Identification of critical residues of linear B cell epitope on Goodpasture autoantigen

The autoantigen of anti-glomerular basement membrane (GBM) disease has been identified as the non-collagenous domain 1 of α3 chain of type IV collagen, α3(IV)NC1. Our previous study revealed a peptide on α3(IV)NC1 as a major linear epitope for B cells and potentially nephrogenic, designated as P14 (...

Full description

Saved in:
Bibliographic Details
Published in:PloS one 2015-04, Vol.10 (4), p.e0123277-e0123277
Main Authors: Jia, Xiao-yu, Cui, Zhao, Li, Jian-nan, Hu, Shui-yi, Zhao, Ming-hui
Format: Article
Language:English
Subjects:
Acids
Adult
Aged
Alanine
Amino acid sequence
Amino acids
Anti-Glomerular Basement Membrane Disease - immunology
Antibodies
Antibody Specificity
Antigens
Autoantibodies - chemistry
Autoantigens - chemistry
C-Terminus
Collagen (type IV)
Collagen Type IV - chemistry
Disease prevention
Education
Enzyme-Linked Immunosorbent Assay
Epitope Mapping
Epitopes
Epitopes, B-Lymphocyte - chemistry
Etiology
Female
Hospitals
Humans
Hydrophobicity
Immunogenicity
Immunoglobulins
Kidney diseases
Laboratories
Lymphocytes
Lymphocytes B
Lymphocytes T
Male
Medicine
Microscopy
Middle Aged
Nephrology
Patients
Peptides
Peptides - chemistry
Protein Structure, Tertiary
Residues
Rodents
Tetanus
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The autoantigen of anti-glomerular basement membrane (GBM) disease has been identified as the non-collagenous domain 1 of α3 chain of type IV collagen, α3(IV)NC1. Our previous study revealed a peptide on α3(IV)NC1 as a major linear epitope for B cells and potentially nephrogenic, designated as P14 (α3129-150). This peptide has also been proven to be the epitope of auto-reactive T cells in anti-GBM patients. This study was aimed to further characterize the critical motif of P14. 16 patients with anti-GBM disease and positive anti-P14 antibodies were enrolled. A set of truncated and alanine substituted peptides derived from P14 were synthesized. Circulating antibodies against the peptides were detected by enzyme linked immunosorbent assay (ELISA). We found that all sera with anti-P14 antibodies reacted with the 13-mer sequence in the C-terminus of P14 (P14c) exclusively. The level of antibodies against P14 was highly correlated with the level of antibodies against P14c (r=0.970, P
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0123277