Autophagy Activated by Peroxiredoxin of Entamoeba histolytica

DOI Web Site 2 Citations 32 References Open Access
  • Xia Li
    Department of Medical Microbiology and Parasitology, School of Basic Medical Sciences, Fudan University, Shanghai 200000, China
  • Yuhan Zhang
    Department of Medical Microbiology and Parasitology, School of Basic Medical Sciences, Fudan University, Shanghai 200000, China
  • Yanqing Zhao
    Department of Medical Microbiology and Parasitology, School of Basic Medical Sciences, Fudan University, Shanghai 200000, China
  • Ke Qiao
    Institute of Metabolic & Integrative Biology, Fudan University, Shanghai 200438, China
  • Meng Feng
    Department of Medical Microbiology and Parasitology, School of Basic Medical Sciences, Fudan University, Shanghai 200000, China
  • Hang Zhou
    Department of Medical Microbiology and Parasitology, School of Basic Medical Sciences, Fudan University, Shanghai 200000, China
  • Hiroshi Tachibana
    Department of Infectious Diseases, Tokai University School of Medicine, Isehara, Kanagawa 259-1193, Japan
  • Xunjia Cheng
    Department of Medical Microbiology and Parasitology, School of Basic Medical Sciences, Fudan University, Shanghai 200000, China

Description

<jats:p>Autophagy, an evolutionarily conserved mechanism to remove redundant or dangerous cellular components, plays an important role in innate immunity and defense against pathogens, which, in turn, can regulate autophagy to establish infection within a host. However, for Entamoeba histolytica, an intestinal protozoan parasite causing human amoebic colitis, the interaction with the host cell autophagy mechanism has not been investigated. In this study, we found that E. histolytica peroxiredoxin (Prx), an antioxidant enzyme critical for parasite survival during the invasion of host tissues, could activate autophagy in macrophages. The formation of autophagosomes in macrophages treated with recombinant Prx of E. histolytica for 24 h was revealed by immunofluorescence and immunoblotting in RAW264.7 cells and in mice. Prx was cytotoxic for RAW264.7 macrophages after 48-h treatment, which was partly attributed to autophagy-dependent cell death. RNA interference experiments revealed that Prx induced autophagy mostly through the toll-like receptor 4 (TLR4)–TIR domain-containing adaptor-inducing interferon (TRIF) pathway. The C-terminal part of Prx comprising 100 amino acids was the key functional domain to activate autophagy. These results indicated that Prx of E. histolytica could induce autophagy and cytotoxic effects in macrophages, revealing a new pathogenic mechanism activated by E. histolytica in host cells.</jats:p>

Journal

  • Cells

    Cells 9 (11), 2462-, 2020-11-12

    MDPI AG

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