Evaluation and comparison of the potential of two ferritins as anti-tick vaccines against Haemaphysalis longicornis
The passage of immunoglobulins in the blood meal into hemolymph prompts development of vaccines against internal antigens of ticks, but little is known about kinetics and specificity of the immunoglobulin uptake. We used capillary feeding of adult Amblyomma americanum hard ticks to introduce compounds into the midgut and then examined the hemolymph after various times for their presence and concentration. Immunoglobulins of different sources, albumin, choramphenicol acetyltransferase, inulin, and mannitol were labeled with (125)I, (14)C, or biotin. With the exception of the carbohydrate inulin, all the compounds entered the hemolymph of tick during capillary feeding. The small molecule mannitol had the highest rate of entry at 9% after 6 h. Among proteins, the entry of immunoglobulin G (IgG) of different species into the hemolymph was greater at 6% after 6 h than for the smaller proteins albumin or choramphenicol acetyltransferase at 1 and 3%, respectively. The entry of denatured IgG was equal to that of nondenatured protein. There was no evidence of degradation of the IgG or of its binding to cells once it entered the hemolymph. A monoclonal IgG antibody labeled with biotin entered the hemolymph and retained its ability to bind to its specific antigen in an immunoassay. Although different proteins entered the hemolymph after capillary feeding, there was evidence of a specific mechanism for immunoglobulin uptake.