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Yuan, D.* ; Luo, S. ; Xu, L.* ; Zeng, X.* ; Wu, Z.*

Regulatory effect of host miR-101b-3p on parasitism of nematode Angiostrongylus cantonensis via superoxide dismutase 3.

Biochim. Biophys. Acta-Gene Regul. Mech. 1862, 557-566 (2019)
DOI PMC
MicroRNA plays a vital role in the regulation of host-parasite interaction. In recent years, genomic and transcriptomic resources have become increasingly available for many helminths, but only a limited number of reports in this area are on the regulatory effects of host microRNAs on parasitic nematodes. In this work, we screened increased expression of host microRNAs after nematode infection from miRNA-seq data and predicted target genes by combined bioinformatics analysis and transcriptional profiling. We elucidated regulatory effects of one host miRNA on nematode infection using miRNA inhibitor and adeno-associated virus (AAV)-based TuD miRNA inhibitor. Using AAV-based TuD miRNA inhibitor, we showed that stable blockade of mmu-miR-101b-3p could alleviate the pathological damages of Angiostrongylus cantonensis, a parasitic nematode. Data from a luciferase report assay showed that mmu-miR-101b-3p targeted the extracellular superoxide dismutase 3 (Acsod3). Increased Acsod3 expression in larvae and alleviated oxidative damages were seen in the groups receiving mmumiR-101b-3p inhibitor treatment in vitro and AAV-based TuD miRNA inhibitor injection in vivo. Results of this study demonstrate that murine miR-101b-3p inhibits the expression of antioxidant enzyme in A. cantonensis to strengthen host oxidative responses to nematodes. This work expands our knowledge of interspecies regulation of nematode gene expression by of host miRNAs.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Mmu-mir-101b-3p ; Angiostrongylus Cantonensis ; Superoxide Dismutase ; Inhibitor; Oxidative Stress; Expression; Localization; Enzymes; Sod
ISSN (print) / ISBN 1874-9399
e-ISSN 1876-4320
Zeitschrift Biochimica et Biophysica Acta - Gene Regulatory Mechanisms
Quellenangaben Band: 1862, Heft: 5, Seiten: 557-566 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort Po Box 211, 1000 Ae Amsterdam, Netherlands
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Virology (VIRO)