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Published in: Virology Journal 1/2017

Open Access 01-12-2017 | Research

Herpes simplex virus 1 infection dampens the immediate early antiviral innate immunity signaling from peroxisomes by tegument protein VP16

Authors: Chunfu Zheng, Chenhe Su

Published in: Virology Journal | Issue 1/2017

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Abstract

Background

Herpes simplex virus 1 (HSV-1) is an archetypal member of the alphaherpesvirus subfamily with a large genome encoding over 80 proteins, many of which play a critical role in virus-host interactions and immune modulation. Upon viral infections, the host cells activate innate immune responses to restrict their replications. Peroxisomes, which have long been defined to regulate metabolic activities, are reported to be important signaling platforms for antiviral innate immunity. It has been verified that signaling from peroxisomal MAVS (MAVS-Pex) triggers a rapid interferon (IFN) independent IFN-stimulated genes (ISGs) production against invading pathogens. However, little is known about the interaction between DNA viruses such as HSV-1 and the MAVS-Pex mediated signaling.

Results

HSV-1 could activate the MAVS-Pex signaling pathway at a low multiplicity of infection (MOI), while infection at a high MOI dampens MAVS-Pex induced immediately early ISGs production. A high-throughput screen assay reveals that HSV-1 tegument protein VP16 inhibits the immediate early ISGs expression downstream of MAVS-Pex signaling. Moreover, the expression of ISGs was recovered when VP16 was knockdown with its specific short hairpin RNA.

Conclusion

HSV-1 blocks MAVS-Pex mediated early ISGs production through VP16 to dampen the immediate early antiviral innate immunity signaling from peroxisomes.
Literature
1.
go back to reference Akira S, Uematsu S, Takeuchi O. Pathogen recognition and innate immunity. Cell. 2006;124:783–801.CrossRefPubMed Akira S, Uematsu S, Takeuchi O. Pathogen recognition and innate immunity. Cell. 2006;124:783–801.CrossRefPubMed
2.
go back to reference Beutler B, Eidenschenk C, Crozat K, Imler JL, Takeuchi O, Hoffmann JA, Akira S. Genetic analysis of resistance to viral infection. Nat Rev Immunol. 2007;7:753–66.CrossRefPubMed Beutler B, Eidenschenk C, Crozat K, Imler JL, Takeuchi O, Hoffmann JA, Akira S. Genetic analysis of resistance to viral infection. Nat Rev Immunol. 2007;7:753–66.CrossRefPubMed
3.
go back to reference Medzhitov R. Recognition of microorganisms and activation of the immune response. Nature. 2007;449:819–26.CrossRefPubMed Medzhitov R. Recognition of microorganisms and activation of the immune response. Nature. 2007;449:819–26.CrossRefPubMed
4.
go back to reference Pichlmair A, Schulz O, Tan CP, Naslund TI, Liljestrom P, Weber F, Reis e Sousa C. RIG-I-mediated antiviral responses to single-stranded RNA bearing 5′-phosphates. Science. 2006;314:997–1001.CrossRefPubMed Pichlmair A, Schulz O, Tan CP, Naslund TI, Liljestrom P, Weber F, Reis e Sousa C. RIG-I-mediated antiviral responses to single-stranded RNA bearing 5′-phosphates. Science. 2006;314:997–1001.CrossRefPubMed
5.
go back to reference Rehwinkel J, Tan CP, Goubau D, Schulz O, Pichlmair A, Bier K, Robb N, Vreede F, Barclay W, Fodor E, Reis e Sousa C. RIG-I detects viral genomic RNA during negative-strand RNA virus infection. Cell. 2010;140:397–408.CrossRefPubMed Rehwinkel J, Tan CP, Goubau D, Schulz O, Pichlmair A, Bier K, Robb N, Vreede F, Barclay W, Fodor E, Reis e Sousa C. RIG-I detects viral genomic RNA during negative-strand RNA virus infection. Cell. 2010;140:397–408.CrossRefPubMed
6.
