Immunization with a Recombinant Protein of Trichinella britovi 14-3-3 Triggers an Immune Response but No Protection in Mice

Abstract

14-3-3 proteins are present in all eukaryotic organisms and are ubiquitously expressed in a broad range of tissues and cellular compartments. They are regulatory adapter proteins that play key roles in a variety of signaling pathways, and have been proposed as suitable targets for the control and detection of certain parasites. Trichinella britovi is a widely-distributed parasitic nematode, transmitted through ingestion of meat products containing invasive larvae. The present study describes the cloning and expression of Tb14-3-3, and investigates the immunological and protective potential of the recombinant protein. Immunization of mice with rTb14-3-3 triggered an IgG response, and significant differences, in the profiles of secreted cytokines observed in vitro, between experimental groups. Nonetheless, neither specific antibodies, nor increased secretion of IFNγ, IL-4, and IL-10 cytokines, conferred greater protection against infection. No reduction in larval burden was observed during recovery at 48 dpi. Additionally, rTb14-3-3 was not recognized by sera from the infected control mice, except for one, suggesting some mismatch between native and recombinant Tb14-3-3 antigenic sites. Therefore, before 14-3-3 can be considered a potential tool for Trichinella detection and vaccination, more research regarding its target proteins, and actual specific function, is needed.

Proteomic and Immunological Identification of Diagnostic Antigens from Spirometra erinaceieuropaei Plerocercoid

“…Opisthorchis viverrini [57], Trichinella britovi [58] and Strongyloides stercoralis [59]. In S. japonicum, a sandwich time-resolved fluoroimmunoassay (TRFIA) for detecting the circulating antigen 14-3-3 has been developed, and has demonstrated to be a good potential diagnostic method for schistosomiasis [53].…”

“…In the field of parasitology, 14-3-3 protein has been assumed to play an important role in parasite proliferation and survival [ 47 , 51 ]. Various structures and functions of 14-3-3 protein have been studied in Toxoplasma gondii [ 52 ], S. japonicum [ 53 ], Echinococcus granulosus [ 54 ], Fasciola gigantic [ 55 ], Clonorchis sinensis [ 56 ], Opisthorchis viverrini [ 57 ], Trichinella britovi [ 58 ] and Strongyloides stercoralis [ 59 ]. In S. japonicum , a sandwich time-resolved fluoroimmunoassay (TRFIA) for detecting the circulating antigen 14-3-3 has been developed, and has demonstrated to be a good potential diagnostic method for schistosomiasis [ 53 ].…”

Contemporary Enzyme-Based Methods for Recombinant Proteins In Vitro Phosphorylation

“…Recombinant (phospho)proteins are a suitable tool not only for the cell regulation study, as we have already mentioned. They are also widely applied as the main component of new generation vaccines [33,34] or for the production of specific monoclonal antibodies that recognize specific antigens, phosphoproteins, or site-specific amino acid phosphorylation [35], clearly reviewed by [6]. A typical example is the work of Freivalds et al (2011), in which the authors described the production of phosphorylated yeast-derived hepatitis B core protein to carry foreign peptides [16].…”