Viral-Mediated mRNA Degradation for Pathogenesis
Identifieur interne : 000A75 ( Pmc/Corpus ); précédent : 000A74; suivant : 000A76Viral-Mediated mRNA Degradation for Pathogenesis
Auteurs : Shujuan Du ; Xiaoqing Liu ; Qiliang CaiSource :
- Biomedicines [ 2227-9059 ] ; 2018.
Abstract
Cellular RNA decay machinery plays a vital role in regulating gene expression by altering the stability of mRNAs in response to external stresses, including viral infection. In the primary infection, viruses often conquer the host cell’s antiviral immune response by controlling the inherently cellular mRNA degradation machinery to facilitate viral gene expression and establish a successful infection. This review summarizes the current knowledge about the diverse strategies of viral-mediated regulatory RNA shutoff for pathogenesis, and particularly sheds a light on the mechanisms that viruses evolve to elude immune surveillance during infection.
Url:
DOI: 10.3390/biomedicines6040111
PubMed: 30501096
PubMed Central: 6315618
Links to Exploration step
PMC:6315618Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Viral-Mediated mRNA Degradation for Pathogenesis</title><author><name sortKey="Du, Shujuan" sort="Du, Shujuan" uniqKey="Du S" first="Shujuan" last="Du">Shujuan Du</name><affiliation><nlm:aff id="af1-biomedicines-06-00111"></nlm:aff></affiliation></author><author><name sortKey="Liu, Xiaoqing" sort="Liu, Xiaoqing" uniqKey="Liu X" first="Xiaoqing" last="Liu">Xiaoqing Liu</name><affiliation><nlm:aff id="af1-biomedicines-06-00111"></nlm:aff></affiliation></author><author><name sortKey="Cai, Qiliang" sort="Cai, Qiliang" uniqKey="Cai Q" first="Qiliang" last="Cai">Qiliang Cai</name><affiliation><nlm:aff id="af1-biomedicines-06-00111"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">30501096</idno><idno type="pmc">6315618</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6315618</idno><idno type="RBID">PMC:6315618</idno><idno type="doi">10.3390/biomedicines6040111</idno><date when="2018">2018</date><idno type="wicri:Area/Pmc/Corpus">000A75</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000A75</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Viral-Mediated mRNA Degradation for Pathogenesis</title><author><name sortKey="Du, Shujuan" sort="Du, Shujuan" uniqKey="Du S" first="Shujuan" last="Du">Shujuan Du</name><affiliation><nlm:aff id="af1-biomedicines-06-00111"></nlm:aff></affiliation></author><author><name sortKey="Liu, Xiaoqing" sort="Liu, Xiaoqing" uniqKey="Liu X" first="Xiaoqing" last="Liu">Xiaoqing Liu</name><affiliation><nlm:aff id="af1-biomedicines-06-00111"></nlm:aff></affiliation></author><author><name sortKey="Cai, Qiliang" sort="Cai, Qiliang" uniqKey="Cai Q" first="Qiliang" last="Cai">Qiliang Cai</name><affiliation><nlm:aff id="af1-biomedicines-06-00111"></nlm:aff></affiliation></author></analytic><series><title level="j">Biomedicines</title><idno type="eISSN">2227-9059</idno><imprint><date when="2018">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Cellular RNA decay machinery plays a vital role in regulating gene expression by altering the stability of mRNAs in response to external stresses, including viral infection. In the primary infection, viruses often conquer the host cell’s antiviral immune response by controlling the inherently cellular mRNA degradation machinery to facilitate viral gene expression and establish a successful infection. This review summarizes the current knowledge about the diverse strategies of viral-mediated regulatory RNA shutoff for pathogenesis, and particularly sheds a light on the mechanisms that viruses evolve to elude immune surveillance during infection.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Tamarkin Ben Harush, A" uniqKey="Tamarkin Ben Harush A">A. Tamarkin-Ben-Harush</name></author><author><name sortKey="Vasseur, J J" uniqKey="Vasseur J">J.J. Vasseur</name></author><author><name sortKey="Debart, F" uniqKey="Debart F">F. Debart</name></author><author><name sortKey="Ulitsky, I" uniqKey="Ulitsky I">I. Ulitsky</name></author><author><name sortKey="Dikstein, R" uniqKey="Dikstein R">R. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Biomedicines</journal-id><journal-id journal-id-type="iso-abbrev">Biomedicines</journal-id><journal-id journal-id-type="publisher-id">biomedicines</journal-id><journal-title-group><journal-title>Biomedicines</journal-title></journal-title-group><issn pub-type="epub">2227-9059</issn><publisher><publisher-name>MDPI</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">30501096</article-id><article-id pub-id-type="pmc">6315618</article-id><article-id pub-id-type="doi">10.3390/biomedicines6040111</article-id><article-id pub-id-type="publisher-id">biomedicines-06-00111</article-id><article-categories><subj-group subj-group-type="heading"><subject>Review</subject></subj-group></article-categories><title-group><article-title>Viral-Mediated mRNA Degradation for Pathogenesis</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Du</surname><given-names>Shujuan</given-names></name><xref ref-type="aff" rid="af1-biomedicines-06-00111">1</xref><xref ref-type="author-notes" rid="fn1-biomedicines-06-00111">†</xref></contrib><contrib contrib-type="author"><name><surname>Liu</surname><given-names>Xiaoqing</given-names></name><xref ref-type="aff" rid="af1-biomedicines-06-00111">1</xref><xref ref-type="author-notes" rid="fn1-biomedicines-06-00111">†</xref></contrib><contrib contrib-type="author"><name><surname>Cai</surname><given-names>Qiliang</given-names></name><xref ref-type="aff" rid="af1-biomedicines-06-00111">1</xref><xref rid="c1-biomedicines-06-00111" ref-type="corresp">*</xref></contrib></contrib-group><aff id="af1-biomedicines-06-00111">MOE& MOH Key Laboratory of Medical Molecular Virology, School of Basic Medicine, Shanghai Medical College, Fudan University, Shanghai 200032, China;<email>17111010060@fudan.edu.cn</email> (S.D.);<email>17211010045@fudan.edu.cn</email> (X.L.)</aff><author-notes><corresp id="c1-biomedicines-06-00111"><label>*</label>Correspondence: <email>qiliang@fudan.edu.cn</email></corresp><fn id="fn1-biomedicines-06-00111"><label>†</label><p>Equally contributed to this work.