go back to reference Yoneyama M, Onomoto K, Jogi M, Akaboshi T, Fujita T. Viral RNA detection by RIG-I-like receptors. Curr Opin Immunol. 2015;32:48–53.CrossRefPubMed Yoneyama M, Onomoto K, Jogi M, Akaboshi T, Fujita T. Viral RNA detection by RIG-I-like receptors. Curr Opin Immunol. 2015;32:48–53.CrossRefPubMed
7.
go back to reference Nakhaei P, Genin P, Civas A, Hiscott J. RIG-I-like receptors: sensing and responding to RNA virus infection. Semin Immunol. 2009;21:215–22.CrossRefPubMed Nakhaei P, Genin P, Civas A, Hiscott J. RIG-I-like receptors: sensing and responding to RNA virus infection. Semin Immunol. 2009;21:215–22.CrossRefPubMed
8.
go back to reference Kato H, Takeuchi O, Mikamo-Satoh E, Hirai R, Kawai T, Matsushita K, Hiiragi A, Dermody TS, Fujita T, Akira S. Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5. J Exp Med. 2008;205:1601–10.CrossRefPubMedPubMedCentral Kato H, Takeuchi O, Mikamo-Satoh E, Hirai R, Kawai T, Matsushita K, Hiiragi A, Dermody TS, Fujita T, Akira S. Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5. J Exp Med. 2008;205:1601–10.CrossRefPubMedPubMedCentral
9.
go back to reference Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA, Hornung V. RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol. 2009;10:1065–72.CrossRefPubMed Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA, Hornung V. RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol. 2009;10:1065–72.CrossRefPubMed
10.
go back to reference Chiu YH, Macmillan JB, Chen ZJ. RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell. 2009;138:576–91.CrossRefPubMedPubMedCentral Chiu YH, Macmillan JB, Chen ZJ. RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell. 2009;138:576–91.CrossRefPubMedPubMedCentral
11.
go back to reference Melchjorsen J, Rintahaka J, Soby S, Horan KA, Poltajainen A, Ostergaard L, Paludan SR, Matikainen S. Early innate recognition of herpes simplex virus in human primary macrophages is mediated via the MDA5/MAVS-dependent and MDA5/MAVS/RNA polymerase III-independent pathways. J Virol. 2010;84:11350–8.CrossRefPubMedPubMedCentral Melchjorsen J, Rintahaka J, Soby S, Horan KA, Poltajainen A, Ostergaard L, Paludan SR, Matikainen S. Early innate recognition of herpes simplex virus in human primary macrophages is mediated via the MDA5/MAVS-dependent and MDA5/MAVS/RNA polymerase III-independent pathways. J Virol. 2010;84:11350–8.CrossRefPubMedPubMedCentral
12.
go back to reference Sarkar SN, Sen GC. Novel functions of proteins encoded by viral stress-inducible genes. Pharmacol Ther. 2004;103:245–59.CrossRefPubMed Sarkar SN, Sen GC. Novel functions of proteins encoded by viral stress-inducible genes. Pharmacol Ther. 2004;103:245–59.CrossRefPubMed
13.
14.
go back to reference Dixit E, Boulant S, Zhang Y, Lee AS, Odendall C, Shum B, Hacohen N, Chen ZJ, Whelan SP, Fransen M, et al. Peroxisomes are signaling platforms for antiviral innate immunity. Cell. 2010;141:668–81.CrossRefPubMedPubMedCentral Dixit E, Boulant S, Zhang Y, Lee AS, Odendall C, Shum B, Hacohen N, Chen ZJ, Whelan SP, Fransen M, et al. Peroxisomes are signaling platforms for antiviral innate immunity. Cell. 2010;141:668–81.CrossRefPubMedPubMedCentral
15.
