Ochratoxin A promotes porcine circovirus type 2 replication in vitro and in vivo

Gan, Fang; Zhang, Zheqian; Zhi—hua, HU; Hesketh, John E.; Xue, Hongxia; Chen, Xingxiang; Hao, Shu; Huang, Yu; Ezea, Patience Cole; Parveen, Fahmida; Huang, Kehe

doi:10.1016/j.freeradbiomed.2014.12.016

Cited by 49 publications

(56 citation statements)

References 62 publications

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“…After incubation at 37°C for 3 h, total intracellular fluorescence intensity was measured with a Synergy 2 fluorescence microplate reader (BioTek, Winooski, VT, USA). Levels of total intracellular ROS were calculated as the percentage of the RH strain (32). To determine MDA levels, freshly egressed and purified tachyzoites (10 8 ) were used to extract parasite proteins, and MDA levels were detected at 532 nm with the thiobarbituric acid reaction method and an MDA assay kit (Beyotime).…”

Section: Detection Of Ros Malondialdehyde and Total Antioxidant Capmentioning

confidence: 99%

Thioredoxin reductase fromToxoplasma gondii: an essential virulence effector with antioxidant function

et al. 2017

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Thioredoxin reductase (TR) can help pathogens resist oxidative-burst injury from host immune cells by maintaining a thioredoxin-reduction state during NADPH consumption. TR is a necessary virulence factor that enables the persistent infection of some parasites. We performed bioinformatics analyses and biochemical assays to characterize the activity, subcellular localization, and genetic ablation of Toxoplasma gondii TR (TgTR), to shed light on its biologic function. We expressed the TgTR protein with an Escherichia coli expression system and analyzed its enzyme activity, reporting a K m for the recombinant TgTR of 11.47-15.57 mM, using NADPH as a substrate, and 130.48-151.09 mM with dithio-bis-nitrobenzoic acid as a substrate. The TgTR sequence shared homology with that of TR, but lacked a selenocysteine residue in the C-terminal region and was thought to contain 2 flavin adenine dinucleotide (FAD) domains and 1 NADPH domain. In addition, immunoelectron microscopy results showed that TgTR was widely dispersed in the cytoplasm, and we observed that parasite antioxidant capacity, invasion efficiency, and proliferation were decreased in TR-knockout (TR-KO) strains in vitro, although this strain still stimulated the release of reactive oxygen species release in mouse macrophages while being more sensitive to H 2 O 2 toxicity in vitro. Furthermore, our in vivo results revealed that the survival time of mice infected with the TR-KO strain was significantly prolonged relative to that of mice infected with the wild-type strain. These results suggest that TgTR plays an important role in resistance to oxidative damage and can be considered a virulence factor associated with T. gondii

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Section: Detection Of Ros Malondialdehyde and Total Antioxidant Capmentioning

confidence: 99%

Thioredoxin reductase fromToxoplasma gondii: an essential virulence effector with antioxidant function

et al. 2017

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“…In addition, viral reassortment and cross-infection play a contributory role in the ineffectiveness of the vaccine. In particular, previous studies have provided evidence that the severity of viral infection is associated with some environmental, nutritional, and immune factors, such as mycotoxin contamination [3,4], selenium deficiency [5,6], and macrophage polarization [7]. These factors may partially explain the global differences in morbidity and mortality in animals and humans.…”

Section: Introductionmentioning

confidence: 99%

Low-Level Aflatoxin B1 Promotes Influenza Infection and Modulates a Switch in Macrophage Polarization from M1 to M2

Sun

Liu

et al. 2018

Cell Physiol Biochem

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Background/Aims: Swine influenza virus (SIV) is a major pathogen of both animals and humans. Afatoxin B1 (AFB₁) is one of the most common mycotoxins in feed and food. However, the central contribution of AFB₁ to SIV infection remains unclear. Methods: Here, TCID₅₀ assays, fluorescence-based quantitative real-time PCR, western blotting, immunofluorescence staining, histopathological examination, flow cytometry and scanning electron microscopy were performed to investigate the involvement and underlying mechanism of AFB₁ in SIV infection in vivo and in vitro using mouse models and porcine alveolar macrophage (PAM) models, respectively. Results: The in vivo study showed that low levels of AFB₁ promoted SIV infection and increased its severity, as demonstrated by the increased mRNA expression of viral matrix protein (M); by the increased protein expression of nucleoprotein (NP), matrix protein 1 and ion channel protein; and by animal weight loss, lung index and lung histologic damage. In addition, the increased occurrence of SIV infection accompanied by increases in the level of IL-10 in sera and lungs, in the spleen index and in the number of CD206-positive mouse alveolar macrophages but decreases in the level of TNF-α in sera and lungs, in the thymus index and in the number of CD80-positive mouse alveolar macrophages was observed in SIV-infected mice after low-level AFB₁ exposure. The in vitro study showed that low concentrations of AFB₁ promoted SIV infection, as demonstrated by the increases in viral titers and viral M mRNA and NP expression levels in SIV-infected PAMs as well as by the number of cells positive for NP protein expression. Furthermore, AFB₁ promoted the polarization of SIV-infected PAMs to the M1 phenotype at 8 hpi and to the M2 phenotype at 24 hpi, as measured by the increases in IL-10 expression and in the number of CD206-positive PAMs as well as by the morphological changes observed by scanning electron microscopy. The administration of the immune stimulant lipopolysaccharide (LPS) reversed the switch in PAM polarization from M2 to M1 and thereby counteracted the promotion of influenza virus infection induced by AFB₁. Conclusion: Our results are the first to confirm that low-level exposure to AFB₁ promotes SIV infection and modulates a switch in macrophage polarization from M1 to M2. The work reported here provides important data that point to a role for AFB₁ in SIV infection, and it opens a new field of study.

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“…Oxidative stress also activates cellular signaling pathways [75]. Ochratoxin A can promote PCV2 proliferation in PK15 cells via the oxidative stress-mediated p38/ERK1/2 MAPK signaling pathway [76], whereas astragalus polysaccharide inhibited PCV2 DNA replication by decreasing oxidative stress and NFjB signaling pathway activation [77].…”

Section: Interactions Related To Pcv2 Propagationmentioning

confidence: 99%

Interactions of porcine circovirus 2 with its hosts

2016

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Porcine circovirus 2 (PCV2) can cause porcine circovirus diseases and porcine circovirus-associated diseases (PCVD/PCVAD), which are widely presented in swine-producing countries. Since the discovery of this virus, considerable efforts have been devoted to understanding this pathogen and its interactions with its host. Here, we review the current state of knowledge on interactions between host cell factors and PCV2 with respect to viral proliferation, virus-induced cell apoptosis and autophagy, and host antiviral defenses during PCV2 infection. We also review mouse model systems for PCV2 infection.

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Ochratoxin A promotes porcine circovirus type 2 replication in vitro and in vivo

Cited by 49 publications

References 62 publications

Thioredoxin reductase fromToxoplasma gondii: an essential virulence effector with antioxidant function

Thioredoxin reductase fromToxoplasma gondii: an essential virulence effector with antioxidant function

Low-Level Aflatoxin B1 Promotes Influenza Infection and Modulates a Switch in Macrophage Polarization from M1 to M2

Interactions of porcine circovirus 2 with its hosts

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