</p></fn></author-notes><pub-date pub-type="epub"><day>29</day><month>11</month><year>2018</year></pub-date><pub-date pub-type="collection"><month>12</month><year>2018</year></pub-date><volume>6</volume><issue>4</issue><elocation-id>111</elocation-id><history><date date-type="received"><day>01</day><month>11</month><year>2018</year></date><date date-type="accepted"><day>29</day><month>11</month><year>2018</year></date></history><permissions><copyright-statement>© 2018 by the authors.</copyright-statement><copyright-year>2018</copyright-year><license license-type="open-access"><license-p>Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/4.0/">http://creativecommons.org/licenses/by/4.0/</ext-link>).</license-p></license></permissions><abstract><p>Cellular RNA decay machinery plays a vital role in regulating gene expression by altering the stability of mRNAs in response to external stresses, including viral infection. In the primary infection, viruses often conquer the host cell’s antiviral immune response by controlling the inherently cellular mRNA degradation machinery to facilitate viral gene expression and establish a successful infection. This review summarizes the current knowledge about the diverse strategies of viral-mediated regulatory RNA shutoff for pathogenesis, and particularly sheds a light on the mechanisms that viruses evolve to elude immune surveillance during infection.</p></abstract><kwd-group><kwd>mRNA degradation</kwd><kwd>viral pathogenesis</kwd></kwd-group></article-meta></front><body><sec id="sec1-biomedicines-06-00111"><title>1. Introduction</title><p>Many human diseases, including cancer, are related to the imbalance of gene expression. mRNA degradation plays a key role in the regulation of gene expression by counterbalancing the effects of transcription. The cellular RNA decay machinery, including the mRNA deadenylation, decapping, and mRNA quality control (QC) pathways, controls the fate of RNA transcripts. Cellular RNA decay machinery plays a vital role in regulating gene expression by altering the stability of mRNAs in response to external stresses, including viral infection. In the primary infection, viruses completely rely on the host cell translation machinery, and use a variety of mechanisms (including inhibiting cap-dependent translation, transcription, and promoting host mRNA degradation) to dampen host gene expressions that are essential for viral replication. To date, it has been demonstrated that viruses have evolved several strategies to utilize cellular mRNA degradation for pathogenesis including immune evasion during viral infections.</p></sec><sec id="sec2-biomedicines-06-00111"><title>2. Cellular mRNA Degradation Pathways</title><p>mRNA decay plays a vital role in transcriptional regulation. Eukaryotic mRNAs typically possess a cap at the 5′ end, 5′-UTR, CDS, and 3′-UTR, and a poly(A) tail at the 3′ end (<xref ref-type="fig" rid="biomedicines-06-00111-f001">Figure 1</xref>A). Conventional cap-dependent translation of most cellular mRNA commences with the recognition of the 7-methylguanosine cap by the eukaryotic initiation factor (eIF) 4E and the poly(A)-binding protein C1 (PABPC1) at the 3′ poly(A) tail [<xref rid="B1-biomedicines-06-00111" ref-type="bibr">1</xref>]. The N terminus of eIF4G binds to poly(A)-binding protein (PABP), and the central region recruits mRNA through eIF3 binding to the 40S ribosome subunit [<xref rid="B2-biomedicines-06-00111" ref-type="bibr">2</xref>,<xref rid="B3-biomedicines-06-00111" ref-type="bibr">3</xref>]. The interaction between eIF4G and PABP contributes to the stabilization of mRNA by forming the closed-loop mRNA. Circularization of mRNA during translation protects mRNA from cellular decay enzymes. Thus, the 5′ 7-methylguanosine cap and the 3′ poly(A) tail serve as a ‘guardian’ by protecting mRNA from the action of exoribonucleases, and also serve to recruit translation initiation machinery (<xref ref-type="fig" rid="biomedicines-06-00111-f001">Figure 1</xref>B).</p><p>Shortening and removal of the 3′ poly(A) tail of mature mRNA is the first and rate-limiting step in mRNA degradation, which is mediated by poly(A)-specific 3′ exonucleases (deadenylases). The majority of the chemokine receptor 4 (CCR4)-NOT and PAN2-PAN3 complexes play a major role in cytoplasmic deadenylase activity [<xref rid="B4-biomedicines-06-00111" ref-type="bibr">4</xref>]. Both the PAN2-PAN3 and CCR4-NOT complexes can interact with PABPC1 and be recruited to cytoplasmic mRNA for promoting mRNA deadenylation. The PAN2/3 complex removes long poly(A) tails of above 150 nt to initiate deadenylation [<xref rid="B5-biomedicines-06-00111" ref-type="bibr">5</xref>]. The CCR4-NOT complex is a generic deadenylase, and its two catalytic subunits have distinct activities regarding PABPC: CAF1 trims PABPC-free A tails, while CCR4 removes PABPC-bound A tails. PABPC coordinates mRNA deadenylation and decay in a timely order by promoting deadenylation and blocking precocious decay [<xref rid="B5-biomedicines-06-00111" ref-type="bibr">5</xref>] (<xref ref-type="fig" rid="biomedicines-06-00111-f001">Figure 1</xref>C). Following deadenylation, the removal of the 5′ 7-methylguanosine cap by the decapping complex DCP1/2 and its activators is triggered by the binding of the Lsm1–7 complex to the oligoadenylated 3′ end [<xref rid="B6-biomedicines-06-00111" ref-type="bibr">6</xref>,<xref rid="B7-biomedicines-06-00111" ref-type="bibr">7</xref>,<xref rid="B8-biomedicines-06-00111" ref-type="bibr">8</xref>,<xref rid="B9-biomedicines-06-00111" ref-type="bibr">9</xref>,<xref rid="B10-biomedicines-06-00111" ref-type="bibr">10</xref>] (<xref ref-type="fig" rid="biomedicines-06-00111-f001">Figure 1</xref>D). After decapping, the mRNA body is degraded by the 5′ monophosphate-dependent 5′-3′ exoribonuclease 1 (Xrn1) and the 3′-5′ exoribonucleases (the exosome complex and Dis3L2) [<xref rid="B11-biomedicines-06-00111" ref-type="bibr">11</xref>] (<xref ref-type="fig" rid="biomedicines-06-00111-f001">Figure 1</xref>D).