Abstract

BackgroundN-acetyltransferase 13 (NAT13) is a probable catalytic component of the ARD1A-NARG1 complex possessing alpha (N-terminal) acetyltransferase activity.ResultsIn this study, a full-length complementary DNA (cDNA) encoding Schistosoma japonicum NAT13 (SjNAT13) was isolated from schistosome cDNAs. The 621 bp open reading frame of SjNAT13 encodes a polypeptide of 206 amino acids. Real-time PCR analysis revealed SjNAT13 expression in all tested developmental stages. Transcript levels were highest in cercariae and 21-day-old worms, and higher in male adult worms than female adult worms. The rSjNAT13 protein induced high levels of anti-rSjNAT13 IgG antibodies. In two independent immunoprotection trials, rSjNAT13 induced 24.23% and 24.47% reductions in the numbers of eggs in liver. RNA interference (RNAi) results showed that small interfering RNA (siRNA) Sj-514 significantly reduced SjNAT13 transcript levels in worms and decreased egg production in vitro.ConclusionsThus, rSjNAT13 might play an important role in the development and reproduction of schistosomes.

Highlights

  • Schistosomiasis is a chronic and damaging zoonotic parasitic disease caused by trematode worms of the genus Schistosoma

  • Expression and purification of rSjNAT13 The full-length sequence of Schistosoma japonicum NAT13 (SjNAT13) was obtained by Room temperature (RT)-PCR amplification from complementary DNA (cDNA) of schistosomes

  • The rSjNAT13 protein containing a His-tag was successfully expressed in E. coli BL21 (DE3) cells induced by IPTG at 37 °C

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Summary

Introduction

Schistosomiasis is a chronic and damaging zoonotic parasitic disease caused by trematode worms of the genus Schistosoma. It affects more than 200 million people in 52 countries across Africa, Asia and South America [1]. First discovered for histones, has been extensively studied in prokaryotes and eukaryotes [4,5,6,7,8,9]. It plays a critical role in the regulation of gene target gene expression [10, 11]. N-acetyltransferase 13 (NAT13) is a probable catalytic component of the ARD1A-NARG1 complex possessing alpha (N-terminal) acetyltransferase activity

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