The Role of Zinc-Finger Antiviral Proteins in Immunity against Viruses
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The Role of Zinc-Finger Antiviral Proteins in Immunity against Viruses Syed Lal Badshaha, *, Asad Ullaha, and Shahzia Syedb aDepartment
of Chemistry, Islamia College University Peshawar, Peshawar, 25120 Pakistan of Zoology, University of Peshawar, Peshawar, 25120 Pakistan *e-mail: [email protected]
bDepartment
Received December 10, 2019; revised December 17, 2019; accepted December 23, 2019
Abstract—The Zinc finger antiviral proteins (ZAP) are expressed by the cells in response to different viral attacks. The ZAP marks the viral mRNA for degradation with the help of different cellular proteins for exosome. Beside the degradation of viral mRNA, the ZAP protein also inihibits translation of proteins from this mRNA. Although it is not a universal antiviral protein, but a number of important human pathogenic viruses are controlled by the ZAP protein. In this review article we have discussed the current progress made in understanding the structure, function, mechanism and therapeutic roles of the ZAP protein. Keywords: zinc-finger domain, ribonucleic acids, exosomes, engineered proteins, antiviral agents DOI: 10.3103/S0891416820020020
of the ZAP protein [8]. The ZAP are also called Poly(ADP-ribose) Polymerase-13 (PARP-13) [9]. The ZAP protein was initially discovered in rats and later on it was identified in humans [10, 11]. The different forms of ZAP/PARP proteins are present inside the cytoplasm, where it is localized to membrane organelles like endoplasmic reticulum and Golgi apparatus [12, 13]. Zho and Gao presented their point of view on the ZAP proteins and their role in different viral mRNA degradation [14]. The ZAP virus inhibit the replication of different viruses but it does not possess antiviral inhibitory affect against all of the viruses [14]. The ZAP protein identifies the positive and negative-stranded RNA group of viruses including Retroviridae, Filoviridae, Togaviridae, Hepadnaviridae and murine gammaherpesvirus [7]. Zho and Gao propsed that the N-terminal domain is the most functional part while the C-terminal has regulatory role [14]. Humans possess two form of the ZAP protein (Fig. 2). The two isoforms differ from one another in the C-terminals domain and amino acid sequence length [11]. It has been observed that the longer isoform has high antiviral activity when tested on alphaviruses [11, 15]. The long ZAP protein isoform contains a poly(ADP-ribose) polymerase (PARP)-like domain at the C-terminus that is essential for its antiviral action [15]. It has been observed that mutation of this triad to other amino acids like alanine resulted in complete loss of antiviral activity [15]. It has been observed that the ZAP protein not only inhibit the viruses but also transposons and retrotransposons [16]. The ZAP or PARP also regulate the host mRNA in the absence of viral infection and
BACKGROUND The zinc finger proteins are the proteins that are involved in interaction with DNA, RNA and proteins and have diverse functions [1]. They contain a structural motif where one or more zinc ions (
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