Functional characterization of a cystatin from the tick Rhipicephalus haemaphysaloides.

ABSTRACT:

Background

Ticks and tick-borne diseases affect animal and human health worldwide and cause significant economic losses in the animal industry. Functional molecular research is important to understand the biological characteristics of ticks at the molecular level. Enzymes and enzyme inhibitory molecules play very important roles in tick physiology, and the cystatins are tight-binding inhibitors of papain-like cysteine proteases. To this end, a novel cystatin, designated RHcyst-1, was isolated from the tick Rhipicephalus haemaphysaloides.

Methods

The full-length gene of RHcyst-1 was cloning by RACE. The recombinant protein of RHcyst-1 was expressed in a glutathione S-transferase (GST)-fused soluble form in Escherichia coli, and its inhibitory activity against cathepsin L, B,

SUBMITTER: Wang Y 

PROVIDER: S-EPMC4352250 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature