Virulence of Herpes Simplex Virus 1 Harboring a UAG Stop Codon between the First and Second Initiation Codon in the Thymidine Kinase Gene
Herpes simplex virus 1 (HSV-1)-TK (8UAG) expresses a truncated thymidine kinase (TK) translated from the second initiation codon due to a stop codon (UAG) at the 8th position (counted from the first initiation codon). Here, we showed that the sensitivity of HSV-1-TK (8UAG) to acyclovir (ACV) is simi...
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| Published in | Japanese Journal of Infectious Diseases Vol. 75; no. 4; pp. 368 - 373 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
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Japan
National Institute of Infectious Diseases, Japanese Journal of Infectious Diseases Editorial Committee
31.07.2022
Japan Science and Technology Agency |
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| Abstract | Herpes simplex virus 1 (HSV-1)-TK (8UAG) expresses a truncated thymidine kinase (TK) translated from the second initiation codon due to a stop codon (UAG) at the 8th position (counted from the first initiation codon). Here, we showed that the sensitivity of HSV-1-TK (8UAG) to acyclovir (ACV) is similar to that of the control HSV-1 wild-type (WT), which expresses an intact TK protein. However, HSV-1-TK (44UAG), which expresses a truncated TK due to a UAG codon at position 44, showed lower sensitivity to ACV. A mouse infection model was used to compare the virulence of HSV-1-TK (8UAG) and HSV-1-TK (44UAG) to that of HSV-1 WT. The 50% lethal dose (LD50) for HSV-1-TK (44UAG) was 7.8-fold higher than that for HSV-1-TK (8UAG), whereas the LD50 for HSV-1-TK (8UAG) was the same as that for the parental HSV-1 WT. There were no statistically significant differences among HSV-1-TK (44UAG), HSV-1-TK (8UAG), and HSV-1 WT with respect to replication capacity and viral TK mRNA expression in the mouse brain. Thus, the virulence of HSV-1 expressing the truncated viral TK translated from the second initiation codon might depend on the position of the UAG stop codon. |
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| AbstractList | Herpes simplex virus 1 (HSV-1)-TK (8UAG) expresses a truncated thymidine kinase (TK) translated from the second initiation codon due to a stop codon (UAG) at the 8th position (counted from the first initiation codon). Here, we showed that the sensitivity of HSV-1-TK (8UAG) to acyclovir (ACV) is similar to that of the control HSV-1 wild-type (WT), which expresses an intact TK protein. However, HSV-1-TK (44UAG), which expresses a truncated TK due to a UAG codon at position 44, showed lower sensitivity to ACV. A mouse infection model was used to compare the virulence of HSV-1-TK (8UAG) and HSV-1-TK (44UAG) to that of HSV-1 WT. The 50% lethal dose (LD50) for HSV-1-TK (44UAG) was 7.8-fold higher than that for HSV-1-TK (8UAG), whereas the LD50 for HSV-1-TK (8UAG) was the same as that for the parental HSV-1 WT. There were no statistically significant differences among HSV-1-TK (44UAG), HSV-1-TK (8UAG), and HSV-1 WT with respect to replication capacity and viral TK mRNA expression in the mouse brain. Thus, the virulence of HSV-1 expressing the truncated viral TK translated from the second initiation codon might depend on the position of the UAG stop codon. Herpes simplex virus 1 (HSV-1)-TK(8UAG) expresses a truncated thymidine kinase (TK) translated from the second initiation codon due to a stop UAG codon at the 8th position (counted from the first initiation codon). Here, we showed that the sensitivity of HSV-1-TK(8UAG) to acyclovir (ACV) is similar to that of control HSV-1 wild-type (WT), which expresses an intact TK protein. However, HSV-1-TK(44UAG), which expresses a truncated TK due to a UAG codon