Npro His49 and Erns Lys412 mutations in pig bovine viral diarrhea virus type 2 synergistically enhance the cellular antiviral response

Tao, Jie; Li, Benqiang; Chen, Jinghua; Zhang, Chunyu; Ma, Yufei; Zhu, Guoqiang; Liu, Huili

doi:10.1007/s11262-017-1506-3

Cited by 4 publications

(2 citation statements)

References 29 publications

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“…However, the double mutant of N pro and E rns above-mentioned could significantly induce the production of IFN-I, thereby preventing the establishment of the PI fetus, indicating that N pro and E rns have a synergistic effect in the formation of PI (Meyers et al, 2007). Furthermore, Tao et al of our group discovered that N pro His49 and E rns Lys412 were crux amino acid sites in this course (Tao et al, 2018). In short, BVDV N pro and E rns are nonredundant antagonists of IFN that cooperate to escape the host's antiviral response in vivo and in vitro.…”

Section: E Rns Inhibits Ifns Productionmentioning

confidence: 75%

Pestiviruses infection: Interferon-virus mutual regulation

Hong

Yang²,

Wang³

et al. 2023

Front. Cell. Infect. Microbiol.

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Pestiviruses are a class of viruses that in some cases can cause persistent infection of the host, thus posing a threat to the livestock industry. Interferons (IFNs) are a group of secreted proteins that play a crucial role in antiviral defense. In this review, on the one hand, we elaborate on how pestiviruses are recognized by the host retinoic acid-inducible gene-I (RIG-I), melanoma-differentiation-associated protein 5 (MDA5), and Toll-like receptor 3 (TLR3) proteins to induce the synthesis of IFNs. On the other hand, we focus on reviewing how pestiviruses antagonize the production of IFNs utilizing various strategies mediated by self-encoded proteins, such as the structural envelope protein (Erns) and non-structural protein (Npro). Hence, the IFN signal transduction pathway induced by pestiviruses infection and the process of pestiviruses blockade on the production of IFNs intertwines into an intricate regulatory network. By reviewing the interaction between IFN and pestiviruses (based on studies on BVDV and CSFV), we expect to provide a theoretical basis and reference for a better understanding of the mechanisms of induction and evasion of the innate immune response during infection with these viruses.

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Section: E Rns Inhibits Ifns Productionmentioning

confidence: 75%

Pestiviruses infection: Interferon-virus mutual regulation

Hong

Yang²,

Wang³

et al. 2023

Front. Cell. Infect. Microbiol.

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“…Here, we provide strong evidence that the envelope glycoprotein E rns of most pestiviruses possess dsRNase activity and is able to block dsRNA-induced IFN synthesis, with only the E rns of pronghorn antelope displaying the lowest activity as RNase and no activity in our in vitro Mx assays. Thus, only the E rns proteins from BVDV-2 (Pestivirus B) and ovine pestiviruses (Pestivirus O) have not yet formally been shown to be able to act as IFN antagonist, with indirect evidence reported for BVDV-2 [53]. However, based on the sequence conservation and their close proximity to the classical ruminant pestiviruses, it is highly probable that their E rns proteins possess similar activities.…”

Section: Discussionmentioning

confidence: 99%

Fifty Shades of Erns: Innate Immune Evasion by the Viral Endonucleases of All Pestivirus Species

Martin

Schweizer

2022

Viruses

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The genus Pestivirus, family Flaviviridae, includes four historically accepted species, i.e., bovine viral diarrhea virus (BVDV)-1 and -2, classical swine fever virus (CSFV), and border disease virus (BDV). A large number of new pestivirus species were identified in recent years. A common feature of most members is the presence of two unique proteins, Npro and Erns, that pestiviruses evolved to regulate the host’s innate immune response. In addition to its function as a structural envelope glycoprotein, Erns is also released in the extracellular space, where it is endocytosed by neighboring cells. As an endoribonuclease, Erns is able to cleave viral ss- and dsRNAs, thus preventing the stimulation of the host’s interferon (IFN) response. Here, we characterize the basic features of soluble Erns of a large variety of classified and unassigned pestiviruses that have not yet been described. Its ability to form homodimers, its RNase activity, and the ability to inhibit dsRNA-induced IFN synthesis were investigated. Overall, we found large differences between the various Erns proteins that cannot be predicted solely based on their primary amino acid sequences, and that might be the consequence of different virus-host co-evolution histories. This provides valuable information to delineate the structure-function relationship of pestiviral endoribonucleases.

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