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Subolesin/akirin orthologs from Ornithodoros spp soft ticks: cloning, RNAi gene silencing and protective effect of the recombinant proteins

AuthorsManzano Román, Raúl ; Díaz Martín, Verónica ; Oleaga, Ana ; Siles Lucas, Mar ; Pérez Sánchez, Ricardo
Soft ticks
RNA interference
Issue Date2012
CitationVeterinary Parasitology 185: 248-259
AbstractSubolesin/akirin is a well characterized protective antigen highly conserved across vector species and thus potentially useful for the development of a broad-spectrum vaccine for the control of arthropod infestations including hard ticks, mosquitoes, sand flies and the poultry red mite Dermanyssus gallinae. Soft ticks could be also targeted by this vaccine if proved that the soft tick subolesin orthologs are conserved and induce protective immune responses too. However, to date no soft tick subolesin orthologs have been fully characterized nor tested as recombinant antigens in vaccination trials. The objectives of the present work were to clone and characterize the subolesin orthologs from two important vector species of soft ticks as Ornithodoros erraticus and O. moubata, to evaluate the effect of subolesin gene silencing by RNAi, and to test the protective value of the recombinant antigens in vaccination trials. The obtained results demonstrate that both soft tick subolesins are highly conserved showing more than 69% and 74% identity with those of hard ticks in their nucleotide and amino acid sequences, respectively. Additionally, we demonstrate that both soft ticks possess fully operative RNAi machinery, and that subolesin gene silencing by dsRNA injection inhibits oviposition indicating the involvement of subolesin in tick reproduction. Finally, vaccination with the recombinant soft tick subolesins induced a partial protective effect resulting in the reduction of the oviposition rate. These preliminary results encourage further studies on the use of recombinant subolesins as vaccines for the control of soft tick infestations, either alone or in combination with other specific molecules.
Description29 p., 3 tablas, 4 figuras
Publisher version (URL)doi:10.1016/j.vetpar.2011.10.032
Appears in Collections:(IRNASA) Artículos
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