at position 44, showed lower sensitivity to ACV. A mouse infection model was used to compare the virulence of HSV-1-TK(8UAG) and HSV-1-TK(44UAG) with that of HSV-1 wild-type (WT). The 50% lethal dose (LD ) value of HSV-1-TK(44UAG) was 7.8-fold higher than that of HSV-1-TK(8UAG), whereas the LD value of HSV-1-TK(8UAG) was the same as that of the parental HSV-1 WT. There were no statistically significant differences between HSV-1-TK(44UAG), HSV-1-TK(8UAG), and HSV-1 WT with respect to replication capacity and viral TK mRNA expression in mouse brain. Thus, the virulence of HSV-1 expressing a truncated viral TK translated from the second initiation codon might depend on the position of the UAG stop codon. Herpes simplex virus 1 (HSV-1)-TK (8UAG) expresses a truncated thymidine kinase (TK) translated from the second initiation codon due to a stop codon (UAG) at the 8th position (counted from the first initiation codon). Here, we showed that the sensitivity of HSV-1-TK (8UAG) to acyclovir (ACV) is similar to that of the control HSV-1 wild-type (WT), which expresses an intact TK protein. However, HSV-1-TK (44UAG), which expresses a truncated TK due to a UAG codon at position 44, showed lower sensitivity to ACV. A mouse infection model was used to compare the virulence of HSV-1-TK (8UAG) and HSV-1-TK (44UAG) to that of HSV-1 WT. The 50% lethal dose (LD50) for HSV-1-TK (44UAG) was 7.8-fold higher than that for HSV-1-TK (8UAG), whereas the LD50 for HSV-1-TK (8UAG) was the same as that for the parental HSV-1 WT. There were no statistically significant differences among HSV-1-TK (44UAG), HSV-1-TK (8UAG), and HSV-1 WT with respect to replication capacity and viral TK mRNA expression in the mouse brain. Thus, the virulence of HSV-1 expressing the truncated viral TK translated from the second initiation codon might depend on the position of the UAG stop codon.Herpes simplex virus 1 (HSV-1)-TK (8UAG) expresses a truncated thymidine kinase (TK) translated from the second initiation codon due to a stop codon (UAG) at the 8th position (counted from the first initiation codon). Here, we showed that the sensitivity of HSV-1-TK (8UAG) to acyclovir (ACV) is similar to that of the control HSV-1 wild-type (WT), which expresses an intact TK protein. However, HSV-1-TK (44UAG), which expresses a truncated TK due to a UAG codon at position 44, showed lower sensitivity to ACV. A mouse infection model was used to compare the virulence of HSV-1-TK (8UAG) and HSV-1-TK (44UAG) to that of HSV-1 WT. The 50% lethal dose (LD50) for HSV-1-TK (44UAG) was 7.8-fold higher than that for HSV-1-TK (8UAG), whereas the LD50 for HSV-1-TK (8UAG) was the same as that for the parental HSV-1 WT. There were no statistically significant differences among HSV-1-TK (44UAG), HSV-1-TK (8UAG), and HSV-1 WT with respect to replication capacity and viral TK mRNA expression in the mouse brain. Thus, the virulence of HSV-1 expressing the truncated viral TK translated from the second initiation codon might depend on the position of the UAG stop codon. |
| ArticleNumber | JJID.2021.674 |
| Author | Yamada, Souichi Fukushi, Shuetsu Harada, Shizuko Nguyen, Phu Hoang Anh Saijo, Masayuki Mizuguchi, Masashi |
| Author_xml | – sequence: 1 fullname: Yamada, Souichi organization: Department of Virology 1, National Institute of Infectious Diseases, Japan – sequence: 1 fullname: Nguyen, Phu Hoang Anh organization: Department of Developmental Medical Sciences, The University of Tokyo, Japan – sequence: 1 fullname: Saijo, Masayuki organization: Public Health Office, Health and Welfare Bureau, Sapporo Municipal Government, Japan – sequence: 1 fullname: Harada, Shizuko organization: Department of Virology 1, National Institute of Infectious Diseases, Japan – sequence: 1 fullname: Fukushi, Shuetsu organization: Department of Virology 1, National Institute of Infectious Diseases, Japan – sequence: 1 fullname: Mizuguchi, Masashi organization: Department of Developmental Medical Sciences, The University of Tokyo, Japan |
