Proteome-wide analysis of lysine acetylation in adult Schistosoma japonicum worm

Hong, Yang; Cao, Xiaodan; Han, Qian; Yuan, Chunxiu; Zhang, Min; Han, Yanhui; Zhu, Chuangang; Lin, Tao; Ke, Lu; Li, Hao; Fu, Zhiqiang; Lin, Jiaojiao

doi:10.1016/j.jprot.2016.08.008

Cited by 24 publications

(42 citation statements)

References 66 publications

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“…Bound conjugates were detected using the SuperSignal WestPico substrate (Pierce) or Clarity Western ECL substrate (BioRad) and images acquired using a UVP Biospectrum–AC w/Bio Chemi camera (Cambridge, United Kingdom) or Bio-Rad ChemiDoc MP imaging system. The specificity of the PTM-specific antibodies has been previously reported (Chu et al, 2016 ; Hong et al, 2016 ).…”

Section: Methodsmentioning

confidence: 66%

Pathogenic Leptospires Modulate Protein Expression and Post-translational Modifications in Response to Mammalian Host Signals

Nally

Grassmann

Planchon

et al. 2017

Front. Cell. Infect. Microbiol.

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Pathogenic species of Leptospira cause leptospirosis, a bacterial zoonotic disease with a global distribution affecting over one million people annually. Reservoir hosts of leptospirosis, including rodents, dogs, and cattle, exhibit little to no signs of disease but shed large numbers of organisms in their urine. Transmission occurs when mucosal surfaces or abraded skin come into contact with infected urine or urine-contaminated water or soil. Whilst little is known about how Leptospira adapt to and persist within a reservoir host, in vitro studies suggest that leptospires alter their transcriptomic and proteomic profiles in response to environmental signals encountered during mammalian infection. We applied the dialysis membrane chamber (DMC) peritoneal implant model to compare the whole cell proteome of in vivo derived leptospires with that of leptospires cultivated in vitro at 30°C and 37°C by 2-dimensional difference in-gel electrophoresis (2-D DIGE). Of 1,735 protein spots aligned across 9 2-D DIGE gels, 202 protein spots were differentially expressed (p < 0.05, fold change >1.25 or < −1.25) across all three conditions. Differentially expressed proteins were excised for identification by mass spectrometry. Data are available via ProteomeXchange with identifier PXD006995. The greatest differences were detected when DMC-cultivated leptospires were compared with IV30- or IV37-cultivated leptospires, including the increased expression of multiple isoforms of Loa22, a known virulence factor. Unexpectedly, 20 protein isoforms of LipL32 and 7 isoforms of LipL41 were uniformly identified by DIGE as differentially expressed, suggesting that unique post-translational modifications (PTMs) are operative in response to mammalian host conditions. To test this hypothesis, a rat model of persistent renal colonization was used to isolate leptospires directly from the urine of experimentally infected rats. Comparison of urinary derived leptospires to IV30 leptospires by 2-D immunoblotting confirmed that modification of proteins with trimethyllysine and acetyllysine occurs to a different degree in response to mammalian host signals encountered during persistent renal colonization. These results provide novel insights into differential protein and PTMs present in response to mammalian host signals which can be used to further define the unique equilibrium that exists between pathogenic leptospires and their reservoir host of infection.

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Section: Methodsmentioning

confidence: 66%

Pathogenic Leptospires Modulate Protein Expression and Post-translational Modifications in Response to Mammalian Host Signals

Nally

Grassmann

Planchon

et al. 2017

Front. Cell. Infect. Microbiol.

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“…RhoA was not identified by Joshi et al . [ 21 ] as interacting with hHDAC8 and does not seem to be acetylated in human [ 22 ], although it was found to be acetylated in Schistosoma japonicum [ 51 ]. Here, our Y2H screen shows the direct interaction between Sm HDAC8 and Sm Rho1, the orthologue of human RhoA.…”