go back to reference Horner SM, Liu HM, Park HS, Briley J, Gale Jr M. Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus. Proc Natl Acad Sci U S A. 2011;108:14590–5.CrossRefPubMedPubMedCentral Horner SM, Liu HM, Park HS, Briley J, Gale Jr M. Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus. Proc Natl Acad Sci U S A. 2011;108:14590–5.CrossRefPubMedPubMedCentral
16.
go back to reference Seth RB, Sun L, Ea CK, Chen ZJ. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3. Cell. 2005;122:669–82.CrossRefPubMed Seth RB, Sun L, Ea CK, Chen ZJ. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3. Cell. 2005;122:669–82.CrossRefPubMed
19.
go back to reference Mannaerts GP, Van Veldhoven PP. Metabolic pathways in mammalian peroxisomes. Biochimie. 1993;75:147–58.CrossRefPubMed Mannaerts GP, Van Veldhoven PP. Metabolic pathways in mammalian peroxisomes. Biochimie. 1993;75:147–58.CrossRefPubMed
20.
go back to reference Odendall C, Dixit E, Stavru F, Bierne H, Franz KM, Durbin AF, Boulant S, Gehrke L, Cossart P, Kagan JC. Diverse intracellular pathogens activate type III interferon expression from peroxisomes. Nat Immunol. 2014;15:717–26.CrossRefPubMedPubMedCentral Odendall C, Dixit E, Stavru F, Bierne H, Franz KM, Durbin AF, Boulant S, Gehrke L, Cossart P, Kagan JC. Diverse intracellular pathogens activate type III interferon expression from peroxisomes. Nat Immunol. 2014;15:717–26.CrossRefPubMedPubMedCentral
21.
go back to reference Lam Q, Smibert CA, Koop KE, Lavery C, Capone JP, Weinheimer SP, Smiley JR. Herpes simplex virus VP16 rescues viral mRNA from destruction by the virion host shutoff function. EMBO J. 1996;15:2575–81.PubMedPubMedCentral Lam Q, Smibert CA, Koop KE, Lavery C, Capone JP, Weinheimer SP, Smiley JR. Herpes simplex virus VP16 rescues viral mRNA from destruction by the virion host shutoff function. EMBO J. 1996;15:2575–81.PubMedPubMedCentral
22.
go back to reference Mossman KL, Sherburne R, Lavery C, Duncan J, Smiley JR. Evidence that herpes simplex virus VP16 is required for viral egress downstream of the initial envelopment event. J Virol. 2000;74:6287–99.CrossRefPubMedPubMedCentral Mossman KL, Sherburne R, Lavery C, Duncan J, Smiley JR. Evidence that herpes simplex virus VP16 is required for viral egress downstream of the initial envelopment event. J Virol. 2000;74:6287–99.CrossRefPubMedPubMedCentral
23.
go back to reference Smibert CA, Popova B, Xiao P, Capone JP, Smiley JR. Herpes simplex virus VP16 forms a complex with the virion host shutoff protein vhs. J Virol. 1994;68:2339–46.PubMedPubMedCentral Smibert CA, Popova B, Xiao P, Capone JP, Smiley JR. Herpes simplex virus VP16 forms a complex with the virion host shutoff protein vhs. J Virol. 1994;68:2339–46.PubMedPubMedCentral
24.
go back to reference Wang QY, Zhou C, Johnson KE, Colgrove RC, Coen DM, Knipe DM. Herpesviral latency-associated transcript gene promotes assembly of heterochromatin on viral lytic-gene promoters in latent infection. Proc Natl Acad Sci U S A. 2005;102:16055–9.CrossRefPubMedPubMedCentral Wang QY, Zhou C, Johnson KE, Colgrove RC, Coen DM, Knipe DM. Herpesviral latency-associated transcript gene promotes assembly of heterochromatin on viral lytic-gene promoters in latent infection. Proc Natl Acad Sci U S A. 2005;102:16055–9.CrossRefPubMedPubMedCentral
25.