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| Cites_doi | 10.1128/JVI.01440-13 10.1099/0022-1317-64-3-523 10.1073/pnas.74.12.5716 10.1128/JCM.42.1.242-249.2004 10.1002/(SICI)1096-9071(199908)58:4<387::AID-JMV11>3.0.CO;2-K 10.1016/j.antiviral.2010.03.002 10.1099/0022-1317-70-4-869 10.1038/289081a0 10.1086/515626 10.1128/jvi.71.5.3872-3878.1997 10.1128/AAC.17.2.209 10.1186/s12985-017-0728-2 10.1017/S0022172400025109 10.1016/j.antiviral.2003.08.018 10.1128/JVI.77.2.1382-1391.2003 10.1046/j.1365-2133.1998.02374.x 10.1128/JVI.01979-16 10.1093/infdis/jix042 10.1099/0022-1317-70-2-375 10.1016/S0021-9258(17)34236-9 10.1002/jmv.1890430319 10.1093/oxfordjournals.aje.a118408 10.1016/S0166-3542(85)80003-6 10.1016/S1386-6532(02)00263-9 10.1099/vir.0.039776-0 10.1128/JVI.01161-19 10.1016/S0166-0934(03)00069-7 10.1128/JVI.75.7.3105-3110.2001 10.1128/AAC.31.7.1117 10.1128/AAC.35.11.2322 10.1099/vir.0.18881-0 10.1111/j.1348-0421.1995.tb03271.x 10.1016/0042-6822(85)90009-1 10.1007/s00705-007-1096-9 10.3389/fmicb.2019.00941 10.1128/AAC.23.5.676 10.7883/yoken.JJID.2020.313 |
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| References | 17. Larder BA, Darby G. Selection and characterisation of acyclovir-resistant herpes simplex virus type 1 mutants inducing altered DNA polymerase activities. Virology. 1985;146:262-271. 33. Xie Y, Wu L, Wang M, et al. Alpha-herpesvirus thymidine kinase genes mediate viral virulence and are potential therapeutic targets. Front Microbiol. 2019;10:941. 20. Efstathiou S, Kemp S, Darby G, et al. The role of herpes simplex virus type 1 thymidine kinase in pathogenesis. J Gen Virol. 1989;70:869-879. 28. Saijo M, Suzutani T, Mizuta K, et al. Characterization and susceptibility to antiviral agents of herpes simplex virus type 1 containing a unique thymidine kinase gene with an amber codon between the first and the second initiation codons. Arch Virol. 2008;153:303-314. 16. Sauerbrei A, Deinhardt S, Zell R, et al. Phenotypic and genotypic characterization of acyclovir-resistant clinical isolates of herpes simplex virus. Antiviral Res. 2010;86:246-252. 21. Suzutani T, Koyano S, Takada M, et al. Analysis of the relationship between cellular thymidine kinase activity and virulence of thymidine kinase-negative herpes simplex virus types 1 and 2. Microbiol Immunol. 1995;39:787-794. 19. Field HJ, Darby G. Pathogenicity in mice of strains of herpes simplex virus which are resistant to acyclovir in vitro and in vivo. Antimicrob Agents Chemother. 1980;17:209-216. 24. Huang CY, Yao HW, Wang LC, et al. Thymidine kinase-negative herpes simplex virus 1 can efficiently establish persistent infection in neural tissues of nude mice. J Virol. 2017;91:e01979-16. 37. Xing J, Ni L, Wang S, et al. Herpes simplex virus 1-encoded tegument protein VP16 abrogates the production of beta interferon (IFN) by inhibiting NF-κB activation and blocking IFN regulatory factor 3 to recruit its coactivator CBP. J Virol. 2013;87:9788-9801. 7. Fyfe JA, Keller PM, Furman PA, et al. Thymidine kinase from herpes simplex virus phosphorylates the new antiviral compound, 9-(2-hydroxyethoxymethyl) guanine. J Biol Chem. 1978;253:8721-8727. 25. Omura N, Fujii H, Yoshikawa T, et al. Association between sensitivity of viral thymidine kinase-associated acyclovir-resistant herpes simplex virus type 1 and virulence. Virol J. 2017;14:59. 30. Reed LJ, Muench H. A simple method of estimating fifty percent endpoint. Am J Hyg. 1938;27:493-497. 