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Elevated levels of antibodies against 70 kDa heat shock proteins in the sera of patients with HIV infection
Author(s) -
Kocsis Judit,
Prohászka Zoltán,
Bíró Adrienn,
Füst George,
Bánhegyi Dénes
Publication year - 2003
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/jmv.10507
Subject(s) - hsp70 , antibody , virology , immune system , heat shock protein , viral load , virus , immunology , human immunodeficiency virus (hiv) , biology , viral disease , immunopathology , medicine , biochemistry , gene
Abstract Heat shock proteins (Hsp), especially 70 kDa heat shock protein (Hsp70) play an important role in the life cycle of HIV‐1 virus. Hsp70 is overexpressed in HIV‐infected cells and this is the most abundant Hsp associated with HIV virions. The aim of our study was to investigate whether HIV infection increases the extent of specific humoral immune response against Hsp70. The serum concentration of anti‐Hsp70 IgG antibodies was measured in 47 HIV‐infected patients, and 62 healthy, HIV‐seronegative persons. Nineteen patients on highly active anti‐retroviral therapy (HAART) were followed for 24 months in a longitudinal study. Anti‐Hsp70 antibodies were measured by ELISA, using recombinant human Hsp70. Levels of anti‐Hsp70 antibodies were significantly ( P < 0.0001) higher in the HIV‐infected patients (median: 1409 (25th–75th percentile: 1031–2214) AU/ml) than in healthy control subjects (626 (429–970) AU/ml). In 19 HIV patients, serum levels of anti‐Hsp70 antibodies significantly ( P < 0.001) decreased during 24 (11–41) months HAART (1309 (887–2213) AU/ml before and 640 (386–959) AU/ml during HAART), accompanied by viral load reduction and CD4+ count elevation. It is concluded that HIV‐infection induces a marked increase in the anti‐Hsp70 antibody levels, which is consistent with the enhanced expression of Hsp70 on the surface of HIV‐infected cells and/or incorporation of the protein into the membrane of HIV virions. J. Med. Virol. 71:480–482, 2003. © 2003 Wiley‐Liss, Inc.