</p><p>In addition to exonucleolytic decay, an mRNA can be internally cleaved in an endonucleolytic decay manner, which is a result of the mRNA QC pathway, including nonsense-mediated decay (NMD). NMD is an efficient mRNA surveillance process that selectively eliminates aberrant transcripts which harboring premature termination codons (PTCs). NMD-targeted transcripts are thought to be primarily degraded via removal of the 5′ 7-methyl guanosine cap by the decapping enzymes DCP1/2 and the subsequent 5′-3′ exonuclease activity of Xrn1 [<xref rid="B12-biomedicines-06-00111" ref-type="bibr">12</xref>]. To date, it has been demonstrated that the NMD pathway is repressed by a variety of stress conditions, such as hypoxia, nutrient deprivation, or viral infection [<xref rid="B13-biomedicines-06-00111" ref-type="bibr">13</xref>,<xref rid="B14-biomedicines-06-00111" ref-type="bibr">14</xref>].</p><p>It is thought that RNA degradation occurs within cytoplasmic RNA granules known as processing bodies (P bodies, PBs). P bodies have been shown to contain several mRNA decay enzymes, including the DCP1/2 complex, XRN1, the Lsm1–7 complex, PAN2-PAN3, the CCR4-NOT complex, Rck/p54 (DDX6), and NUDT16, along with the P-body component GW182. Strikingly, exosome and the SKI complex proteins, involved in the 3′-5′ decay pathway, have not been observed in P bodies. P bodies are dynamic foci where protein and mRNA components are readily exchanged between the stress granules and the cytosol.</p><p>Stress granules (SGs) are dynamic and non-membrane-bound cytoplasmic compartments that arrest cytoplasmic mRNA, protein translation factors, and RNA binding proteins. SGs play a main role in regulation of mRNA translation. SGs contain stalled pre-initiation complexes (PICs), T-cell-restricted intracellular antigen 1 (TIA-1), and the two aggregation-prone RasGAP SH3-domain binding protein 1 (G3BP) and RNA-binding proteins (RBPs). It is known that cycloheximide (CHX) can bind mRNAs on polysomes and inhibit SG formation [<xref rid="B15-biomedicines-06-00111" ref-type="bibr">15</xref>]. SGs assemble or disassemble rapidly, which depends on whether stress is appeared or alleviated.</p></sec><sec id="sec3-biomedicines-06-00111"><title>3. Viruses Indirectly Destabilize Cellular mRNAs via Different Targets</title><p>It has been demonstrated that many cellular stresses exist including viral infection could cause different deregulation of cellular mRNA. Virus infection usually imposes stress on host cells, and hijacks the host translation machinery to ensure virus translation and production [<xref rid="B16-biomedicines-06-00111" ref-type="bibr">16</xref>]. In order to establish a successful viral infection, different viruses have evolved mechanisms to disrupt the cellular decay machinery by inactivating the enzymes and co-factors, which are involved in both the constitutive and viral-induced mRNA surveillance and degradation pathways.</p><p>SGs and PBs, as important structures for regulating cellular mRNA stability and translatability, have also been demonstrated to be inhibited by many viruses for viral survival (<xref ref-type="fig" rid="biomedicines-06-00111-f002">Figure 2</xref>). For examples, flaviviruses, such as West Nile virus (WNV) and dengue virus (DV), can inhibit SG formation through inducing relocalization and interaction of the cellular SG components. Although WNV infection results in a reduction in the number of P bodies, the mechanism of interference with P body assembly remains unclear [<xref rid="B13-biomedicines-06-00111" ref-type="bibr">13</xref>]. The genomic RNA of dengue virus could interact with the P body component Rck/p54 (DDX6), and is presumed to be important for viral replication. Similarly, infection with hepatitis C virus (HCV) leads to a progressive reduction in the number of P body foci and relocalization of P body components to viral replication centers [<xref rid="B17-biomedicines-06-00111" ref-type="bibr">17</xref>]. Picornavirus infection can also interfere with the formation of SGs. EV71-encoded 2A protease can block tSG (typical) formation but induce aSG (atypical) formation to facilitate viral translation. These aSGs are induced by cleavage of eIF4GI and are different from tSGs as they are devoid of G3BP and a series of eIFs. The aSGs are independent of eIF2α and PKR phosphorylation, and although they cannot be dissolved by CHX, it can specifically sequester cellular mRNAs instead of viral mRNAs [<xref rid="B15-biomedicines-06-00111" ref-type="bibr">15</xref>]. Newcastle disease virus induces formation of bona fide in SGs to facilitate viral replication through manipulating host protein translation by activating the protein kinase R (PKR)/eIF2a pathway [<xref rid="B18-biomedicines-06-00111" ref-type="bibr">18</xref>]. In addition, influenza A virus (IAV) can deploy viral nonstructural protein 1 to inhibit activation of PKR kinase and eIF2α phosphorylation, in turn blocking SG formation [<xref rid="B19-biomedicines-06-00111" ref-type="bibr">19</xref>]. Semliki Forest virus (SFV) nsP3 combines its viral replication complex with host G3BP, resulting in suppression of SG formation on viral RNAs and efficient viral mRNA translation [<xref rid="B20-biomedicines-06-00111" ref-type="bibr">20</xref>]. Poliovirus could prevent the assembly of SGs through the 3C-proteinase-mediated cleavage of G3BP.</p><p>In contrast to SGs, the studies on PBs in viral infection have been less comprehensive (<xref ref-type="fig" rid="biomedicines-06-00111-f002">Figure 2</xref>). Poliovirus infection leads to the loss of P bodies and the cleavage or degradation of several key proteins that are critical for cellular RNA decay, such as the P-body proteins DCP1a and PAN3. Degradation of these proteins can protect poliovirus from Xrn1-mediated antiviral response [<xref rid="B21-biomedicines-06-00111" ref-type="bibr">21</xref>]. During poliovirus infection, cleavages of both eIF4GII and PABP have been proposed to contribute to host translation shutoff [<xref rid="B22-biomedicines-06-00111" ref-type="bibr">22</xref>,<xref rid="B23-biomedicines-06-00111" ref-type="bibr">23</xref>].