31. Ebeling SB, Eric Borst HP, Simonetti ER, et al. Development and application of quantitative real time PCR and RT-PCR assays that discriminate between the full-length and truncated herpes simplex virus thymidine kinase gene. J Virol Methods. 2003;109:177-186. 6. Elion GB, Furman PA, Fyfe JA, et al. Selectivity of action of an antiherpetic agent, 9-(2-hydroxyethoxymethyl) guanine. Proc Natl Acad Sci U S A. 1977;74:5716-5720. 8. Smee DF, Martin JC, Verheyden JP, et al. Anti-herpesvirus activity of the acyclic nucleoside 9-(1,3-dihydroxy-2-propoxymethyl) guanine. Antimicrob Agents Chemother. 1983;23:676-682. 23. Grey F, Sowa M, Collins P, et al. Characterization of a neurovirulent aciclovir-resistant variant of herpes simplex virus. J Gen Virol. 2003;84:1403-1410. 22. Stroop WG, Careene Banks M, Qavi H, et al. A thymidine kinase deficient HSV-2 strain causes acute keratitis and establishes trigeminal ganglionic latency, but poorly reactivates in vivo. J Med Virol. 1994;43:297-309. 10. Ellis MN, Keller PM, Fyfe JA, et al. Clinical isolate of herpes simplex virus type 2 that induces a thymidine kinase with altered substrate specificity. Antimicrob Agents Chemother. 1987;31:1117-1125. 15. Morfin F, Thouvenot D. Herpes simplex virus resistance to antiviral drugs. J Clin Virol. 2003;26:29-37. 9. Darby G, Field HJ, Salisbury SA. Altered substrate specificity of herpes simplex virus thymidine kinase confers acyclovir resistance. Nature.1981;289:81-83. 11. Larder BA, Cheng YC, Darby G. Characterization of abnormal thymidine kinases induced by drug-resistant strains of herpes simplex virus type 1. J Gen Virol. 1983;64:523-532. 18. Collins P, Larder BA, Oliver NM, et al. Characterization of a DNA polymerase mutant of herpes simplex virus from a severely immunocompromised patient receiving acyclovir. J Gen Virol. 1989;70:375-382. 36. Loret S, Lippé R. Biochemical analysis of infected cell polypeptide (ICP)0, ICP4, UL7 and UL23 incorporated into extracellular herpes simplex virus type 1 virions. J Gen Virol. 2012;93:624-634. 13. Sasadeusz JJ, Tufaro F, Safrin S, et al. Homopolymer mutational hot spots mediate herpes simplex virus resistance to acyclovir. J Virol.1997;71:3872-3878. 29. Tanaka M, Kagawa H, Yamanashi Y, et al. Construction of an excisable bacterial artificial chromosome containing a full-length infectious clone of herpes simplex virus type 1: viruses reconstituted from the clone exhibit wild-type properties in vitro and in vivo. J Virol. 2003;77:1382-1391. 12. De Clercq E. Recent trends and development in antiviral chemotherapy. Antiviral Res. 1985;Suppl 1:11-9. 3. Danve-Szatanek C, Aymard M, Thouvenot D, et al. Surveillance network for herpes simplex virus resistance to antiviral drugs: 3-year follow-up. J Clin Microbiol. 2004;42:242-249. 35. Boukhvalova MS, Mortensen E, Mbaye A, et al. Herpes simplex virus 1 induces brain inflammation and multifocal demyelination in the cotton rat Sigmodon hispidus. J Virol. 2019;94:e01161-19. 4. Kakiuchi S, Tsuji M, Nishimura H, et al. Association of the emergence of acyclovir-resistant herpes simplex virus type 1 with prognosis in hematopoietic stem cell transplantation patients. J Infect Dis. 2017;215:865-873. 14. Bestman-Smith J, Schmit I, Papadopoulou B, et al. Highly reliable heterologous system for evaluating resistance of clinical herpes simplex virus isolates to nucleoside analogues. J Virol. 2001;75:3105-3110. 32. Hill EL, Hunter GA, Ellis MN. In vitro and in vivo characterization of herpes simplex virus clinical isolates recovered from patients infected with human immunodeficiency virus. Antimicrob Agents Chemother. 1991;35:2322-2328. 27. Saijo M, Suzutani T, Itoh K, et al. Nucleotide sequence of thymidine kinase gene of sequential acyclovir-resistant herpes simplex virus type 1 isolates recovered from a child with Wiskott-Aldrich syndrome: evidence for reactivation of acyclovir-resistant herpes simplex virus. J Med Virol. 