{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079527/checksum.txt"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079527/Anti_LOS_1.msf"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079527/Anti_Porin_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079527/Anti_Porin_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079527/Anti_LOS_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079527/mAb_04_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079527/mAb_04_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079527/Anti_LOS_2.raw"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["l.salvini@toscanalifesciences.org"],"submitter":["Mattia Cicogni"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Yrap","Reverse vaccinology 2.0","Neisseria gonorrhoeae","Bexsero.","Ngo_1985","Monoclonal antibodies"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD079527"],"sample_protocol":["Native Outer Membrane Vesicles (nOMVs) were produced from Neisseria gonorrhoeae cultures. Culture supernatants were cleared by centrifugation ($8,000 \\times g$, 30 min, 4°C) and filtered through 0.22 µm nitrocellulose membranes. nOMVs were then pelleted via ultracentrifugation ($170,000 \\times g$, 3 h, 4°C), washed twice in PBS, and quantified using a Lowry assay. Target enrichment was achieved by non-denaturing solubilization of nOMVs using a mild, non-ionic NP-40 lysis buffer (20 mM Tris-HCl pH 8, 165 mM NaCl, 1% Nonidet P-40, 5 mM EDTA) for 10 minutes on ice. Solubilized proteins were collected after centrifugation and subjected to Immunoprecipitation (IP). Specific candidate monoclonal antibodies (mAbs, 1–10 mg/mL) were coupled to Dynabeads Protein G for 1 hour at room temperature. Lysed nOMVs (10–50 µg/mL) were added to the mAb-coated beads and incubated overnight at 4°C with gentle shaking. Bound antigen complexes were washed and eluted using Tris-Glycine at pH 2.7, followed by immediate neutralization with 1 M Tris-HCl at pH 9.0. Eluted immunoprecipitated protein samples were chemically reduced using dithiothreitol (DTT) and subsequently alkylated with iodoacetamide at room temperature. Proteins were precipitated using a cold methanol/chloroform mixture (80% methanol / 20% chloroform) and pelleted by centrifugation ($2\\text{ min}$, 4°C). The resulting protein pellets were allowed to dry and then completely resuspended in a denaturing solution of 6 M urea. Enzymatic peptide digestion was carried out by adding trypsin (Promega) and incubating the mixture overnight at 37°C.Following overnight proteolytic digestion, the resulting tryptic peptides were desalted and thoroughly dried using a vacuum centrifuge. Immediately prior to liquid chromatography-mass spectrometry (LC-MS/MS) analysis, the dried peptide samples were reconstituted in an aqueous solution containing 0.1% trifluoroacetic acid (TFA)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw MS/ms data were processed using Proteome Discoverer 2.5 (Thermo Fisher Scientific). Database searching was performed against the Neisseria gonorrhoeae protein database using Trypsin as the proteolytic enzyme, allowing for up to two missed cleavages. Carbamidomethylation of cysteine was set as a fixed modification, while oxidation of methionine was specified as a variable modification. Protein and peptide identifications were filtered and validated applying a False Discovery Rate (FDR) threshold of less than 1%."],"omics_type":["Proteomics"],"labhead":["Laura Salvini"],"instrument_platform":[""],"labhead_affiliation":["Toscana Life Sciences"],"submission_type":["PARTIAL"],"species":["Neisseria Gonorrhoeae (strain Atcc 700825 / Fa 1090)","Bacteria"],"publication":["10.3389/fmicb.2026.1830193"],"submitter_mail":["m.cicogni@toscanalifesciences.org"],"submitter_affiliation":["toscana life sciences"],"submitter_country":["Italy"],"additional_accession":[]},"is_claimable":false,"name":"Discovery and characterization of an anti-Neisseria gonorrhoeae NGO_1985 monoclonal antibody and cognate antigen","description":"Gonorrhea, caused by Neisseria gonorrhoeae (Ng), represents a major global health concern, exacerbated by the lack of an available vaccine and rising antibiotic resistance. Partial protection has been linked to the anti-meningococcal 4CMenB vaccine. Using a Reverse Vaccinology 2.0 approach, memory B cells from 4CMenB-vaccinated volunteers were used to generate monoclonal antibodies (mAbs) cross-reactive against Ng. A specific antibody, mAb_4, was selected for detailed investigation. To identify its target, native Outer Membrane Vesicles (nOMVs) from Ng strains were subjected to immunoprecipitation (IP) with mAb_4, followed by liquid chromatography-mass spectrometry (LC-MS/MS) analysis. The cognate antigen was successfully identified as NGO_1985, an outer membrane biogenesis protein and ortholog of the N. meningitidis GNA_2091 vaccine component. Complementary Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS) was further employed to map the specific conformational epitope recognized by the antibody. This study elucidates the molecular basis of 4CMenB cross-protection and provides insights for future vaccine and therapeutic 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