Characterization of vitellin protein in the twospotted spider mite, Tetranychus urticae (Acari: Tetranychidae).
In mites, vitellogenin synthesis, regulation and uptake by the oocytes as vitellin remain practically unknown. Although a partial sequence of the gene is now available, no previous studies have been conducted that describe the native vitellin protein in mites. The objective of this study was to characterize vitellin in the twospotted spider mite, Tetranychus urticae. The native twospotted spider mite vitellin migrated as a single major band with a molecular weight of 476+/-14.5 kDa as compared to 590+/-25.5 kDa for vitellin from the American dog tick, Dermacentor variabilis. However, isoelectric focusing analysis of native spider mite vitellin showed five bands with pI values slightly acidic to neutral (pH 5.8, 6.2, 6.7, 7.0 and 7.2), as is the case for insect and tick vitellins. Reducing conditions (SDS-PAGE) also revealed multiple subunits ranging from 290.9 to 3.6 kDa and was similar to that found in D. variabilis. Spider mite vitellin weakly bound lipids and carbohydrates compared to the tick. Unlike D. variabilis, the spider mite egg yolk protein does not bind heme. The significance of non-heme binding in mites is discussed.
Cabrera
Ana R
AR
North Carolina State University, Department of Entomology, Campus Box 7613, Raleigh, NC 27695, USA.
Donohue
Kevin V
KV
Khalil
Sayed M S
SM
Sonenshine
Daniel E
DE
Roe
R Michael
RM
D000818:Animals; D006418:Heme / Q000378:metabolism; D007526:Isoelectric Point; D008970:Molecular Weight; D055550:Protein Stability; D040102:Tetranychidae / Q000737:chemistry* / Q000378:metabolism; D013987:Ticks / Q000737:chemistry / Q000378:metabolism; D047048:Vitellins / Q000737:chemistry* / Q000378:metabolism
D047048:Vitellins; D006418:Heme