1999;58:387-393. 34. Field HJ, Wildy P. The pathogenicity of thymidine kinase-deficient mutants of herpes simplex virus in mice. J Hyg (Lond). 1978;81:267-277. 5. Saijo M, Suzutani T, Murono K, et al. Recurrent aciclovir-resistant herpes simplex in a child with Wiskott-Aldrich syndrome. Br J Dermatol. 1998;139:311-314. 26. Nguyen PHA, Yamada S, Shibamura M, et al. New mechanism of acyclovir resistance in herpes simplex virus 1, which has a UAG stop codon between the first and second AUG initiation codons. Jpn J Infect Dis. 2020;73:447-451. 2. Chibo D, Druce J, Sasadeusz J, et al. Molecular analysis of clinical isolates of acyclovir resistant herpes simplex virus. Antiviral Res. 2004;61:83-91. 1. Gaudreau A, Hill E, Balfour Jr HH, et al. Phenotypic and genotypic characterization of acyclovir-resistant herpes simplex viruses from immunocompromised patients. J Infect Dis. 1998;178:297-303. 22 23 24 25 26 27 28 29 30 31 10 32 11 33 12 34 13 35 14 36 15 37 16 17 18 19 1 2 3 4 5 6 7 8 9 20 21 |
| References_xml | – reference: 35. Boukhvalova MS, Mortensen E, Mbaye A, et al. Herpes simplex virus 1 induces brain inflammation and multifocal demyelination in the cotton rat Sigmodon hispidus. J Virol. 2019;94:e01161-19. – reference: 33. Xie Y, Wu L, Wang M, et al. Alpha-herpesvirus thymidine kinase genes mediate viral virulence and are potential therapeutic targets. Front Microbiol. 2019;10:941. – reference: 37. Xing J, Ni L, Wang S, et al. Herpes simplex virus 1-encoded tegument protein VP16 abrogates the production of beta interferon (IFN) by inhibiting NF-κB activation and blocking IFN regulatory factor 3 to recruit its coactivator CBP. J Virol. 2013;87:9788-9801. – reference: 34. Field HJ, Wildy P. The pathogenicity of thymidine kinase-deficient mutants of herpes simplex virus in mice. J Hyg (Lond). 1978;81:267-277. – reference: 8. Smee DF, Martin JC, Verheyden JP, et al. Anti-herpesvirus activity of the acyclic nucleoside 9-(1,3-dihydroxy-2-propoxymethyl) guanine. Antimicrob Agents Chemother. 1983;23:676-682. – reference: 11. Larder BA, Cheng YC, Darby G. Characterization of abnormal thymidine kinases induced by drug-resistant strains of herpes simplex virus type 1. J Gen Virol. 1983;64:523-532. – reference: 15. Morfin F, Thouvenot D. Herpes simplex virus resistance to antiviral drugs. J Clin Virol. 2003;26:29-37. – reference: 32. Hill EL, Hunter GA, Ellis MN. In vitro and in vivo characterization of herpes simplex virus clinical isolates recovered from patients infected with human immunodeficiency virus. Antimicrob Agents Chemother. 1991;35:2322-2328. – reference: 4. Kakiuchi S, Tsuji M, Nishimura H, et al. Association of the emergence of acyclovir-resistant herpes simplex virus type 1 with prognosis in hematopoietic stem cell transplantation patients. J Infect Dis. 2017;215:865-873. – reference: 10. Ellis MN, Keller PM, Fyfe JA, et al. Clinical isolate of herpes simplex virus type 2 that induces a thymidine kinase with altered substrate specificity. Antimicrob Agents Chemother. 1987;31:1117-1125. – reference: 26. Nguyen PHA, Yamada S, Shibamura M, et al. New mechanism of acyclovir resistance in herpes simplex virus 1, which has a UAG stop codon between the first and second AUG initiation codons. Jpn J Infect Dis. 2020;73:447-451. – reference: 19. Field HJ, Darby G. Pathogenicity in mice of strains of herpes simplex virus which are resistant to acyclovir in vitro and in vivo. Antimicrob Agents Chemother. 