Elevated levels of antibodies against 70 kDa heat shock proteins in the sera of patients with HIV infection

Kocsis, Judit; Prohászka, Zoltán; Bı́ró, Adrienn; Füst, George; Bánhegyi, Dénes

doi:10.1002/jmv.10507

Cited by 24 publications

(21 citation statements)

References 10 publications

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“…Prohaszka et al (1999) reported that there was an increase of anti-hHsp60 and mycobacterial Hsp65 and a strong positive correlation between the levels of autoantibodies against C1q and antibodies to these Hsps in the sera of HIV-infected patients. There have been reports of an increase in serum Hsp70 and antibodies to Hsp70 in HIV-infected patients (Kocsis et al 2003). Antibodies to the Hsp70 cochaperone HspB1 have also been found in HIV-infected subjects but also in uninfected controls consistent with the absence of any relationship between the autoantibodies and clinical parameters (Papp et al 2005).…”

Section: Anti-hsps and Infectious Diseasesmentioning

confidence: 89%

Antibodies against heat shock proteins in environmental stresses and diseases: friend or foe?

Tanguay²

2006

Cell Stress Chaper

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Heat shock proteins (Hsps) can be found in two forms, intracellular and extracellular. The intracellular Hsps are induced as a result of stress and have been found to be cytoprotective in many instances due to their chaperone functions in protein folding and in protein degradation. The origin and role of extracellular Hsps is less clear. Although they were suspected originally to be released from damaged cells (necrosis), their presence in most normal individuals rather suggests that they have regulatory functions in circulation. As immunodominant molecules, Hsps can stimulate the immune system, leading to the production of autoantibodies recognizing epitopes shared by microbial and human Hsps. Thus, extracellular Hsps can influence the inflammatory response as evidenced by the production of inflammatory cytokines. Antibodies to Hsps have been found under normal conditions but seem to be increased in certain stresses and diseases. Such antibodies could regulate the inflammatory response positively or negatively. Here, we review the literature on the findings of antibodies to Hsps in situations of environmental or occupational stress and in a number of diseases and discuss their possible significance for the diagnosis, prognosis, or pathogenesis of these diseases.

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Section: Anti-hsps and Infectious Diseasesmentioning

confidence: 89%

Antibodies against heat shock proteins in environmental stresses and diseases: friend or foe?

Tanguay²

2006

Cell Stress Chaper

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“…Several studies reported increased expression of Hsp70 in HIV-1 infection and showed its presence in the virion (23,24,45). Therefore, we assessed the Hsp40 expression level in HIV-1-infected CEM-GFP cells by immunoblotting for Hsp40.…”

Section: Nl4-3 Nef Also Interacts With Hsp40 Both In Vitro and In Vivo-mentioning

confidence: 99%

Heat Shock Protein 40 Is Necessary for Human Immunodeficiency Virus-1 Nef-mediated Enhancement of Viral Gene Expression and Replication

