title: Proteome-wide analysis of lysine acetylation in adult Schistosoma japonicum worm.
abstract: Lysine acetylation, a ubiquitous and conserved posttranslational modification, has recently been shown to participate in many diverse non-chromatin-associated biological processes in prokaryotes and eukaryotes. However, the full extent and functional significance of acetylation in Schistosoma japonicum is still unknown. To investigate the nature, extent, and biological functions of lysine acetylation in schistosomes, immunoaffinity-based acetyl-lysine peptide enrichment, integrated with mass spectrometry, was used to comprehensively characterize the lysine-acetylated proteins in this parasite. In total, 1109 acetylated proteins and 2393 acetylation sites in S. japonicum were identified, representing the largest acetylome yet reported in a parasite. In a bioinformatic analysis showed that these acetylated proteins were mainly enriched in the biological process categories of metabolism, gene expression, translation, and transport. The classification according to molecular function revealed that the largest class involved the catalytic activity of different enzymes, including oxidoreductase, transferase, and pyrophosphatase activities. Most of the acetylated proteins in the cellular component category occurred in the cytoplasm, membrane, cytoskeleton, and nucleus. These data demonstrate the generality of lysine acetylation and provide the first global survey of acetylation in schistosomes. Our findings are an exciting starting point for the further exploration of the functions of acetylation in the biology of this parasite.
  
  
  
  Schistosomiasis is one of the world's most prevalent and neglected tropical parasitic zoonotic diseases, and it causes almost 200,000 deaths annually. To control and eradicate schistosomiasis, effective vaccines are urgently required, and drug targets that are essential for schistosome survival must be identified in fundamental studies of schistosome biology. Posttranslational modifications are complex, fundamental, and important mechanisms that regulate the physiological functions of organisms. Lysine acetylation, a ubiquitous and conserved posttranslational modification, has recently been shown to participate in many diverse non-chromatin-associated biological processes in prokaryotes and eukaryotes. However, the full extent and functional significance of acetylation in Schistosoma japonicum is still unknown. To investigate the nature, extent, and biological functions of lysine acetylation in S. japonicum, we employ immunoaffinity-based acetyl-lysine peptide enrichment, integrated with mass spectrometry to comprehensively characterize the lysine-acetylated proteins in this parasite. The results of our data demonstrate the generality of lysine acetylation and provide the first global survey of acetylation in schistosomes. Our findings are an exciting starting point for the further exploration of the functions of acetylation in the biology of this parasite. Meanwhile, identifying the mechanisms and proteins targeted by acetylation may also provide a promising avenue for specific drug design and the development of sophisticated therapeutic strategies.
authors.affiliation: Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology, Ministry of Agriculture of China, Shanghai 200241, PR China.
authors.forename: Yang
authors.initials: Y
authors.lastname: Hong
authors.affiliation: Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology, Ministry of Agriculture of China, Shanghai 200241, PR China.
authors.forename: Xiaodan
authors.initials: X
authors.lastname: Cao
authors.affiliation: Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology, Ministry of Agriculture of China, Shanghai 200241, PR China.
authors.forename: Qian
authors.initials: Q
authors.lastname: Han
authors.affiliation: Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology, Ministry of Agriculture of China, Shanghai 200241, PR China.
authors.forename: Chunxiu
authors.initials: C
authors.lastname: Yuan
authors.affiliation: College of Animal Science and Technology, Henan University of Science and Technology, Luoyang, Henan Province 471023, PR China.
authors.forename: Min
authors.initials: M
authors.lastname: Zhang
authors.affiliation: College of Animal Science, Henan Institute of Science and Technology, Xinxiang, Henan Province 453003, PR China.
authors.forename: Yanhui
authors.initials: Y
authors.lastname: Han
authors.affiliation: Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology, Ministry of Agriculture of China, Shanghai 200241, PR China.
authors.forename: Chuangang
authors.initials: C
authors.lastname: Zhu
authors.affiliation: Department of Chemistry and Biochemistry, South Dakota State University, Brookings, SD 57007, United States.
authors.forename: Tao
authors.initials: T
authors.lastname: Lin
authors.affiliation: Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology, Ministry of Agriculture of China, Shanghai 200241, PR China.
authors.forename: Ke
authors.initials: K
authors.lastname: Lu
authors.affiliation: Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology, Ministry of Agriculture of China, Shanghai 200241, PR China.
authors.forename: Hao
authors.initials: H
authors.lastname: Li
authors.affiliation: Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology, Ministry of Agriculture of China, Shanghai 200241, PR China. Electronic address: fuzhiqiang@shvri.ac.cn.
authors.forename: Zhiqiang
authors.initials: Z
authors.lastname: Fu
authors.affiliation: Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology, Ministry of Agriculture of China, Shanghai 200241, PR China; Jiangsu Co-innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou, Jiangsu Province 225009, PR China. Electronic address: jjlin@shvri.ac.cn.
authors.forename: Jiaojiao
authors.initials: J
authors.lastname: Lin
mesh_terms: D000107:Acetylation; D000818:Animals; D001692:Biological Transport; D019295:Computational Biology; D015870:Gene Expression; D015801:Helminth Proteins / Q000032:analysis* / Q000378:metabolism; D008239:Lysine / Q000378:metabolism; D008660:Metabolism; D014176:Protein Biosynthesis; D011499:Protein Processing, Post-Translational; D020543:Proteome / Q000032:analysis / Q000378:metabolism*; D012549:Schistosoma japonicum / Q000737:chemistry*; D053719:Tandem Mass Spectrometry
chemical_list: D015801:Helminth Proteins; D020543:Proteome; D008239:Lysine
keywords: Acetylome; Adult worm; Lysine acetylation (LysAc); Posttranslational modifications; Schistosoma japonicum