go back to reference Xing J, Ni L, Wang S, Wang K, Lin R, Zheng C. Herpes simplex virus 1-encoded tegument protein VP16 abrogates the production of beta interferon (IFN) by inhibiting NF-kappaB activation and blocking IFN regulatory factor 3 to recruit its coactivator CBP. J Virol. 2013;87:9788–801.CrossRefPubMedPubMedCentral Xing J, Ni L, Wang S, Wang K, Lin R, Zheng C. Herpes simplex virus 1-encoded tegument protein VP16 abrogates the production of beta interferon (IFN) by inhibiting NF-kappaB activation and blocking IFN regulatory factor 3 to recruit its coactivator CBP. J Virol. 2013;87:9788–801.CrossRefPubMedPubMedCentral
26.
go back to reference Carlton-Smith C, Elliott RM. Viperin, MTAP44, and protein kinase R contribute to the interferon-induced inhibition of Bunyamwera Orthobunyavirus replication. J Virol. 2012;86:11548–57.CrossRefPubMedPubMedCentral Carlton-Smith C, Elliott RM. Viperin, MTAP44, and protein kinase R contribute to the interferon-induced inhibition of Bunyamwera Orthobunyavirus replication. J Virol. 2012;86:11548–57.CrossRefPubMedPubMedCentral
27.
go back to reference Chin KC, Cresswell P. Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus. Proc Natl Acad Sci U S A. 2001;98:15125–30.CrossRefPubMedPubMedCentral Chin KC, Cresswell P. Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus. Proc Natl Acad Sci U S A. 2001;98:15125–30.CrossRefPubMedPubMedCentral
28.
go back to reference Fredericksen BL, Smith M, Katze MG, Shi PY, Gale Jr M. The host response to West Nile Virus infection limits viral spread through the activation of the interferon regulatory factor 3 pathway. J Virol. 2004;78:7737–47.CrossRefPubMedPubMedCentral Fredericksen BL, Smith M, Katze MG, Shi PY, Gale Jr M. The host response to West Nile Virus infection limits viral spread through the activation of the interferon regulatory factor 3 pathway. J Virol. 2004;78:7737–47.CrossRefPubMedPubMedCentral
29.
go back to reference Helbig KJ, Carr JM, Calvert JK, Wati S, Clarke JN, Eyre NS, Narayana SK, Fiches GN, McCartney EM, Beard MR. Viperin is induced following dengue virus type-2 (DENV-2) infection and has anti-viral actions requiring the C-terminal end of viperin. PLoS Negl Trop Dis. 2013;7:e2178.CrossRefPubMedPubMedCentral Helbig KJ, Carr JM, Calvert JK, Wati S, Clarke JN, Eyre NS, Narayana SK, Fiches GN, McCartney EM, Beard MR. Viperin is induced following dengue virus type-2 (DENV-2) infection and has anti-viral actions requiring the C-terminal end of viperin. PLoS Negl Trop Dis. 2013;7:e2178.CrossRefPubMedPubMedCentral
30.
go back to reference Helbig KJ, Eyre NS, Yip E, Narayana S, Li K, Fiches G, McCartney EM, Jangra RK, Lemon SM, Beard MR. The antiviral protein viperin inhibits hepatitis C virus replication via interaction with nonstructural protein 5A. Hepatology. 2011;54:1506–17.CrossRefPubMedPubMedCentral Helbig KJ, Eyre NS, Yip E, Narayana S, Li K, Fiches G, McCartney EM, Jangra RK, Lemon SM, Beard MR. The antiviral protein viperin inhibits hepatitis C virus replication via interaction with nonstructural protein 5A. Hepatology. 2011;54:1506–17.CrossRefPubMedPubMedCentral
31.
go back to reference McGillivary G, Jordan ZB, Peeples ME, Bakaletz LO. Replication of respiratory syncytial virus is inhibited by the host defense molecule viperin. J Innate Immun. 2013;5:60–71.CrossRefPubMed McGillivary G, Jordan ZB, Peeples ME, Bakaletz LO. Replication of respiratory syncytial virus is inhibited by the host defense molecule viperin. J Innate Immun. 2013;5:60–71.CrossRefPubMed
32.
