{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PP_200227_J2__FDR.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/20525-PPR-J3__FDR.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PPR_200623_J4__FDR.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/20525-PPR-J5__FDR.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PP_200227_J1__FDR.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/20525-PPR-J6__FDR.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PPR_200623_J7__FDR.xlsx"],"Wiff":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/20525-PPR-J6.wiff.scan","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PP_200227_J2.wiff","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PP_200227_J2.wiff.scan","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PPR_200623_J7.wiff","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PPR_200623_J4.wiff","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PPR_200623_J4.wiff.scan","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/20525-PPR-J6.wiff","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/20525-PPR-J3.wiff","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/20525-PPR-J5.wiff.scan","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PP_200227_J1.wiff.scan","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/20525-PPR-J5.wiff","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/20525-PPR-J3.wiff.scan","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PPR_200623_J7.wiff.scan","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PP_200227_J1.wiff"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PP_200227_J2.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PP_200227_J1.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/20525-PPR-J5.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PPR_200623_J7.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/20525-PPR-J6.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/PPR_200623_J4.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD028655/20525-PPR-J3.mgf"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["mpperez@isciii.es"],"submitter":["Luz Valero"],"technology_type":["Mass Spectrometry","Gel-based experiment"],"disease":["Viral Infectious Disease"],"software":["Not available"],"submitter_keywords":["Cytomegalovirus","vaccine","cmv-specific immune response","neutralizing antibodies","Cytomegalovirus; cmv-specific immune response; neutralizing antibodies; vaccine"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD028655"],"tissue":["Blood Serum"],"sample_protocol":["Firstly, an \"In-gel\" digestion of the protein bands was performed. The gel fraction was cut and the samples were digested with sequencing grade trypsin (Promega), as previously described (Shevchenko et al., 1996). 100-200 ng of trypsin in 50 µL of ABC solution was used. The digestion was stopped with TFA (1% final concentration), a double extraction with acetonitrile (ACN) was done and all the peptide solutions and dried in a rotatory evaporator. Samples were re suspended with 10-30 µL of 2% ACN; 0.1% TFA (Trifluoroacetic acid).  For the LC-MS/MS analysis, five µl of the digested mixture sample was loaded onto a trap column (3µ C18-CL 120 Ᾰ, 350 m x 0.5mm; Eksigent) and desalted with 0.1% TFA at 5 µl min-1 for 5 min. Peptides were loaded onto an analytical column (LC Column 3µ C18-CL 120 Ᾰ, 0.075 x 150 mm; Eksigent) equilibrated in 5% acetonitrile 0.1% FA (formic acid). Peptide elution was carried out with a linear gradient of 7-40% B in A for 20 min. (A: 0.1% FA; B: ACN, 0.1% FA) at a flow rate of 300 nL min-1. Peptides were analyzed in a nanoESIq QTOF mass spectrometer (6600plus TripleTOF, ABSCIEX). Sample was ionized in a Source Type: Optiflow< 1 uL Nano applying 3.0 kV to the spray emitter at 200 ºC. Analysis was carried out in a data-dependent mode. Survey MS1 scans were acquired from 350–1400 m/z for 250 ms. The quadrupole resolution was set to ‘LOW’ for MS2 experiments, which were acquired 100–1500 m/z for 25 ms in ‘high sensitivity’ mode. Following switch criteria were used: charge: 2+ to 4+; minimum intensity; 100 counts per second (cps). Up to 100 ions were selected for fragmentation after each survey scan. Dynamic exclusion was set to 15 s. The system sensitivity was controlled by analyzing 500 ng of K562 trypsin digestion (Sciex), in these conditions 2260 proteins were identified (FDR <1%) in 45 minutes gradient"],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The LC-MS/MS information was sent to search the SwissProt, the Herpesviridae Uniprot database (82000 proteins) and herpesviridae NCBI database (290,000 proteins) with the Paragon algorithm of the ProteinPilot software, v. 5.0 with the following parameters: trypsin specificity, IAM cys-alkylation, taxonomy no restricted, and the search effort set to rapid with FDR analysis."],"omics_type":["Proteomics"],"labhead":["Pilar Pérez-Romero"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["National Center for Microbiology, Instituto de Salud Carlos III. Majadahonda, Madrid, Spain"],"species":["Homo Sapiens (human)","Cytomegalovirus Sp."],"publication":["10.1016/J.ANTIVIRAL.2024.105914"],"submitter_mail":["mluz.valero@uv.es"],"submitter_affiliation":["Universitat de Valencia"],"submitter_country":["Spain"],"additional_accession":[]},"is_claimable":false,"name":"Cytomegalovirus UL44 Protein as a new target of Humoral Immune Response in Solid Organ Transplant Recipients","description":"Due to the severity of CMV infection and the high number of deaths associated to this pathogen, the American Institute of Medicine proposed the development of a vaccine as a priority. Numerous attempts have been made to develop vaccines against CMV however, the complex interaction between CMV and the immune system and the absence of an animal model able to reproduce human physiology associated to CMV infection have hindered the development of a vaccine. Based on the long history of unsuccessful trials, it is necessary to keep looking for new CMV antigens that can contribute to induce a wide immune response. We designed a proteomic approach to find, select and characterize CMV antigens that induce a CMV-specific immune response, using serum samples from patients that have developed a protective CMV-specific response after transplantation. Serum samples from 28 kidney transplant recipients that exhibit a high neutralizing antibody response and CMV-specific immune response collected at the University Hospital 12 Octubre in Spain were tested. One sample was collected at transplantation with no or low antibody titers (baseline) and the second sample (post-immunization) after acquiring high neutralizing antibody titers (>1/640). Using serum samples from immunized patients as primary antibody, we detected by western blot CMV antigens that were specifically recognized by the post-immunization serum compared with the baseline serum. Excised proteins were further characterized and identified using liquid chromatography coupled with tandem mass spectrometry. To prove the recognition of the identified protein, the open reading frames were cloned and individually expressed in HEK 293T cells and further detected by western blot using serum samples. To characterize the in vivo immune response elicited against UL44, groups of mice were immunized using the pcDNA-UL44 construct and PBS control. We identified and validated three proteins (UL83, UL55 and UL44). Proteins UL83 (pp65) and UL55 (gB) have previously shown to elicit a potent antibody response, while UL44 was newly identified to elicit a neutralizing antibody immune response. In conclusion, we demonstrate that using serum of immunized patients is an excellent strategy to identify CMV proteins that may be involved on stimulating a wide and protective CMV-specific 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