</p><p>The mosquito-transmitted bunyavirus Rift Valley fever virus (RVFV) encodes nucleocapsid protein (N) to associate with P bodies for gaining access to host ribosomes by “cap-snatching” the 5′ ends of host mRNAs, while another bunyavirus, Sin Nombre virus, directly localizes to P bodies in human cells [<xref rid="B24-biomedicines-06-00111" ref-type="bibr">24</xref>]. RVFV infection triggers the RNA decapping enzyme NUDT16 and selectively degrades 5′-TOP mRNAs. The increased RNA decay results in the loss of visible P bodies and stress granules. Because RVFV cap-snatches in RNA granules, the increased level of 5′-TOP mRNAs in this compartment leads to snatching of these targets, which are translationally suppressed during infection. Therefore, RVFV-induced translational arrest via decay of 5′-TOP mRNAs restricts viral infection [<xref rid="B25-biomedicines-06-00111" ref-type="bibr">25</xref>].</p><p>Respiratory syncytialvirus (RSV) infection affects the expression patterns of cellular proteins by regulating mRNA translation and degradation. Following RSV infection, DCP1a is phosphorylated rapidly and this phosphorylation may modulate the expression of host chemokines in response to RSV infection [<xref rid="B26-biomedicines-06-00111" ref-type="bibr">26</xref>]. DCP1 interacts with Ge-1 of Drosophila melanogastersigma virus (DMelSV) and commits mRNA for degradation by removing the 5′ cap. This RNA degradation pathway could help host cell against DMelSV infection [<xref rid="B27-biomedicines-06-00111" ref-type="bibr">27</xref>]. In contrast, calicivirus 3C-like proteinase inhibits cellular translation by cleavage of PABP [<xref rid="B23-biomedicines-06-00111" ref-type="bibr">23</xref>].</p><p>For herpesviruses, as shown in the <xref rid="biomedicines-06-00111-t001" ref-type="table">Table 1</xref>, Kaposi’s sarcoma-associated herpesvirus (KSHV) inhibits SG formation by encoding a viral ORF57 protein to block PKR activation, and thus enhances virion production during lytic replication [<xref rid="B28-biomedicines-06-00111" ref-type="bibr">28</xref>]. Distinct from KSHV, Epstein–Barr virus (EBV) protein EB2 stimulates translation initiation of mRNAs through directly interacting with both PABP and eIF4G [<xref rid="B29-biomedicines-06-00111" ref-type="bibr">29</xref>]. Human cytomegalovirus (HCMV) encodes a noncoding RNA named as miRDE to induce the host miRNA turnover via sequence-specific noncanonical miRNA-mRNA interactions, and accelerates virus production [<xref rid="B30-biomedicines-06-00111" ref-type="bibr">30</xref>]. In contrast, the human T- lymphotropic virus type 1 (HTLV-1) encodes the Tax protein to interact with both the core NMD effector UPF1 and eIF3E (a subunit of the translation initiation factor) to impair the accumulation of phosphorylated UPF1-Tax complexes in P bodies. Disruption of UPF1-INT6 association and prevention of UPF1 recycling can lead to inhibition of the NMD pathway in HTLV-1-infected cells [<xref rid="B31-biomedicines-06-00111" ref-type="bibr">31</xref>].</p><p>In addition, many viruses have also evolved to counteract the interferon-induced RNase L pathway. The interferon-induced RNase L pathway is an innate immunity pathway and often is triggered by dsRNAs upon viral infection, which leads to apoptosis of the infected cells [<xref rid="B32-biomedicines-06-00111" ref-type="bibr">32</xref>]. The 2′, 5′-oligoadenylate synthetase enzyme (OAS) is a upstream protein that generates the RNase L activator, 2′,5′-oligoadenylate (2-5A) from ATP. In order to overcome the degradation by cellular RNase L, many viruses encode viral dsRNA-binding proteins to inhibit the activation of OAS, such as vaccinia virus protein E3L, influenza virus NS1, HCMV proteins TRS1 and IRS1, and HSV1-encoded Us11 [<xref rid="B32-biomedicines-06-00111" ref-type="bibr">32</xref>,<xref rid="B33-biomedicines-06-00111" ref-type="bibr">33</xref>,<xref rid="B34-biomedicines-06-00111" ref-type="bibr">34</xref>].</p></sec><sec id="sec4-biomedicines-06-00111"><title>4. The Viral Proteins Directly Commandeer Cellular mRNA Turnover Pathways to Destroy Host mRNAs</title><p>Viruses have evolved different abilities to exploit the cellular mRNA decay machinery to modulate host gene expression. The description below will address the subversion mechanisms about how viruses promote host mRNA turnover (<xref rid="biomedicines-06-00111-t002" ref-type="table">Table 2</xref>).</p><sec id="sec4dot1-biomedicines-06-00111"><title>4.1. Viral Endonucleases Mediate RNA Degradation</title><p>Host shutoff is a process that virus inhibits innate immune responses and simultaneously provides preferential access for viral mRNAs to the cellular translation machinery. It has been shown that host shutoff is usually caused by viral endonucleases. For examples, influenza A virus PA-X, SARS coronavirus nsp1, or HSV-1 virion host shutoff (vhs) protein can efficiently induce endonucleolytic cleavage of the host RNA, following by RNA degradation induced by host enzymes [<xref rid="B43-biomedicines-06-00111" ref-type="bibr">43</xref>].</p><p>In influenza A virus (IAV), the viral protein PA-X is an mRNA endonuclease that can restrict host gene expression through cap snatching in the nucleus [<xref rid="B41-biomedicines-06-00111" ref-type="bibr">41</xref>,<xref rid="B44-biomedicines-06-00111" ref-type="bibr">44</xref>]. It is generated by a ribosome frameshifting event during translation of the PA subunit of the viral RNA-dependent RNA polymerase (RdRp) [<xref rid="B41-biomedicines-06-00111" ref-type="bibr">41</xref>,<xref rid="B44-biomedicines-06-00111" ref-type="bibr">44</xref>,<xref rid="B45-biomedicines-06-00111" ref-type="bibr">45</xref>]. PA-X can selectively target host RNA polymerase II (Pol II)-transcribed mRNAs or RNAs within the nucleus. Once activation of PA-X-mediated endonucleolytic cleavage, the complete degradation of host mRNAs is induced, which relies on the host 5′->3′-exonuclease Xrn1. Therefore, the distinct biogenesis mechanism through which IAV PA-X hijacks cellular RNA biogenesis processes for direct degradation of host RNAs provides a convenient way to discriminate host and viral products [<xref rid="B45-biomedicines-06-00111" ref-type="bibr">45</xref>]. In contrast, nsp1 encoded by SARS corona virus is a potent inhibitor of host gene expression, which not only inactivates viral translation functions, but also induces host mRNA degradation by means of binding to 40S ribosomes [<xref rid="B42-biomedicines-06-00111" ref-type="bibr">42</xref>].