go back to reference Nasr N, Maddocks S, Turville SG, Harman AN, Woolger N, Helbig KJ, Wilkinson J, Bye CR, Wright TK, Rambukwelle D, et al. HIV-1 infection of human macrophages directly induces viperin which inhibits viral production. Blood. 2012;120:778–88.CrossRefPubMed Nasr N, Maddocks S, Turville SG, Harman AN, Woolger N, Helbig KJ, Wilkinson J, Bye CR, Wright TK, Rambukwelle D, et al. HIV-1 infection of human macrophages directly induces viperin which inhibits viral production. Blood. 2012;120:778–88.CrossRefPubMed
33.
go back to reference Severa M, Coccia EM, Fitzgerald KA. Toll-like receptor-dependent and -independent viperin gene expression and counter-regulation by PRDI-binding factor-1/BLIMP1. J Biol Chem. 2006;281:26188–95.CrossRefPubMed Severa M, Coccia EM, Fitzgerald KA. Toll-like receptor-dependent and -independent viperin gene expression and counter-regulation by PRDI-binding factor-1/BLIMP1. J Biol Chem. 2006;281:26188–95.CrossRefPubMed
34.
go back to reference Szretter KJ, Brien JD, Thackray LB, Virgin HW, Cresswell P, Diamond MS. The interferon-inducible gene viperin restricts West Nile virus pathogenesis. J Virol. 2011;85:11557–66.CrossRefPubMedPubMedCentral Szretter KJ, Brien JD, Thackray LB, Virgin HW, Cresswell P, Diamond MS. The interferon-inducible gene viperin restricts West Nile virus pathogenesis. J Virol. 2011;85:11557–66.CrossRefPubMedPubMedCentral
35.
go back to reference Tan KS, Olfat F, Phoon MC, Hsu JP, Howe JL, Seet JE, Chin KC, Chow VT. In vivo and in vitro studies on the antiviral activities of viperin against influenza H1N1 virus infection. J Gen Virol. 2012;93:1269–77.CrossRefPubMed Tan KS, Olfat F, Phoon MC, Hsu JP, Howe JL, Seet JE, Chin KC, Chow VT. In vivo and in vitro studies on the antiviral activities of viperin against influenza H1N1 virus infection. J Gen Virol. 2012;93:1269–77.CrossRefPubMed
36.
go back to reference Teng TS, Foo SS, Simamarta D, Lum FM, Teo TH, Lulla A, Yeo NK, Koh EG, Chow A, Leo YS, et al. Viperin restricts chikungunya virus replication and pathology. J Clin Invest. 2012;122:4447–60.CrossRefPubMedPubMedCentral Teng TS, Foo SS, Simamarta D, Lum FM, Teo TH, Lulla A, Yeo NK, Koh EG, Chow A, Leo YS, et al. Viperin restricts chikungunya virus replication and pathology. J Clin Invest. 2012;122:4447–60.CrossRefPubMedPubMedCentral
37.
go back to reference Wang X, Hinson ER, Cresswell P. The interferon-inducible protein viperin inhibits influenza virus release by perturbing lipid rafts. Cell Host Microbe. 2007;2:96–105.CrossRefPubMed Wang X, Hinson ER, Cresswell P. The interferon-inducible protein viperin inhibits influenza virus release by perturbing lipid rafts. Cell Host Microbe. 2007;2:96–105.CrossRefPubMed
38.
go back to reference Xing J, Wang S, Lin R, Mossman KL, Zheng C. Herpes simplex virus 1 tegument protein US11 downmodulates the RLR signaling pathway via direct interaction with RIG-I and MDA-5. J Virol. 2012;86:3528–40.CrossRefPubMedPubMedCentral Xing J, Wang S, Lin R, Mossman KL, Zheng C. Herpes simplex virus 1 tegument protein US11 downmodulates the RLR signaling pathway via direct interaction with RIG-I and MDA-5. J Virol. 2012;86:3528–40.CrossRefPubMedPubMedCentral
39.
