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Published on: January 21, 2020
Identification and functional characterization of a novel cytidine deaminase in a gastropod abalone, Haliotis
Liuji Wu1, Xinzhong Wu, Baojian Zhu
1Laboratory of Marine Life Science and Technology, College of Animal Sciences, Zhejiang University, 268 Kaixuan Road, Hangzhou, PR China.
Abstract:
Cytidine deaminase (CDA, also designated CDD) is a zinc-dependent enzyme involved in the pyrimidine salvage pathways and becoming very important in anticancer and antiviral therapy. Here we report the identification and characterization of a CDA homologue in abalone, which we named ab-CDA. The analysis of the amino acids sequence revealed that the ab-CDA shares conserved signature motifs and belongs to homotetrameric class of CDA family. Real-time PCR analysis indicated that the ab-CDA was ubiquitously expressed in various tissues of abalone and relatively higher expressed in hemocyte. Significant up-regulation of ab-CDA was also observed after LPS or Poly I: C challenge. The biological activity of ab-CDA was identified by spectrophotometry analysis and the intracellular localization displayed that ab-CDA was largely concentrated in the cytoplasm and partially in the nuclei. These results strongly suggest that ab-CDA is a CDA homologue and it is involved in the immune response of gastropod abalone.