</p><p>In human herpesviruses, it is known that α-herpesvirus including HSV-1 contain a conserved virally UL41 gene that encodes a ribonuclease called the vhs. The vhs protein is directed to mRNAs through interaction with the cellular cap-binding complex eIF4F [<xref rid="B35-biomedicines-06-00111" ref-type="bibr">35</xref>]. vhs possesses a potent mRNA-specific endonuclease activity that promotes endonucleolytic cleavage of viral and host mRNAs, instead of the host rRNA and tRNA [<xref rid="B46-biomedicines-06-00111" ref-type="bibr">46</xref>,<xref rid="B47-biomedicines-06-00111" ref-type="bibr">47</xref>]. Therefore, vhs triggers the accelerated decay of cellular mRNAs, and also destabilizes viral mRNAs. Although viral and host mRNAs are rapidly degraded, viral mRNA is transcribed at a higher rate than cellular mRNA, thus, viral mRNAs and viral proteins are not dramatically impaired by vhs protein. Similarly, PABP is partially relocated to the nucleus during HSV-1 infection, without impairing virus replication [<xref rid="B48-biomedicines-06-00111" ref-type="bibr">48</xref>], the redistribution of PABP may be involved in post-transcriptional regulation of mRNA processing and/or nuclear export [<xref rid="B49-biomedicines-06-00111" ref-type="bibr">49</xref>]. In contrast, although the pUL89 protein encoded by HCMV has been demonstrated as a large terminase subunit with endonucleolytic activity for genome cleavage during genome packaging and particle assembly, whether pUL89 is involved in host mRNA turnover remains obscure [<xref rid="B30-biomedicines-06-00111" ref-type="bibr">30</xref>].</p></sec><sec id="sec4dot2-biomedicines-06-00111"><title>4.2. Viral Exonucleases Mediate RNA Degradation</title><p>To induce global degradation of cellular mRNAs, it has been demonstrated that gamma-herpesviruses also encode a conserved viral alkaline exonuclease, such as SOX in KSHV, muSOX in murine gammaherpesvirus 68 (MHV68), and BGLF5 in EBV, to induce host shutoff. The KSHV protein SOX is encoded by ORF37 and is able to strongly cause a widespread shutoff of cellular gene expression through enhancing global mRNA turnover [<xref rid="B50-biomedicines-06-00111" ref-type="bibr">50</xref>]. The SOX-induced mRNA turnover is firstly initiated by SOX, and then degraded by exonuclease Xrn1 [<xref rid="B51-biomedicines-06-00111" ref-type="bibr">51</xref>]. The SOX bound to the KSHV pre-miRNA stem loop fragment K2-31 and SOX-mediated turnover are independent of recognition of a particular consensus sequence [<xref rid="B36-biomedicines-06-00111" ref-type="bibr">36</xref>]. Moreover, SOX stimulates host mRNA destruction via a unique mechanism involving polyadenylation [<xref rid="B37-biomedicines-06-00111" ref-type="bibr">37</xref>]. PABPC facilitates mRNA deadenylation while preventing precocious uridylation and decay. Under steady-state conditions, PABP associates with both eIF4G and the poly(A) tail of mRNAs in the cytoplasm, thereby inducing the circularization of mRNAs. This facilitates translation initiation and hampers mRNA degradation [<xref rid="B52-biomedicines-06-00111" ref-type="bibr">52</xref>]. Expression of KSHV SOX and subsequent mRNA degradation lead to the nuclear accumulation of PABP [<xref rid="B37-biomedicines-06-00111" ref-type="bibr">37</xref>]. The nuclear retention of RNA transcripts could be due to a nuclear mRNA export block.</p><p>Because EBV-encoded DNase BGLF5 displays 40% homology to KSHV SOX at the amino acid level, EBV BGLF5 can also induce a robust and generalized host shutoff in productively infected cells [<xref rid="B53-biomedicines-06-00111" ref-type="bibr">53</xref>]. BGLF5 can degrade mRNAs of both cellular and viral origin, irrespective of polyadenylation [<xref rid="B54-biomedicines-06-00111" ref-type="bibr">54</xref>]. Similarly, EBV BGLF5 could also induce the nuclear relocation of PABP. Within the nucleus compartment, PABPC causes hyperadenylation and retention of nuclear mRNA molecules, thereby augmenting the shutoff phenotype initiated by BGLF5 [<xref rid="B37-biomedicines-06-00111" ref-type="bibr">37</xref>]. In contrast, MHV68-encoded muSOX also induces both cellular and viral mRNA degradation upon productive infection [<xref rid="B38-biomedicines-06-00111" ref-type="bibr">38</xref>]. However, the association between muSOX and PABP remains unknown.</p></sec><sec id="sec4dot3-biomedicines-06-00111"><title>4.3. Viral Decapping Enzymes Mediates RNA Degradation</title><p>In order to inhibit the host antiviral responses, it has been shown that some poxviruses, such as vaccinia virus (VACV), can encode a Nudix hydrolase motif-containing mRNA decapping enzymes D9 and D10, to remove protective caps from mRNA 5-termini by preventing dsRNA accumulation and shutdown of host protein synthesis [<xref rid="B55-biomedicines-06-00111" ref-type="bibr">55</xref>]. The D9- or D10-deficient VACV are effective oncolytic viruses, and their VACV mutants unable to execute a fundamental step in virus-induced mRNA decay [<xref rid="B40-biomedicines-06-00111" ref-type="bibr">40</xref>]. Similarly, African Swine Fever Virus (ASFV) also contains a gene (D250R in strain Ba71V and g5R in strain Malawi) to encode a decapping protein (ASFV-DP) that has a Nudix hydrolase motif and decapping activity in vitro [<xref rid="B39-biomedicines-06-00111" ref-type="bibr">39</xref>,<xref rid="B56-biomedicines-06-00111" ref-type="bibr">56</xref>]. Interestingly, g5R binds to the RNA body rather than the cap, whereas VACV D10 binds both the methylated cap and the RNA body. ASFV-DP was expressed from early times and accumulated throughout the infection with a subcellular localization typically in the endoplasmic reticulum, and co-localizing with ribosomal protein L23a in the cap structure. Moreover, the N-terminal region of the ASFV-DP protein has been shown to interact with poly(A) RNA of both viral and cellular RNAs in the infected cells, which results in decreased transcripts levels [<xref rid="B39-biomedicines-06-00111" ref-type="bibr">39</xref>].