Therefore, the development of a vaccine to prevent Trichinella infection in domestic CX-5461 molecular weight animals and humans is a necessary approach for controlling this disease. Heat shock proteins (Hsps) are a group of proteins that are induced upon exposure to a range of environmental stresses that include heat shock, oxygen deprivation, pH extremes, and nutrient deprivation

[6]. This family of proteins is highly conserved among different species and highly immunogenic during infections [7], [8], [9] and [10]. The heat shock proteins have recently been reported to play significant roles in antigen presentation, the activation of lymphocytes, and the maturation of dendritic cells [11]. Several researchers have also reported on the protective efficacies of Hsps against various infections by Plasmodium yoelii [7], Brugia malayi [8], Leishmania donovani [9], and Hantaan virus [12]. Several www.selleckchem.com/products/AZD6244.html heat-shock proteins, such as Hsp60, Hsp70 and Hsp80, have been reported and named according to their molecular weight. Of these proteins, Hsp70 is the

most conserved among different organisms, and Hsp70 is an immunodominant antigen during infections caused by a number of pathogens [6], [13] and [14]. In our previous study, Hsp70 from Trichinella spiralis (Ts-Hsp) was cloned via the immunoscreening of a T. spiralis cDNA library with immune serum, and the recombinant Ts-Hsp70 protein (rTs-Hsp70) was expressed in an Escherichia coli expression system [15]. The rTs-Hsp70 protein was recognized not only by the sera from patients with trichinellosis but also in the sera from T. spiralis-infected rabbits, pigs, and mice. The native Ts-Hsp70 was found in the crude somatic extracts of T. spiralis muscle larvae and adult worms. Vaccination with rTs-Hsp70 induces a strong immune response and a 37% reduction in muscle

larvae upon T. spiralis larval challenge compared to PBS control groups [15]. Further investigations in our lab demonstrated that the immunization of mice with rTs-Hsp70 elicited a systemic Th1/Th2 immune response (data not shown). However, as a possible vaccine candidate antigen, the mechanism of Ts-Hsp70-mediated protection Dipeptidyl peptidase requires further clarification. One mechanisms by which an antigen is presented to the immune system is based on the antigen’s ability to alter the maturation of dendritic cells (DCs). DCs are the typical antigen presenting cells (APCs) that induce primary immune responses through the activation and differentiation of helper T cells [16] and [17] and play a crucial role in helminth infections [18] and [19]. Currently, it remains unclear whether the protective immune response against T. spiralis infection induced by rTs-Hsp70 is related to DC activation. In this study, the interaction between rTs-Hsp70 and DCs derived from mouse bone marrow was investigated.