Section: Resultsmentioning

confidence: 99%

Analysis of the interactome of Schistosoma mansoni histone deacetylase 8

et al. 2017

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BackgroundHistone deacetylase 8 from Schistosoma mansoni (SmHDAC8) is essential to parasite growth and development within the mammalian host and is under investigation as a target for the development of selective inhibitors as novel schistosomicidal drugs. Although some protein substrates and protein partners of human HDAC8 have been characterized, notably indicating a role in the function of the cohesin complex, nothing is known of the partners and biological function of SmHDAC8.Methodology/Principal findingsWe therefore employed two strategies to characterize the SmHDAC8 interactome. We first used SmHDAC8 as a bait protein in yeast two-hybrid (Y2H) screening of an S. mansoni cDNA library. This allowed the identification of 49 different sequences encoding proteins. We next performed co-immunoprecipitation (Co-IP) experiments on parasite extracts with an anti-SmHDAC8 antibody. Mass spectrometry (MS) analysis allowed the identification of 160 different proteins.Conclusions/SignificanceSmHDAC8 partners are involved in about 40 different processes, included expected functions such as the cohesin complex, cytoskeleton organization, transcriptional and translational regulation, metabolism, DNA repair, the cell cycle, protein dephosphorylation, proteolysis, protein transport, but also some proteasome and ribosome components were detected. Our results show that SmHDAC8 is a versatile deacetylase, potentially involved in both cytosolic and nuclear processes.

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“…Proteome-wide lysine acetylation has been extensively studied in plant (Fang et al, 2015 ), bacteria (Zhang et al, 2009 ; Xie et al, 2015 ), yeast (Henriksen, 2012 ), Drosophila melanogaster (Weinert et al, 2011 ), human cells (Kim et al, 2006 ; Choudhary et al, 2009 ; Zhao et al, 2010 ), as well as the protozoan parasites Toxoplasma gondii and Plasmodium falciparum (Jeffers and Sullivan, 2012 ; Miao et al, 2013 ). The first study of lysine acetylation in Schistosoma japonicum was also reported, in which 2393 acetylated sites in 1109 acetylated proteins were identified from 42 dpi adult worms (Hong et al, 2016 ). We believe comparative studies of acetylation profiles in different developmental stages will identify differentially acetylated proteins, and by investigating how acetylation of these proteins affects their biological functions, the impacts of protein lysine acetylation on S. japonicum developmental regulation will be further elucidated.…”

Section: Introductionmentioning

confidence: 99%

Comparative Analysis of Proteome-Wide Lysine Acetylation in Juvenile and Adult Schistosoma japonicum

Zhao

et al. 2017

Front. Microbiol.

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Schistosomiasis is a devastating parasitic disease caused by tremotodes of the genus Schistosoma. Eggs produced by sexually mature schistosomes are the causative agents of for pathogenesis and transmission. Elucidating the molecular mechanism of schistosome development and sexual maturation would facilitate the prevention and control of schistosomiasis. Acetylation of lysine is a dynamic and reversible post-translational modification playing keys role in many biological processes including development in both eukaryotes and prokaryotes. To investigate the impacts of lysine acetylation on Schistosoma japonicum (S. japonicum) development and sexual maturation, we used immunoaffinity-based acetyllysine peptide enrichment combined with mass spectrometry (MS), to perform the first comparative analysis of proteome-wide lysine acetylation in both female and male, juvenile (18 days post infection, 18 dpi) and adult (28 dpi) schistosome samples. In total, we identified 874 unique acetylated sites in 494 acetylated proteins. The four samples shared 47 acetylated sites and 46 proteins. More acetylated sites and proteins shared by both females and males were identified in 28 dpi adults (189 and 143, respectively) than in 18 dpi schistosomula (76 and 59, respectively). More stage-unique acetylated sites and proteins were also identified in 28 dpi adults (494 and 210, respectively) than in 18 dpi schistosomula (73 and 44, respectively). Functional annotation showed that in different developmental stages and genders, a number of proteins involving in muscle movement, glycometabolism, lipid metabolism, energy metabolism, environmental stress resistance, antioxidation, etc., displayed distinct acetylation profiles, which was in accordance with the changes of their biological functions during schistosome development, suggesting that lysine acetylation modification exerted important regulatory roles in schistosome development. Taken together, our data provided the first comparative global survey of lysine acetylation in juvenile and adult S. japonicum, which would deepen our understanding of the molecular mechanism of schistosome development and sexual maturation, and provide clues for the development of new anti-schistosome strategies.

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Proteome-wide analysis of lysine acetylation in adult Schistosoma japonicum worm

Cited by 24 publications

References 66 publications

Pathogenic Leptospires Modulate Protein Expression and Post-translational Modifications in Response to Mammalian Host Signals

Pathogenic Leptospires Modulate Protein Expression and Post-translational Modifications in Response to Mammalian Host Signals

Analysis of the interactome of Schistosoma mansoni histone deacetylase 8

Comparative Analysis of Proteome-Wide Lysine Acetylation in Juvenile and Adult Schistosoma japonicum

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