</p></sec></sec><sec id="sec5-biomedicines-06-00111"><title>5. Cellular mRNA Degradation Contributes to Immune Evasion</title><p>To establish a successful infection, it is well known that RNA viruses must contend with the antiviral response. Many viruses have evolved variety of strategies. These include directly preventing the synthesis of antiviral associated proteins or forming special structures with cellular RNA binding proteins or enzymes that can impede the function of RNA degradation, to disrupt and inhibit the decay machinery or redirect decay machinery. How viruses take advantage of host shutoff pathways to evade antiviral immunity has also been broadly investigated. For examples, EBV BGLF5 can reduce expression of HLA class I and II molecules, thereby hampering antigen presentation to T cells [<xref rid="B54-biomedicines-06-00111" ref-type="bibr">54</xref>,<xref rid="B57-biomedicines-06-00111" ref-type="bibr">57</xref>]. Meanwhile, BGLF5-mediated shutoff can reduce expression of the innate EBV-sensing Toll-like receptor-2 and the lipid antigen-presenting cluster of differentiation 1 <monospace>(</monospace>CD1d) [<xref rid="B58-biomedicines-06-00111" ref-type="bibr">58</xref>]. In contrast, HSV-1 vhs-mediated shutoff of host protein synthesis occurs mainly in the immediate-early and early phases of lytic infection. In this phase, vhs reduces synthesis of proteins involved in the innate and adaptive immune responses, including dampen the type I interferon (IFN) system. This helps HSV-1 resist eradication by the immune system. Recent studies showed that vhs also targets the Cyclic GMP-AMP (cGAMP) synthase cGAS/STING-mediated cellular DNA-sensing pathway by selectively degrading cGAS mRNA [<xref rid="B59-biomedicines-06-00111" ref-type="bibr">59</xref>]. This suggests that HSV-1 not only can evade immune evasion but also block the cytosolic DNA sensing and signaling.</p><p>In addition, viruses have also developed different ways to repress or avoid deadenylation which is often the key step in mRNA decay. Many RNA viruses have evolved 3′ terminal stem loop structures to maintain the stability of the transcript and the translational ability [<xref rid="B60-biomedicines-06-00111" ref-type="bibr">60</xref>]. For examples, SCoV mRNAs, which have a 5′ cap structure and 3′ poly A tail like those of typical host mRNAs, are not susceptible tonsp1-mediated RNA cleavage, while the presence of the 5′-end leader sequence could protect the SCoV mRNAs fromnsp1-induced endonucleolytic RNA cleavage. In contrast, some positive-sense single-stranded RNA viruses, such as Sindbis virus (SINV) and Venezuelan equine encephalitis virus (VEEV) whose genomic RNAs are both capped and polyadenylated and resembling cellular mRNAs, have evolved sequences that can stall deadenylation [<xref rid="B61-biomedicines-06-00111" ref-type="bibr">61</xref>]. After deadenylation, the process of RNA degradation is completed through the 5′-3′ or 3′-5′ decay pathway. Different RNA viruses have evolved different or similar strategies to avoid the mRNA decay pathways. For instances, Poliovirus contains an RNA element to interact with and inactivate the RNase L endonuclease [<xref rid="B62-biomedicines-06-00111" ref-type="bibr">62</xref>]. A pseudoknot structure stalling the XRN1 enzyme is presented at the 5′ border of the 3′ UTR of insect-borne flaviviruses [<xref rid="B63-biomedicines-06-00111" ref-type="bibr">63</xref>]. Rous sarcoma virus also contains an RNA element that insulates unspliced viral mRNAs from the nonsense-mediated decay pathway [<xref rid="B64-biomedicines-06-00111" ref-type="bibr">64</xref>]. Moreover, it has been demonstrated that the rate of decay of specific mRNAs can be controlled by using RNA structures. For example, a thermostable RNA secondary structure at the 5′ or 3′ end of RNA could slow down the degradation machinery. Further investigation revealed that some RNA forms could fold subtle three-dimensional conformations to confound or evade the decay machinery [<xref rid="B65-biomedicines-06-00111" ref-type="bibr">65</xref>]. Interestingly, in order to protect themselves from host immune detecting, some negative-sense RNA viruses may steal stability factors from host mRNAs to incorporate into their own transcripts. For example, rabies virus steals host poly(C) binding protein 2 (PCBP2) to regulate expression of its glycoprotein to avoid host immune detection as it replicates and migrates to the central nervous system during infection [<xref rid="B66-biomedicines-06-00111" ref-type="bibr">66</xref>]. Taken together, this evidence indicates that viruses have evolved a number of strategies to avoid or inactivate the cellular mRNA decay pathways and direct an optimum cellular environment for their own replication.</p></sec><sec id="sec6-biomedicines-06-00111"><title>6. Conclusions</title><p>In summary, mRNA decay is important for regulation of cellular gene expression. In order to facilitate viral replication, the virus exploits multiple strategies to corrupt host shutoff through RNA degradation or altering cellular RNA metabolism. mRNA released from disassembled polysomes is sorted and remodeled at SGs; the accumulation of mRNA at SGs may be a consequence of both stress-induced translational arrest and virus-induced host shutoff, from which selected transcripts are delivered to PBs for degradation. Blocking protein synthesis could benefit virus infection. In the absence of host protein synthesis, cellular ribosomes will be committed to the synthesis of viral proteins. Taking advantage of this point, the virus can progress efficiently between the different phases of productive infection by controlling the transition between immediate early, early, and late protein synthesis. Given the essential role of mRNA decay in antiviral defense, host shutoff contributes to immune evasion by preventing the synthesis of proteins involved in antiviral immunity. To fight with the host cell’s antiviral immune response, viruses have evolved multiple strategies including encoding the viral counterpart of endonucleases, exonucleases, and decapping enzymes that can directly commandeer cellular mRNA turnover pathways to destroy host mRNAs, which will facilitate viral gene expression and eventually establish a successful infection.</p></sec></body><back><ack><title>Acknowledgments</title><p>The authors would like to apologize to the many researchers who have contributed to this area of research but have not been cited in this review due to space limitations.