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Longistatin, an EF-hand Ca2+-binding protein from vector tick: identification, purification, and characterization
Anisuzzaman1, M Khyrul Islam, M Abdul Alim
1Department of Global Agricultural Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan.
Methods in Molecular Biology (Clifton, N.J.)
|January 9, 2013
Summary
Researchers discovered longistatin, an EF-hand calcium-binding protein in tick saliva. This secreted protein functions extracellularly, acting as a calcium sensor or buffer.
Area of Science:
- Biochemistry
- Molecular Biology
- Parasitology
Background:
- EF-hand proteins typically function intracellularly as calcium sensors or buffers.
- Some EF-hand proteins are secreted and play extracellular roles.
Purpose of the Study:
- To identify and characterize novel EF-hand calcium-binding proteins from tick salivary glands.
- To investigate the structure and function of the identified protein, longistatin.
Main Methods:
- Identification of longistatin from the salivary glands of Haemaphysalis longicornis.
- Analysis of longistatin's structure, including its EF-hand motifs.
- Electrophoresis (SDS-PAGE) in the presence of calcium and EDTA.
- Ruthenium red staining to confirm calcium-binding properties.
Main Results:
- Longistatin, an EF-hand Ca(2+)-binding protein, was identified in tick saliva.
- Longistatin exhibits a calmodulin-like structure with two EF-hand motifs.
- Distinct electrophoretic mobility changes and positive ruthenium red staining confirm its calcium-binding ability.
Conclusions:
- Longistatin is an extracellularly functioning EF-hand calcium-binding protein secreted by ticks.
- This discovery expands the known roles of EF-hand proteins beyond intracellular calcium regulation.