go back to reference Wang K, Ni L, Wang S, Zheng C. Herpes simplex virus 1 protein kinase US3 hyperphosphorylates p65/RelA and dampens NF-kappaB activation. J Virol. 2014;88:7941–51.CrossRefPubMedPubMedCentral Wang K, Ni L, Wang S, Zheng C. Herpes simplex virus 1 protein kinase US3 hyperphosphorylates p65/RelA and dampens NF-kappaB activation. J Virol. 2014;88:7941–51.CrossRefPubMedPubMedCentral
40.
go back to reference Wang S, Wang K, Li J, Zheng C. Herpes simplex virus 1 ubiquitin-specific protease UL36 inhibits beta interferon production by deubiquitinating TRAF3. J Virol. 2013;87:11851–60.CrossRefPubMedPubMedCentral Wang S, Wang K, Li J, Zheng C. Herpes simplex virus 1 ubiquitin-specific protease UL36 inhibits beta interferon production by deubiquitinating TRAF3. J Virol. 2013;87:11851–60.CrossRefPubMedPubMedCentral
41.
go back to reference Wang S, Wang K, Lin R, Zheng C. Herpes simplex virus 1 serine/threonine kinase US3 hyperphosphorylates IRF3 and inhibits beta interferon production. J Virol. 2013;87:12814–27.CrossRefPubMedPubMedCentral Wang S, Wang K, Lin R, Zheng C. Herpes simplex virus 1 serine/threonine kinase US3 hyperphosphorylates IRF3 and inhibits beta interferon production. J Virol. 2013;87:12814–27.CrossRefPubMedPubMedCentral
42.
go back to reference Zhang J, Wang K, Wang S, Zheng C. Herpes simplex virus 1 E3 ubiquitin ligase ICP0 protein inhibits tumor necrosis factor alpha-induced NF-kappaB activation by interacting with p65/RelA and p50/NF-kappaB1. J Virol. 2013;87:12935–48.CrossRefPubMedPubMedCentral Zhang J, Wang K, Wang S, Zheng C. Herpes simplex virus 1 E3 ubiquitin ligase ICP0 protein inhibits tumor necrosis factor alpha-induced NF-kappaB activation by interacting with p65/RelA and p50/NF-kappaB1. J Virol. 2013;87:12935–48.CrossRefPubMedPubMedCentral
43.
go back to reference Zhang J, Wang S, Wang K, Zheng C. Herpes simplex virus 1 DNA polymerase processivity factor UL42 inhibits TNF-alpha-induced NF-kappaB activation by interacting with p65/RelA and p50/NF-kappaB1. Med Microbiol Immunol. 2013;202:313–25.CrossRefPubMed Zhang J, Wang S, Wang K, Zheng C. Herpes simplex virus 1 DNA polymerase processivity factor UL42 inhibits TNF-alpha-induced NF-kappaB activation by interacting with p65/RelA and p50/NF-kappaB1. Med Microbiol Immunol. 2013;202:313–25.CrossRefPubMed
44.
go back to reference Zhu H, Zheng C, Xing J, Wang S, Li S, Lin R, Mossman KL. Varicella-zoster virus immediate-early protein ORF61 abrogates the IRF3-mediated innate immune response through degradation of activated IRF3. J Virol. 2011;85:11079–89.CrossRefPubMedPubMedCentral Zhu H, Zheng C, Xing J, Wang S, Li S, Lin R, Mossman KL. Varicella-zoster virus immediate-early protein ORF61 abrogates the IRF3-mediated innate immune response through degradation of activated IRF3. J Virol. 2011;85:11079–89.CrossRefPubMedPubMedCentral
45.