</p></ack><notes><title>Author Contributions</title><p>Conceptualization, S.D. and X.L.; Methodology, S.D. and X.L.; Formal Analysis, S.D. and X.L.; Investigation, S.D. and X.L.; Writing-Original Draft Preparation, S.D. and X.L.; Writing-Review and Editing, Q.C.; Supervision, Q.C.; Project Administration, Q.C.; Funding Acquisition, Q.C.</p></notes><notes><title>Funding</title><p>This research was funded by the National Natural Science Foundation of China grant number 81471930, 81672015, and National Key Research and Development Program of China grant number 2016YFC1200400.</p></notes><notes notes-type="COI-statement"><title>Conflicts of Interest</title><p>The authors declare no conflict of interest. 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(<bold>A</bold>) Structure diagram of eukaryotic mRNAs; (<bold>B</bold>) conventional cap-dependent translation initiation of eukaryotic mRNA; (<bold>C</bold>) the degradation pathway of removal of the 3′ poly(A) tail of mature mRNA; (<bold>D</bold>) the decapping and degradation pathways of the mRNA body.</p></caption><graphic xlink:href="biomedicines-06-00111-g001"></graphic></fig><fig id="biomedicines-06-00111-f002" orientation="portrait" position="float"><label>Figure 2</label><caption><p>Schematics of viral-mediated regulation of mRNA degradation in stress granules and P bodies. Arrows indicate induction, T bars indicate repression.</p></caption><graphic xlink:href="biomedicines-06-00111-g002"></graphic></fig><table-wrap id="biomedicines-06-00111-t001" orientation="portrait" position="float"><object-id pub-id-type="pii">biomedicines-06-00111-t001_Table 1</object-id><label>Table 1</label><caption><p>Molecular mechanisms of viruses indirectly destabilize cellular mRNAs. KSHV: Kaposi’s sarcoma-associated herpesvirus; EBV: Epstein–Barr virus; HCMV: Human cytomegalovirus; RSV: respiratory syncytialvirus; DMelSV: Drosophila melanogastersigma virus; IAV: influenza A virus; SFV: Semliki Forest virus. HTLV-1: human T- lymphotropic virus type 1; RVFV: Rift Valley fever virus.</p></caption><table frame="hsides" rules="groups"><thead><tr><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Viruses</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Viral Antigen</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Host Shutoff Factor(s)</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Targeting Mechanisms</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Refenrence</th></tr></thead><tbody><tr><td colspan="5" align="center" valign="middle" style="border-bottom:solid thin" rowspan="1">DNA viruses</td></tr><tr><td align="center" valign="middle" rowspan="1" colspan="1">KSHV</td><td align="center" valign="middle" rowspan="1" colspan="1">viral ORF57</td><td align="center" valign="middle" rowspan="1" colspan="1">PKR</td><td align="center" valign="middle" rowspan="1" colspan="1">Inhibits stress granule formation</td><td align="center" valign="middle" rowspan="1" colspan="1">[<xref rid="B28-biomedicines-06-00111" ref-type="bibr">28</xref>]</td></tr><tr><td align="center" valign="middle" rowspan="1" colspan="1">EBV</td><td align="center" valign="middle" rowspan="1" colspan="1">EB2</td><td align="center" valign="middle" rowspan="1" colspan="1">PABP and eIF4G</td><td align="center" valign="middle" rowspan="1" colspan="1">EB2 directly interacts with both PABP and eIF4G</td><td align="center" valign="middle" rowspan="1" colspan="1">[<xref rid="B29-biomedicines-06-00111" ref-type="bibr">29</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">HCMV</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">miRDE in UL144-145 region</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">host miRNA</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">miRNA–mRNA interactions</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B30-biomedicines-06-00111" ref-type="bibr">30</xref>]</td></tr><tr><td colspan="5" align="center" valign="middle" style="border-bottom:solid thin" rowspan="1">RNA viruses</td></tr><tr><td align="center" valign="middle" rowspan="1" colspan="1">RVFV</td><td align="center" valign="middle" rowspan="1" colspan="1">viral nucleocapsid protein (N), viral polymerase (L) </td><td align="center" valign="middle" rowspan="1" colspan="1">P bodies </td><td align="center" valign="middle" rowspan="1" colspan="1">N “cap-snatching” the 5′ ends of host mRNAs, and L cleaved 10–18nt downstream of the 5′ cap. This capped oligomer is used for viral transcription. RVFV N associates with P bodies </td><td align="center" valign="middle" rowspan="1" colspan="1">[<xref rid="B24-biomedicines-06-00111" ref-type="bibr">24</xref>,<xref rid="B25-biomedicines-06-00111" ref-type="bibr">25</xref>]</td></tr><tr><td align="center" valign="middle" rowspan="1" colspan="1">DMelSV</td><td align="center" valign="middle" rowspan="1" colspan="1">Ge-1</td><td align="center" valign="middle" rowspan="1" colspan="1">DCP1</td><td align="center" valign="middle" rowspan="1" colspan="1">DCP1 interacts with Ge-1</td><td align="center" valign="middle" rowspan="1" colspan="1">[<xref rid="B27-biomedicines-06-00111" ref-type="bibr">27</xref>]</td></tr><tr><td align="center" valign="middle" rowspan="1" colspan="1">RSV</td><td align="center" valign="middle" rowspan="1" colspan="1"></td><td align="center" valign="middle" rowspan="1" colspan="1">DCP1 phosphorylation</td><td align="center" valign="middle" rowspan="1" colspan="1">Inhibits IL-8 expression</td><td align="center" valign="middle" rowspan="1" colspan="1">[<xref rid="B26-biomedicines-06-00111" ref-type="bibr">26</xref>]</td></tr><tr><td align="center" valign="middle" rowspan="1" colspan="1">IAV</td><td align="center" valign="middle" rowspan="1" colspan="1">nsP1</td><td align="center" valign="middle" rowspan="1" colspan="1">PKR</td><td align="center" valign="middle" rowspan="1" colspan="1">Blocking SG formation</td><td align="center" valign="middle" rowspan="1" colspan="1">[<xref rid="B19-biomedicines-06-00111" ref-type="bibr">19</xref>]</td></tr><tr><td align="center" valign="middle" rowspan="1" colspan="1">SFV</td><td align="center" valign="middle" rowspan="1" colspan="1">nsP3</td><td align="center" valign="middle" rowspan="1" colspan="1">Ras-GAP</td><td align="center" valign="middle" rowspan="1" colspan="1">Suppression