1980;17:209-216. – reference: 25. Omura N, Fujii H, Yoshikawa T, et al. Association between sensitivity of viral thymidine kinase-associated acyclovir-resistant herpes simplex virus type 1 and virulence. Virol J. 2017;14:59. – reference: 27. Saijo M, Suzutani T, Itoh K, et al. Nucleotide sequence of thymidine kinase gene of sequential acyclovir-resistant herpes simplex virus type 1 isolates recovered from a child with Wiskott-Aldrich syndrome: evidence for reactivation of acyclovir-resistant herpes simplex virus. J Med Virol. 1999;58:387-393. – reference: 7. Fyfe JA, Keller PM, Furman PA, et al. Thymidine kinase from herpes simplex virus phosphorylates the new antiviral compound, 9-(2-hydroxyethoxymethyl) guanine. J Biol Chem. 1978;253:8721-8727. – reference: 17. Larder BA, Darby G. Selection and characterisation of acyclovir-resistant herpes simplex virus type 1 mutants inducing altered DNA polymerase activities. Virology. 1985;146:262-271. – reference: 22. Stroop WG, Careene Banks M, Qavi H, et al. A thymidine kinase deficient HSV-2 strain causes acute keratitis and establishes trigeminal ganglionic latency, but poorly reactivates in vivo. J Med Virol. 1994;43:297-309. – reference: 2. Chibo D, Druce J, Sasadeusz J, et al. Molecular analysis of clinical isolates of acyclovir resistant herpes simplex virus. Antiviral Res. 2004;61:83-91. – reference: 16. Sauerbrei A, Deinhardt S, Zell R, et al. Phenotypic and genotypic characterization of acyclovir-resistant clinical isolates of herpes simplex virus. Antiviral Res. 2010;86:246-252. – reference: 29. Tanaka M, Kagawa H, Yamanashi Y, et al. Construction of an excisable bacterial artificial chromosome containing a full-length infectious clone of herpes simplex virus type 1: viruses reconstituted from the clone exhibit wild-type properties in vitro and in vivo. J Virol. 2003;77:1382-1391. – reference: 12. De Clercq E. Recent trends and development in antiviral chemotherapy. Antiviral Res. 1985;Suppl 1:11-9. – reference: 5. Saijo M, Suzutani T, Murono K, et al. Recurrent aciclovir-resistant herpes simplex in a child with Wiskott-Aldrich syndrome. Br J Dermatol. 1998;139:311-314. – reference: 3. Danve-Szatanek C, Aymard M, Thouvenot D, et al. Surveillance network for herpes simplex virus resistance to antiviral drugs: 3-year follow-up. J Clin Microbiol. 2004;42:242-249. – reference: 20. Efstathiou S, Kemp S, Darby G, et al. The role of herpes simplex virus type 1 thymidine kinase in pathogenesis. J Gen Virol. 1989;70:869-879. – reference: 6. Elion GB, Furman PA, Fyfe JA, et al. Selectivity of action of an antiherpetic agent, 9-(2-hydroxyethoxymethyl) guanine. Proc Natl Acad Sci U S A. 1977;74:5716-5720. – reference: 14. Bestman-Smith J, Schmit I, Papadopoulou B, et al. Highly reliable heterologous system for evaluating resistance of clinical herpes simplex virus isolates to nucleoside analogues. J Virol. 2001;75:3105-3110. – reference: 28. Saijo M, Suzutani T, Mizuta K, et al. Characterization and susceptibility to antiviral agents of herpes simplex virus type 1 containing a unique thymidine kinase gene with an amber codon between the first and the second initiation codons. Arch Virol. 2008;153:303-314. – reference: 18. Collins P, Larder BA, Oliver NM, et al. Characterization of a DNA polymerase mutant of herpes simplex virus from a severely immunocompromised patient receiving acyclovir. J Gen Virol. 1989;70:375-382. – reference: 13. Sasadeusz JJ, Tufaro F, Safrin S, et al. Homopolymer mutational hot spots mediate herpes simplex virus resistance to acyclovir. J Virol.1997;71:3872-3878. – reference: 30. Reed LJ, Muench H. A simple method of estimating fifty percent endpoint. Am J Hyg. 1938;27:493-497. – reference: 36. Loret S, Lippé R. Biochemical analysis of infected cell polypeptide (ICP)0, ICP4, UL7 and UL23 incorporated into extracellular herpes simplex virus type 1 virions. J Gen Virol. 