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The Korean Journal of Parasitology ; : 117-120, 2014.
Artigo em Inglês | WPRIM | ID: wpr-14498

RESUMO

Several studies have reported that the citrus red mites Panonychus citri were an important allergen of citrus-cultivating farmers in Jeju Island. The aim of the present study was to purify and assess properties of a cysteine protease from the mites acting as a potentially pathogenic factor to citrus-cultivating farmers. A cysteine protease was purified using column chromatography of Mono Q anion exchanger and Superdex 200 HR gel filtration. It was estimated to be 46 kDa by gel filtration column chromatography and consisted of 2 polypeptides, at least. Cysteine protease inhibitors, such as trans poxy-succinyl-L-leucyl-amido (4-guanidino) butane (E-64) and iodoacetic acid (IAA) totally inhibited the enzyme activities, whereas serine or metalloprotease inhibitors did not affect the activities. In addition, the purified enzyme degraded human IgG, collagen, and fibronectin, but not egg albumin. From these results, the cysteine protease of the mites might be involved in the pathogenesis such as tissue destruction and penetration instead of nutrient digestion.


Assuntos
Animais , Humanos , Cromatografia em Gel , Cromatografia por Troca Iônica , Colágeno/metabolismo , Cisteína Proteases/química , Inibidores de Cisteína Proteinase/metabolismo , Fibronectinas/metabolismo , Imunoglobulina G/metabolismo , Peso Molecular , Subunidades Proteicas/química , Proteólise , Especificidade por Substrato , Tetranychidae/enzimologia
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