Immunisation of cattle with recombinant acetylcholinesterase from Dictyocaulus viviparus and with adult worm ES products.
Dictyocaulus viviparus causes a serious lung disease of cattle. For over 30 years, a radiation-attenuated larval vaccine has been used with success; however, this vaccine has several disadvantages. A more stable vaccine against D. viviparus, capable of stimulating prolonged protective immunity, would be beneficial. Recent research has been directed at adult worm ES components that may be involved in parasite survival in the host. One component is the secreted enzyme, acetylcholinesterase (AChE), a target for circulating antibody in infected calves. Here, we describe a study where protection was investigated in calves immunised with either native adult ES products or a recombinant parasite AChE. These antigens were administered twice with Freund's incomplete adjuvant. Subsequently, all calves were challenged with 700 L3 and their worm burdens and immune responses compared with those in calves that received an anthelmintic-abbreviated infection and challenge control calves. Significant levels of protection were not obtained in the immunised groups but significant immunity was achieved in the calves that received the anthelmintic abbreviated infection. Antibody responses amongst the groups were different, with significantly higher IgG1 responses in the immune, infected group and in adult ES recipients. Significantly higher IgG2 responses were found in the latter group. Following challenge, the groups that received the abbreviated infection and the fusion protein produced specific antibody that bound the native enzyme. No differences were observed between groups in peripheral blood mononuclear cell responsiveness to either antigen. However, adult ES products appeared to have a mitogenic effect on these cells, whilst the fusion protein exhibited an inhibitory effect. These results suggest that in this form, AChE is not a potential vaccine candidate and that adult ES products, in contrast to previous experiments in guinea pigs, do not contain protective components.
Department of Veterinary Clinical Science and Animal Husbandry, Faculty of Veterinary Science, University of Liverpool, Leahurst, South CH64 7TE, Wirral, UK. j.b.matthews@liv.ac.uk
J B
JB
Matthews
A J
AJ
Davidson
K L
KL
Freeman
N P
NP
French
D000110:Acetylcholinesterase / Q000235:genetics / Q000276:immunology*; D000818:Animals; D000909:Antibodies, Helminth / Q000097:blood; D000947:Antigens, Helminth / Q000276:immunology*; D002417:Cattle; D002418:Cattle Diseases / Q000469:parasitology / Q000517:prevention & control*; D004021:Dictyocaulus / Q000201:enzymology / Q000235:genetics / Q000254:growth & development / Q000276:immunology*; D004022:Dictyocaulus Infections / Q000469:parasitology / Q000517:prevention & control*; D015801:Helminth Proteins / Q000276:immunology; D007114:Immunization; D008213:Lymphocyte Activation; D011993:Recombinant Fusion Proteins / Q000276:immunology
D000909:Antibodies, Helminth; D000947:Antigens, Helminth; D015801:Helminth Proteins; D011993:Recombinant Fusion Proteins; D000110:Acetylcholinesterase