Anti-tick monoclonal antibody applied by artificial capillary feeding in Rhipicephalus (Boophilus) microplus females
Autor: | Andressa Varella Gonsioroski, Aoi Masuda, Itabajara da Silva Vaz, Kiyoko Uemura Utiumi, Sandra Estrazulas Farias, Isis Abel Bezerra, David Driemeier |
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Rok vydání: | 2012 |
Předmět: |
Rhipicephalus (Boophilus) microplus
medicine.drug_class Oviposition Blotting Western Immunology Capillary Tubing Tick Monoclonal antibody Artificial feeding Mice Capillary Antigen parasitic diseases Rhipicephalus medicine Animals Tick Control Antigens Mice Inbred BALB C Vaccines Hybridomas biology Acaricide fungi Antibodies Monoclonal General Medicine biology.organism_classification Immunohistochemistry Virology Infectious Diseases biology.protein Rhipicephalus microplus Cattle Female Parasitology Antibody |
Zdroj: | Experimental Parasitology. 130(4):359-363 |
ISSN: | 0014-4894 |
DOI: | 10.1016/j.exppara.2012.02.006 |
Popis: | The tick Rhipicephalus microplus is an ectoparasite harmful to livestock, a vector of disease agents that affects meat and milk production. However, resistance to acaricides reflects the need for alternative tick control methods, among which vaccines have gained increasing relevance. In this scenario, monoclonal antibodies can be used to identify and characterize antigens that can be used as vaccine immunogens. Capillary tube artificial feeding of partially engorged R. microplus females with monoclonal antibodies against proteins from the gut of tick were used to test the effects of immunoglobulins in the physiology of the parasite. The results of artificial feeding showed that female ticks over 25mg and under 60mg in weight performed better in the artificial feeding process, with a 94–168% weight increase after 24h of feeding. Results showed that artificial feeding of ticks proved to be a viable technique to study the effects of antibodies or drugs in the physiology of the parasite. One monoclonal antibody (BrBm2) induced decreased oviposition. Moreover, the antigen recognized by BrBm2 was identified as a 27-kDa protein and immunolabeled on digestive vesicles membranes of digestive cells of partially and fully engorged females. |
Databáze: | OpenAIRE |
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