Kumar¹,

Mitra

2005

Journal of Biological Chemistry

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The human immunodeficiency virus-1 (HIV-1) Nef protein, originally identified as a negative factor, has now emerged as one of the most important viral proteins necessary for viral pathogenesis and disease progression. Nef has been also implicated in viral infectivity and replication, however, the molecular mechanism of Nef-induced viral gene expression and replication is not clearly understood. Although involvement of heat shock proteins in viral pathogenesis has been reported earlier, a clear understanding of their role remains to be elucidated. Here we report for the first time that Nef not only interacts with heat shock protein 40 (Hsp40) but it also induces the expression of Hsp40 in HIV-1-infected cells. The interaction between Nef and Hsp40 is important for increased Hsp40 translocation into the nucleus of infected cells, which seems to facilitate viral gene expression by becoming part of the cyclin-dependent kinase 9-associated transcription complex regulating long terminal repeat-mediated gene expression. The finding is consistent with the failure of the nef-deleted virus to induce Hsp40, resulting in reduced virus production. Our data further shows that, whereas, Hsp40 overexpression induces viral gene expression, silencing of Hsp40 reduces the gene expression in a Nef-dependent manner. Thus our results clearly indicate that Hsp40 is crucial for Nef-mediated enhancement of viral gene expression and replication.Viruses are known to modulate cellular proteins for successful replication within the host cells. The sequence of events in the establishment of a productive infection by human immunodeficiency virus type 1 (HIV-1) 3 not only involves interaction between a number of viral and cellular factors but is also accompanied by complex and dynamic changes in the patterns of cellular gene expression. Nef, a 27-30-kDa myristoylated phosphoprotein, encoded by HIV-1 has been shown to play a crucial role in viral pathogenesis by modulating cellular gene expression and signaling pathways (1, 2). nef-deleted viruses fail to replicate efficiently in vivo, and do not develop symptoms of acquired immunodeficiency syndrome (AIDS) (3, 4). Nef is also thought to contribute to viral pathogenesis by down-regulation of CD4 and major histocompatibility complex class I surface molecules preventing viral superinfection and by helping the virus to evade host immune system. Nef has also been implicated in the activation of T cells, making the cells permissible to the virus (5, 6). All these functions of Nef are manifested by a number of important events such as activation of upstream signaling molecules, inhibition of apoptosis in the infected cell, activation and up-regulation of transcription factors, alleviation of repressors of transcription, as well as increase of the infectivity of newly produced virions (1, 7). Even though these functions of Nef have been well studied, controversy exists on its role in viral infectivity and replication as both negative (8, 9) and positive (10, 11) effects are available in the literature...

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“…Since our group was active in the study of the connection between antibodies against different heat shock proteins and coronary artery disease (Burian et al 2001;Kocsis et al 2003;Lu et al 2010;Prohaszka et al 1999;Veres et al 2002), we carried out B cell epitope analysis with sera of coronary artery disease. As to our best knowledge, only T cell epitopes of HSP60 have been analyzed until now in IBD (Puga Yung et al 2009).…”

Section: Introductionmentioning

confidence: 99%

Comparison of epitope specificity of anti-heat shock protein 60/65 IgG type antibodies in the sera of healthy subjects, patients with coronary heart disease and inflammatory bowel disease

Füst

Uray

Bene

et al. 2012

Cell Stress and Chaperones

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Previously, we reported on the presence of antibodies to linear epitopes of human and mycobacterial 60 kD heat shock proteins (HSP) in the sera of healthy blood donors. Since many recent findings indicate that the levels of these antibodies may be altered in coronary heart disease (CHD) and also inflammatory bowel diseases (IBD), it seemed worthwhile to compare the epitope specificity of the anti-HSP60 and anti-HSP65 antibodies in the sera of patients with these diseases to those in healthy subjects. The multipin enzyme-linked immunosorbent assay method was applied with a large overlapping set of synthetic 10-mer peptides covering selected regions of human HSP60 and Mycobacterium bovis HSP65. Sera of 12 healthy persons (HP), 14 CHD, and 14 IBD patients with the same concentration of total anti-HSP60 and HSP65 IgG antibodies were tested. We have identified CHDspecific epitopes in the equatorial domain of the HSP60 protein but in neither region of the HSP65 molecule, indicating that the formation of anti-HSP60 antibodies is not or only partially due to the cross-reaction between human HSP60 and bacterial HSP65. IBD-specific epitopes were found in many regions of the HSP60 and in even more regions of the HSP65 molecule including an IBD-specific T cell epitope in region X as well. These findings indicate that the epitope specificity of the anti-human and antimycobacterial HSP60 antibodies associated with various diseases is different.

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Elevated levels of antibodies against 70 kDa heat shock proteins in the sera of patients with HIV infection

Cited by 24 publications

References 10 publications

Antibodies against heat shock proteins in environmental stresses and diseases: friend or foe?

Antibodies against heat shock proteins in environmental stresses and diseases: friend or foe?

Heat Shock Protein 40 Is Necessary for Human Immunodeficiency Virus-1 Nef-mediated Enhancement of Viral Gene Expression and Replication

Comparison of epitope specificity of anti-heat shock protein 60/65 IgG type antibodies in the sera of healthy subjects, patients with coronary heart disease and inflammatory bowel disease

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