Molecular and enzymatic characterization of acid phosphatase from venom of Scleroderma guani

Acid phosphatase (ACPase) is a common component in venom of parasitoids. Although extensive researches regarding this enzyme have been conducted in many other organisms, its characteristics as a venomous enzyme are still sparsely known. In this study, we aimed to reveal the gene expression patterns,...

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Bibliographic Details
Published in:Journal of Asia-Pacific entomology 2017, 20(4), , pp.1434-1441
Main Authors: Liu, Nai-Yong, Fan, Xiao-Hong, Zhang, Zhi-Quan, Wu, Guo-Xing, Zhu, Jia-Ying
Format: Article
Language:English
Subjects:
Acid phosphatase
Enzymatic activity
Molecular cloning
Scleroderma guani
Structure
Venom
농수해양학
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Summary:Acid phosphatase (ACPase) is a common component in venom of parasitoids. Although extensive researches regarding this enzyme have been conducted in many other organisms, its characteristics as a venomous enzyme are still sparsely known. In this study, we aimed to reveal the gene expression patterns, and structural and biochemical properties of an ACPase from the venom of Scleroderma guani. The cloned open reading frame of venomous ACPase gene of S. guani was 1218bp encoding 406 deduced amino acids, shared 40% and 41% identities to ACPases from venoms of Apis mellifera and Pteromalus puparum, respectively. The structural analysis of this ACPase implied common functions and differences to the honeybee venom ACPase. qPCR analysis showed that this gene was abundantly expressed in the venom apparatus, and most highly expressed in the adult stage after one and three days emergence. Activity assay using p-nitrophenyl phosphate as the substrate revealed that the optimal pH and temperature for this venomous enzyme was 4.8 and 45°C, respectively. NaF is an effective inhibitor for it. The results will enrich our knowledge for the ACPase as toxin, which may contribute to further uncovering its role involved in parasitism. [Display omitted] •An acid phosphatase was cloned in Scleroderma guani.•The acid phosphatase was abundantly expressed in venom apparatus and early emerged adult.•Structural differences of acid phosphatases between S. guani and Apis mellifera were presented.•The acid phosphatase displayed optimal activity at pH4.8 and 45°C.•NaF was an effective inhibitor of the acid phosphatase.
ISSN:1226-8615
1876-7990
DOI:10.1016/j.aspen.2017.10.012