a. Here, we developed and tested a nano-liquid chromatography tandem mass spectrometry (nLC-MS/MS) parallel reaction monitoring (PRM) method for the site-specific study of CD16a glycosylation. The PRM method was tested by spiking recombinant CD16a (F158 or V158) into a complex matrix consisting of THP-1 cell lysate digest, then the CD16a glycopeptide PRM method was applied to measure statistically significant changes in site N162 N-glycan compositions corresponding to high affinity glycoforms of CD16a in a model of monocyte differentiation. Analyses were extended to the analysis of CD16a derived from human primary monocytes and peripheral blood mononuclear cells. CD16a site N162 N-glycosylation demonstrated remarkable similarity across the surveyed cell types, including in THP-1 cells – a monocyte cell line isolated from the peripheral blood of an acute monocytic leukemia patient, as well as primary human monocytes, and PBMCs. Critically, CD16a glycopeptide PRM facilitated measurement of changes in CD16a glycosylation at site N162, with high mannose N-glycan compositions, corresponding to high affinity glycoforms of CD16a, increasing in a model of monocyte differentiation into macrophages. Here, we have demonstrated the feasibility of utilizing a glycopeptide nLC-MS/MS-PRM targeted approach to study CD16a glycosylation in material from primary cells in a glycosylation site-specific manner. This strategy is well-suited for adaptation to clinical studies focused on understanding the role of CD16a glycosylation in physiology and disease, with a focus on immune 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