Genes encoding ferritins were isolated and cloned from cDNA libraries of hard tick Ixodes ricinus and soft tick Ornithodoros moubata. Both tick ferritins are composed of 172 amino-acid residues and their calculated mass is 19,667.2 Da and 19,974.5 Da for I. ricinus and O. moubata, respectively. The sequences of both proteins are closely related to each other as well as to the ferritin from another tick species Dermacentor variabilis (>84% similarity). The proteins contain the conserved motifs for ferroxidase center typical for heavy chains of vertebrate ferritins. The stem-loop structure of a putative iron responsive element was found in the 5' untranslated region of ferritin mRNA of both ticks. Antibodies against fusion ferritin from O. moubata were raised in a rabbit and used to monitor the purification of a small amount of ferritins from both tick species. The authenticity of ferritin purified from O. moubata was confirmed by mass-fingerprinting analysis. In the native state, the tick ferritins are apparently larger (~500 kDa) than horse spleen ferritin (440 kDa). On SDS-PAGE tick ferritins migrate as a single band of about 21 kDa. These results suggest that tick ferritins are homo-oligomers of 24 identical subunits of heavy-chain type. The Northern blot analysis revealed that O. moubata ferritin mRNA level is likely not up-regulated after ingestion of a blood meal.

Institute of Parasitology Academy of Sciences of the Czech Republic and Faculty of Biological Sciences University of South Bohemia Branisovská 31 370 05 Ceské Budejovice Czech Republic

Citace poskytuje Crossref.org

Genome sequences of four Ixodes species expands understanding of tick evolution

Ixodes ricinus Salivary Serpin Iripin-8 Inhibits the Intrinsic Pathway of Coagulation and Complement

Mialostatin, a Novel Midgut Cystatin from Ixodes ricinus Ticks: Crystal Structure and Regulation of Host Blood Digestion

The structure and function of Iristatin, a novel immunosuppressive tick salivary cystatin

RNA-seq analyses of the midgut from blood- and serum-fed Ixodes ricinus ticks

Acquisition of exogenous haem is essential for tick reproduction

Characterization of gut-associated cathepsin D hemoglobinase from tick Ixodes ricinus (IrCD1)

Dynamics of digestive proteolytic system during blood feeding of the hard tick Ixodes ricinus

Knockdown of proteins involved in iron metabolism limits tick reproduction and development

Insight into the sialome of the castor bean tick, Ixodes ricinus

Profiling of proteolytic enzymes in the gut of the tick Ixodes ricinus reveals an evolutionarily conserved network of aspartic and cysteine peptidases

IrAE: an asparaginyl endopeptidase (legumain) in the gut of the hard tick Ixodes ricinus

Zobrazit více v PubMed

GENBANK
AF068224, AF068225