2012;93:624-634. – reference: 23. Grey F, Sowa M, Collins P, et al. Characterization of a neurovirulent aciclovir-resistant variant of herpes simplex virus. J Gen Virol. 2003;84:1403-1410. – reference: 9. Darby G, Field HJ, Salisbury SA. Altered substrate specificity of herpes simplex virus thymidine kinase confers acyclovir resistance. Nature.1981;289:81-83. – reference: 24. Huang CY, Yao HW, Wang LC, et al. Thymidine kinase-negative herpes simplex virus 1 can efficiently establish persistent infection in neural tissues of nude mice. J Virol. 2017;91:e01979-16. – reference: 1. Gaudreau A, Hill E, Balfour Jr HH, et al. Phenotypic and genotypic characterization of acyclovir-resistant herpes simplex viruses from immunocompromised patients. J Infect Dis. 1998;178:297-303. – reference: 31. Ebeling SB, Eric Borst HP, Simonetti ER, et al. Development and application of quantitative real time PCR and RT-PCR assays that discriminate between the full-length and truncated herpes simplex virus thymidine kinase gene. J Virol Methods. 2003;109:177-186. – reference: 21. Suzutani T, Koyano S, Takada M, et al. Analysis of the relationship between cellular thymidine kinase activity and virulence of thymidine kinase-negative herpes simplex virus types 1 and 2. Microbiol Immunol. 1995;39:787-794. – ident: 37 doi: 10.1128/JVI.01440-13 – ident: 11 doi: 10.1099/0022-1317-64-3-523 – ident: 6 doi: 10.1073/pnas.74.12.5716 – ident: 3 doi: 10.1128/JCM.42.1.242-249.2004 – ident: 27 doi: 10.1002/(SICI)1096-9071(199908)58:4<387::AID-JMV11>3.0.CO;2-K – ident: 16 doi: 10.1016/j.antiviral.2010.03.002 – ident: 20 doi: 10.1099/0022-1317-70-4-869 – ident: 9 doi: 10.1038/289081a0 – ident: 1 doi: 10.1086/515626 – ident: 13 doi: 10.1128/jvi.71.5.3872-3878.1997 – ident: 19 doi: 10.1128/AAC.17.2.209 – ident: 25 doi: 10.1186/s12985-017-0728-2 – ident: 34 doi: 10.1017/S0022172400025109 – ident: 2 doi: 10.1016/j.antiviral.2003.08.018 – ident: 29 doi: 10.1128/JVI.77.2.1382-1391.2003 – ident: 5 doi: 10.1046/j.1365-2133.1998.02374.x – ident: 24 doi: 10.1128/JVI.01979-16 – ident: 4 doi: 10.1093/infdis/jix042 – ident: 18 doi: 10.1099/0022-1317-70-2-375 – ident: 7 doi: 10.1016/S0021-9258(17)34236-9 – ident: 22 doi: 10.1002/jmv.1890430319 – ident: 30 doi: 10.1093/oxfordjournals.aje.a118408 – ident: 12 doi: 10.1016/S0166-3542(85)80003-6 – ident: 15 doi: 10.1016/S1386-6532(02)00263-9 – ident: 36 doi: 10.1099/vir.0.039776-0 – ident: 35 doi: 10.1128/JVI.01161-19 – ident: 31 doi: 10.1016/S0166-0934(03)00069-7 – ident: 14 doi: 10.1128/JVI.75.7.3105-3110.2001 – ident: 10 doi: 10.1128/AAC.31.7.1117 – ident: 32 doi: 10.1128/AAC.35.11.2322 – ident: 23 doi: 10.1099/vir.0.18881-0 – ident: 21 doi: 10.1111/j.1348-0421.1995.tb03271.x – ident: 17 doi: 10.1016/0042-6822(85)90009-1 – ident: 28 doi: 10.1007/s00705-007-1096-9 – ident: 33 doi: 10.3389/fmicb.2019.00941 – ident: 8 doi: 10.1128/AAC.23.5.676 – ident: 26 doi: 10.7883/yoken.JJID.2020.313 |
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| Snippet | Herpes simplex virus 1 (HSV-1)-TK (8UAG) expresses a truncated thymidine kinase (TK) translated from the second initiation codon due to a stop codon (UAG) at... Herpes simplex virus 1 (HSV-1)-TK(8UAG) expresses a truncated thymidine kinase (TK) translated from the second initiation codon due to a stop UAG codon at the... |
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| SubjectTerms | Acyclovir acyclovir resistance amber mutation Gene expression Herpes simplex herpes simplex virus 1 Herpes viruses Kinases Lethal dose Sensitivity Statistical analysis Stop codon Thymidine Thymidine kinase viral thymidine kinase Virulence Viruses |
| Title | Virulence of Herpes Simplex Virus 1 Harboring a UAG Stop Codon between the First and Second Initiation Codon in the Thymidine Kinase Gene |
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