go back to reference Xing J, Wang S, Li Y, Guo H, Zhao L, Pan W, Lin F, Zhu H, Wang L, Li M, Zheng C. Characterization of the subcellular localization of herpes simplex virus type 1 proteins in living cells. Med Microbiol Immunol. 2011;200:61–8.CrossRefPubMed Xing J, Wang S, Li Y, Guo H, Zhao L, Pan W, Lin F, Zhu H, Wang L, Li M, Zheng C. Characterization of the subcellular localization of herpes simplex virus type 1 proteins in living cells. Med Microbiol Immunol. 2011;200:61–8.CrossRefPubMed
47.
go back to reference Zenner HL, Mauricio R, Banting G, Crump CM. Herpes simplex virus 1 counteracts tetherin restriction via its virion host shutoff activity. J Virol. 2013;87:13115–23.CrossRefPubMedPubMedCentral Zenner HL, Mauricio R, Banting G, Crump CM. Herpes simplex virus 1 counteracts tetherin restriction via its virion host shutoff activity. J Virol. 2013;87:13115–23.CrossRefPubMedPubMedCentral
48.
go back to reference Shen G, Wang K, Wang S, Cai M, Li ML, Zheng C. Herpes simplex virus 1 counteracts viperin via its virion host shutoff protein UL41. J Virol. \2014;88:12163–6.CrossRefPubMedPubMedCentral Shen G, Wang K, Wang S, Cai M, Li ML, Zheng C. Herpes simplex virus 1 counteracts viperin via its virion host shutoff protein UL41. J Virol. \2014;88:12163–6.CrossRefPubMedPubMedCentral
49.
50.
go back to reference Verpooten D, Ma Y, Hou S, Yan Z, He B. Control of TANK-binding kinase 1-mediated signaling by the gamma(1)34.5 protein of herpes simplex virus 1. J Biol Chem. 2009;284:1097–105.CrossRefPubMedPubMedCentral Verpooten D, Ma Y, Hou S, Yan Z, He B. Control of TANK-binding kinase 1-mediated signaling by the gamma(1)34.5 protein of herpes simplex virus 1. J Biol Chem. 2009;284:1097–105.CrossRefPubMedPubMedCentral
51.
go back to reference Zhang D, Su C, Zheng C. Herpes simplex virus 1 serine protease VP24 blocks the DNA-sensing signal pathway by abrogating activation of interferon regulatory factor 3. J Virol. 2016;90:5824–9.CrossRefPubMedPubMedCentral Zhang D, Su C, Zheng C. Herpes simplex virus 1 serine protease VP24 blocks the DNA-sensing signal pathway by abrogating activation of interferon regulatory factor 3. J Virol. 2016;90:5824–9.CrossRefPubMedPubMedCentral
52.
go back to reference Xing J, Wang S, Lin F, Pan W, Hu CD, Zheng C. Comprehensive characterization of interaction complexes of herpes simplex virus type 1 ICP22, UL3, UL4, and UL20.5. J Virol. 2011;85:1881–6.CrossRefPubMed Xing J, Wang S, Lin F, Pan W, Hu CD, Zheng C. Comprehensive characterization of interaction complexes of herpes simplex virus type 1 ICP22, UL3, UL4, and UL20.5. J Virol. 2011;85:1881–6.CrossRefPubMed
53.
go back to reference Jordan M, Schallhorn A, Wurm FM. Transfecting mammalian cells: optimization of critical parameters affecting calcium-phosphate precipitate formation. Nucleic Acids Res. 1996;24:596–601.CrossRefPubMedPubMedCentral Jordan M, Schallhorn A, Wurm FM. Transfecting mammalian cells: optimization of critical parameters affecting calcium-phosphate precipitate formation. Nucleic Acids Res. 1996;24:596–601.CrossRefPubMedPubMedCentral
Metadata
Title
Herpes simplex virus 1 infection dampens the immediate early antiviral innate immunity signaling from peroxisomes by tegument protein VP16
Authors
Chunfu Zheng
Chenhe Su
Publication date
01-12-2017
Publisher
BioMed Central
Published in
Virology Journal / Issue 1/2017
Electronic ISSN: 1743-422X
DOI
https://doi.org/10.1186/s12985-017-0709-5

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