Abstract
We hypothesized that molecular mimics between human T lymphotropic virus type 1 (HTLV-1) and human autoantigens were based upon post-translational modification of target proteins. Proteins purified from MT-2 (HTLV-1 infected) and Jurkat (HTLV-1 negative) cells were used for western blotting with HTLV-1 associated myelopathy/tropical spastic paraparesis (HAM/TSP) IgG. In contrast to normal IgG, HAM/TSP IgG immunoreacted with proteins in MT-2 cells at 22-24 kDa, pI 8.0, which were identified as peroxiredoxin 1 and HTLV-1-p24-(gag) by mass spectroscopy. Western blots following glycoprotein purification showed that HAM/TSP IgG reacted with PrX-1 and p24 in MT-2 cells but not in Jurkat cells, indicating that the mimicking target proteins were glycosylated. These data suggest that post-translational glycosylation of target proteins may play a role in the pathogenesis of HAM/TSP.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
-
Cells, Cultured
-
Electrophoresis, Gel, Two-Dimensional / methods
-
Glycoproteins / metabolism
-
Glycosylation
-
HTLV-I Infections / complications
-
HTLV-I Infections / immunology*
-
Humans
-
Immunoglobulin G / immunology
-
Jurkat Cells
-
Molecular Mimicry / immunology*
-
Nervous System Diseases / etiology
-
Nervous System Diseases / immunology*
-
Nervous System Diseases / virology*
-
Peroxiredoxins / immunology
-
Peroxiredoxins / metabolism
-
Retroviridae Proteins, Oncogenic / immunology*
-
Retroviridae Proteins, Oncogenic / metabolism
-
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods
-
T-Lymphocytes / metabolism
-
T-Lymphocytes / ultrastructure
Substances
-
Glycoproteins
-
Immunoglobulin G
-
Retroviridae Proteins, Oncogenic
-
p24 protein, Human T-lymphotropic virus 1
-
PRDX1 protein, human
-
Peroxiredoxins