Molecular cloning, expression and isolation of ferritins from two tick species - Ornithodoros moubata and Ixodes ricinus
1.
SYSNO ASEP
0157624
Document Type
J - Journal Article
R&D Document Type
Journal Article
Subsidiary J
Ostatní články
Title
Molecular cloning, expression and isolation of ferritins from two tick species - Ornithodoros moubata and Ixodes ricinus
Author(s)
Kopáček, Petr (PAU-O) Ždychová, J. (CZ) Yoshiga, T. (US) Weise, C. (DE) Rudenko, Natalia (PAU-O) Law, J. H. (US)
Source Title
Insect Biochemistry and Molecular Biology. - : Elsevier
- ISSN 0965-1748
Roč. 33, č. 1 (2003), s. 103-113
Number of pages
11 s.
Language
eng - English
Country
GB - United Kingdom
Keywords
ferritin ; iron metabolism ; tick
Subject RIV
EB - Genetics ; Molecular Biology
R&D Projects
GA206/00/0266 GA ČR - Czech Science Foundation (CSF)
CEZ
AV0Z6022909 - PAU-O, BC-A
MSM 123100003
Annotation
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. 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.
