PXD002475-1

PXD002475 is an original dataset announced via ProteomeXchange.

Title	HCV Cryoprecipitate LC-MS/MS with iTRAQ Quantification
Description	The discovery of hepatitis C virus (HCV) in 1989 revealed the virus as the etiology of 40%-90% of the “essential” mixed cryoglobulinemia, where immune complex forms deposit called cryoprecipitate at temperatures below 37 °C. Cryoprecipitate constitutes monoclonal IgM and polyclonal IgG, some of which has reactivity against HCV core and NS3 epitopes. Resultant immune complex is considered entrapped on microvascular endothelium via C1q receptor, leading to complement activation and organ injury presenting predominantly as dermopathy, peripheral neuropathy and nephropathy. However, currently little is known on whether auto-reactive, cold-precipitating IgG components enriched in cryoprecipitate may play some role on the deposition of immune complex and subsequent complement-mediated injury of specific organs. Recently, with the advent of high-throughput immune repertoire sequencing and mass spectrometry, technical feasibility is growing to delineate antibodies of interest and their sequences directly from serum. To date, vast majority of studies actually utilized the antigen column for affinity purification of antibodies of interest, although this strategy is not applicable to disease entity with unknown antigen involvement. In such cases, disease-specific and organ-specific immune deposits may be a good alternative source of etiological antibodies. Herein, targeting HCV cryoglobulinemic vasculitis as a model, we conducted a proof-of-concept study aiming at characterizing the IgG components most prone to cryoprecipitation. To this end, we longitudinally studied one patient with cryoglobulinemic vasculitis with chronic HCV infection. After obtaining informed consent, cryoprecipitate and supernatant were separated from peripheral blood sample. Fab fragments from Protein G-purified IgG were recovered after papain digestion for isobaric tags for relative and absolute quantification (iTRAQ)-based quantitative proteomics. Simultaneously, total RNA was isolated from peripheral blood, and immunoglobulin heavy chain variable region (IGHV) was PCR-amplified with unique molecular identifier (UMI) strategy to construct a personal IGHV sequence library of immunoglobulin variable region. Sequencing output from MiSeq was bioinformatically converted into mass spectrometry database. Search was performed using MaxQuant software.
HostingRepository	PRIDE
AnnounceDate	2016-07-14
AnnouncementXML	Submission_2016-07-14_00:08:31.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Masato Ogishi
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	iTRAQ4plex-116 reporter+balance reagent acylated residue
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2015-07-06 01:10:52	ID requested
⏵ 1	2016-07-14 00:08:34	announced
2	2024-10-22 04:05:38	announced	2024-10-22: Updated project metadata.

Ogishi M, Yotsuyanagi H, Moriya K, Koike K, Delineation of autoantibody repertoire through differential proteogenomics in hepatitis C virus-induced cryoglobulinemia. Sci Rep, 6():29532(2016) [pubmed]

curator keyword: Biomedical

submitter keyword: Human, HCV, Antibody, Immunoglobulin, iTRAQ

Hiroshi Yotsuyanagi
contact affiliation	Department of Infectious Diseases Internal Medicine Graduate School of Medicine University of Tokyo, Japan
contact email	hyotsu-tky@umin.ac.jp
lab head
Masato Ogishi
contact affiliation	The University of Tokyo
contact email	oogishi-tky@umin.ac.jp
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD002475
     1. Label: PRIDE project
     2. Name: HCV Cryoprecipitate LC-MS/MS with iTRAQ Quantification