Abstract
Adult T cell leukemia is a fatal malignant transformation caused by the human T-cell lymphoptropic virus type I (HTLV-I). HTLV-I is only associated with the development of this disease in a small percentage of infected individuals. Using two rabbit transformed T-cell lines; RH/K30 (asymptomatic) and RH/K34 (leukemogenic), we have investigated the expression of heat shock proteins (HSP) 90 and 70 and the role of anti-HSPs antibodies on virus production. HSPs surface expression was higher on RH/K34 than RH/K30 cells. Heat treatment of cells increased the expression of HSPs proteins and virus production; HSPs augmentation was stabilized after 12 h and virus production reached a maximum between 8 h–12 h then returned to normal level after 24 h of culture. Incubation of cells only with rabbit anti-HSP 70 antibodies prevented virus production specifically in the leukemogenic cell line. The results indicate a relationship between HSP 70 and virus production.
Highlights
Heat shock proteins (HSPs) are a conserved family of proteins that are constitutively expressed in virtually all nucleated cells
Human T-lymphotropic virus type I (HTLV-I) transformed rabbit cell lines; leukemogenic RH/K34 (K34), asymptomatic cell line RH/K30 (K30) and normal rabbit peripheral blood mononuclear cell (NPBMC) were incubated in V bottom plate either with mouse anti-HSP antibodies (& HSP) or normal mice sera (NMS) reveled by peroxidase labeled goat anti-mouse Ig; (b) Immunoblot analysis with rabbit anti-HSP 70 and anti-HSP 90 antibodies of whole cell lysates from RH/K30 and RH/K34 cell line samples harvested at different times (0 h–24 h) after exposure to heat treatment at 42 °C
The results indicate a complicate relation between HSP expression, HTLV-I infection and the role of anti-HSP 70 antibodies on virus production
Summary
Heat shock proteins (HSPs) are a conserved family of proteins that are constitutively expressed in virtually all nucleated cells Their synthesis is enhanced in response to environmental stress and may have important physiological or pathological implications [1] HSPs are considered as a cancer associated antigen [2]. Inoculation with the majority of HTLV-I transformed rabbit cell lines gives rise to chronic asymptomatic infection, administration of certain HTLV-I infected T cell lines leads to acutely fatal disease that mimics human ATLL [11,12,13]. To further understand the relation between stress proteins and HTLV-I infection in the rabbit model, the expression of HSP on the surface of HTLV-I transformed cell line RH/K30 and RH/K34 were tested, and cells were incubated at 42 °C for different times with or without antibodies to HSPs (70 and 90). Our results indicate that HSP 70 may play a modulating role on virus production during stress conditions
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