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Functional characterization of Schistosoma mansoni fucosyltransferases in Nicotiana benthamiana plants.

ABSTRACT: Helminth parasites secrete a wide variety of immunomodulatory proteins and lipids to dampen host immune responses. Many of these immunomodulatory compounds are modified with complex sugar structures (or glycans), which play an important role at the host-parasite interface. As an example, the human blood fluke Schistosoma mansoni produces highly fucosylated glycan structures on glycoproteins and glycolipids. Up to 20 different S. mansoni fucosyltransferase (SmFucT) genes can be found in genome databases, but thus far only one enzyme has been functionally characterized. To unravel the synthesis of highly fucosylated N-glycans by S. mansoni, we examined the ability of ten selected SmFucTs to modify N-glycans upon transient expression in Nicotiana benthamiana plants. All enzymes were localized in the plant Golgi apparatus, which allowed us to identify the SmFucTs involved in core fucosylation and the synthesis of complex antennary glycan motifs. This knowledge provides a starting point for investigations into the role of specific fucosylated glycan motifs of schistosomes in parasite-host interactions. The functionally characterized SmFucTs can also be applied to synthesize complex N-glycan structures on recombinant proteins to study their contribution to immunomodulation. Furthermore, this plant expression system will fuel the development of helminth glycoproteins for pharmaceutical applications or novel anti-helminth vaccines.

SUBMITTER: van Noort K

PROVIDER: S-EPMC7595089 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

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Functional characterization of Schistosoma mansoni fucosyltransferases in Nicotiana benthamiana plants.

van Noort Kim K Nguyen Dieu-Linh DL Kriechbaumer Verena V Hawes Chris C Hokke Cornelis H CH Schots Arjen A Wilbers Ruud H P RHP

Scientific reports 20201028 1

Helminth parasites secrete a wide variety of immunomodulatory proteins and lipids to dampen host immune responses. Many of these immunomodulatory compounds are modified with complex sugar structures (or glycans), which play an important role at the host-parasite interface. As an example, the human blood fluke Schistosoma mansoni produces highly fucosylated glycan structures on glycoproteins and glycolipids. Up to 20 different S. mansoni fucosyltransferase (SmFucT) genes can be found in genome da ...[more]

PMID: 33116178

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Project description:PA28? is a proteasome activator involved in the regulation of the cellular proliferation, differentiation and growth. In the present study, we identified and characterized a cDNA from Schistosoma mansoni exhibiting significant homology to PA28? of diverse taxa ranging from mammals (including humans) to simple invertebrates. Designated SmPA28?, this transcript has a 753bp predicted ORF encoding a protein of 250 amino acid residues. Alignment of SmPA28? with multiple PA28? orthologues revealed an average similarity of ~40% among the investigated organisms, and 90% similarity with PA28? from Schistosoma japonicum. In addition, phylogenetic analysis demonstrated a close linkage between SmPA28? to its sister group that contains well-characterized PA28? sequences from Drosophila spp., as well as sharing the same branch with PA28? from S. japonicum. Gene expression profiling of SmPA28? using real-time quantitative PCR revealed elevated steady-state transcript levels in the eggs, miracidia and paired adult worms compared to other stages. In parallel with gene expression profiles, an affinity-purified anti-SmPA28? antibody produced against recombinant protein exhibited strongest reactivity in Western blot analyses to endogenous SmPA28? from miracidia, sporocysts and paired adult worms. Given its known regulatory function in other organisms, we hypothesized that the high level of SmPA28? transcript and protein in these stages may be correlated with an important role of the PA28? in the cellular growth and/or development of this parasite. To address this hypothesis, miracidia were transformed in vitro to sporocysts in the presence of SmPA28? double-stranded RNAs (dsRNAs) and cultivated for 4 days, after which time steady-state transcript and protein levels, and phenotypic changes were evaluated. SmPA28? dsRNA treatment resulted in gene and protein knockdown of ~60% and ~80%, respectively, which were correlated with a significant decrease in larval length compared to its controls. These findings are consistent with a putative role of SmPA28? in larval growth/development of the S. mansoni.

Dataset Information

Functional characterization of Schistosoma mansoni fucosyltransferases in Nicotiana benthamiana plants.

Publications

Functional characterization of Schistosoma mansoni fucosyltransferases in Nicotiana benthamiana plants.

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