Ticks cause approximately $17ââ?¬â??19 billion economic losses to the livestock industry globally. Development of recombinant\nantitick vaccine is greatly hindered by insufficient knowledge and understanding of proteins expressed by ticks. Ticks secrete\nimmunosuppressant proteins that modulate the hostââ?¬â?¢s immune system during blood feeding; these molecules could be a target for\nantivector vaccine development. Recombinant p36, a 36 kDa immunosuppressor from the saliva of female Dermacentor andersoni,\nsuppresses T-lymphocytes proliferation in vitro. To identify potential unique structural and dynamic properties responsible for\nthe immunosuppressive function of p36 proteins, this study utilized bioinformatic tool to characterize and model structure of\nD. andersoni p36 protein. Evaluation of p36 protein family as suitable vaccine antigens predicted a p36 homolog in Rhipicephalus\nappendiculatus, the tick vector of East Coast fever,with an antigenicity score of 0.7701 that compareswell with that of Bm86 (0.7681),\nthe protein antigen that constitute commercial tick vaccine Tickgard. Ab initio modeling of the D. andersoni p36 protein yielded\na 3D structure that predicted conserved antigenic region, which has potential of binding immunomodulating ligands including\nglycerol and lactose, found located within exposed loop, suggesting a likely role in immunosuppressive functionof tickp36proteins.\nLaboratory confirmation of these preliminary results is necessary in future studies.
Loading....