of SG formation</td><td align="center" valign="middle" rowspan="1" colspan="1">[<xref rid="B20-biomedicines-06-00111" ref-type="bibr">20</xref>]</td></tr><tr><td align="center" valign="middle" rowspan="1" colspan="1">Poliovirus</td><td align="center" valign="middle" rowspan="1" colspan="1">3C-proteinase</td><td align="center" valign="middle" rowspan="1" colspan="1">G3BP, DCP1, PAN3</td><td align="center" valign="middle" rowspan="1" colspan="1">Prevent the assembly of SGs and disrupt PBs</td><td align="center" valign="middle" rowspan="1" colspan="1">[<xref rid="B21-biomedicines-06-00111" ref-type="bibr">21</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">HTLV-1</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Tax</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">UPF1, INT6/EIF3E</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Effect the accumulation of phosphorylated UPF1-Tax complexes in P bodies</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B31-biomedicines-06-00111" ref-type="bibr">31</xref>]</td></tr></tbody></table></table-wrap><table-wrap id="biomedicines-06-00111-t002" orientation="portrait" position="float"><object-id pub-id-type="pii">biomedicines-06-00111-t002_Table 2</object-id><label>Table 2</label><caption><p>Molecular mechanisms of viral enzymes directly destroy gene expression.</p></caption><table frame="hsides" rules="groups"><thead><tr><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Viruses</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Viral Protein</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Viral Gene</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Targeting Mechanisms</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Reference</th></tr></thead><tbody><tr><td colspan="5" align="center" valign="middle" style="border-bottom:solid thin" rowspan="1">DNA viruses</td></tr><tr><td align="center" valign="middle" rowspan="1" colspan="1">HSV1</td><td align="center" valign="middle" rowspan="1" colspan="1">Virion host shutoff protein (vhs)</td><td align="center" valign="middle" rowspan="1" colspan="1"><italic>UL41</italic></td><td align="center" valign="middle" rowspan="1" colspan="1">eIF4H and eIF4AI/II </td><td align="center" valign="middle" rowspan="1" colspan="1">[<xref rid="B35-biomedicines-06-00111" ref-type="bibr">35</xref>]</td></tr><tr><td align="center" valign="middle" rowspan="1" colspan="1">KSHV</td><td align="center" valign="middle" rowspan="1" colspan="1">SOX</td><td align="center" valign="middle" rowspan="1" colspan="1"><italic>ORF37</italic></td><td align="center" valign="middle" rowspan="1" colspan="1">KSHV pre-miRNA stem loop fragment K2-31</td><td align="center" valign="middle" rowspan="1" colspan="1">[<xref rid="B36-biomedicines-06-00111" ref-type="bibr">36</xref>]</td></tr><tr><td align="center" valign="middle" rowspan="1" colspan="1">EBV</td><td align="center" valign="middle" rowspan="1" colspan="1">BGLF5</td><td align="center" valign="middle" rowspan="1" colspan="1"><italic>BGLF5</italic></td><td align="center" valign="middle" rowspan="1" colspan="1">Nuclear relocalization of PABPC1</td><td align="center" valign="middle" rowspan="1" colspan="1">[<xref rid="B37-biomedicines-06-00111" ref-type="bibr">37</xref>]</td></tr><tr><td align="center" valign="middle" rowspan="1" colspan="1">HCMV</td><td align="center" valign="middle" rowspan="1" colspan="1">pUL89</td><td align="center" valign="middle" rowspan="1" colspan="1"><italic>UL89</italic></td><td align="center" valign="middle" rowspan="1" colspan="1">the endonucleolytic activity for virus genome cleavage.</td><td align="center" valign="middle" rowspan="1" colspan="1">[<xref rid="B30-biomedicines-06-00111" ref-type="bibr">30</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">MHV68</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">muSOX</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1"><italic>ORF37</italic></td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Unknown</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B38-biomedicines-06-00111" ref-type="bibr">38</xref>]</td></tr><tr><td colspan="5" align="center" valign="middle" style="border-bottom:solid thin" rowspan="1">RNA viruses</td></tr><tr><td align="center" valign="middle" rowspan="1" colspan="1">ASFV</td><td align="center" valign="middle" rowspan="1" colspan="1">ASFV-DP</td><td align="center" valign="middle" rowspan="1" colspan="1"><italic>Ba71V D250R/Malawi g5R</italic></td><td align="center" valign="middle" rowspan="1" colspan="1">poly(A) RNA RPL23a</td><td align="center" valign="middle" rowspan="1" colspan="1">[<xref rid="B39-biomedicines-06-00111" ref-type="bibr">39</xref>]</td></tr><tr><td align="center" valign="middle" rowspan="1" colspan="1">VACV</td><td align="center" valign="middle" rowspan="1" colspan="1">decapping enzymes</td><td align="center" valign="middle" rowspan="1" colspan="1"><italic>D9</italic>, <italic>D10</italic></td><td align="center" valign="middle" rowspan="1" colspan="1">Cap-binding</td><td align="center" valign="middle" rowspan="1" colspan="1">[<xref rid="B40-biomedicines-06-00111" ref-type="bibr">40</xref>]</td></tr><tr><td align="center" valign="middle" rowspan="1" colspan="1">IAV</td><td align="center" valign="middle" rowspan="1" colspan="1">PA-X</td><td align="center" valign="middle" rowspan="1" colspan="1"><italic>PA</italic></td><td align="center" valign="middle" rowspan="1" colspan="1">selectively targets host RNA polymerase II (Pol II) transcribed mRNAs and non-coding RNAs</td><td align="center" valign="middle" rowspan="1" colspan="1">[<xref rid="B41-biomedicines-06-00111" ref-type="bibr">41</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">SARS</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">nsP1</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1"><italic>ORF1AB</italic></td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">binding to 40S ribosomes, inactivate the translation functions</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B42-biomedicines-06-00111" ref-type="bibr">42</xref>]</td></tr></tbody></table></table-wrap></floats-group></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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