prikaz prve stranice dokumenta Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus
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Scientific paper - Original scientific paper
Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus
Antiviral Research, 36 (1997), 1; 35-42. https://doi.org/10.1016/S0166-3542(97)00034-X
Zimmermann, Albert; Michel, Detlef; Pavić, Ivica; Hampl, Walter; Luske, Anke; Neyts, Johan; De Clercq, Erik; Mertens, Thomas

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Zimmermann, A., Michel, D., Pavić, I., Hampl, W., Luske, A., Neyts, J. ... Mertens, T. (1997). Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus. Antiviral Research, 36. (1), 35-42. doi: 10.1016/S0166-3542(97)00034-X

Zimmermann, Albert, et al. "Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus." Antiviral Research, vol. 36, no. 1, 1997, pp. 35-42. https://doi.org/10.1016/S0166-3542(97)00034-X

Zimmermann, Albert, Detlef Michel, Ivica Pavić, Walter Hampl, Anke Luske, Johan Neyts, Erik De Clercq and Thomas Mertens. "Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus." Antiviral Research 36, no. 1 (1997): 35-42. https://doi.org/10.1016/S0166-3542(97)00034-X

Zimmermann, A., et al. (1997) 'Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus', Antiviral Research, 36(1), pp. 35-42. doi: 10.1016/S0166-3542(97)00034-X

Zimmermann A, Michel D, Pavić I, Hampl W, Luske A, Neyts J, and sur.. Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus. Antiviral Research [Internet]. 1997 [cited 2024 November 23];36(1):35-42. doi: 10.1016/S0166-3542(97)00034-X

A. Zimmermann, et al., "Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus", Antiviral Research, vol. 36, no. 1, pp. 35-42, 1997. [Online]. Available at: https://urn.nsk.hr/urn:nbn:hr:184:740874. [Accessed: 23 November 2024]

Metadata
Title (english)Phosphorylation of aciclovir, ganciclovir, penciclovir and S2242 by the cytomegalovirus UL97 protein: a quantitative analysis using recombinant vaccinia virus
AuthorAlbert Zimmermann
AuthorDetlef Michel
AuthorIvica Pavić
AuthorWalter Hampl
AuthorAnke Luske
AuthorJohan Neyts
AuthorErik De Clercq
AuthorThomas Mertens
Author's institutionUniversity of Rijeka
Faculty of Medicine
(Department of Infectious Diseases)
Scientific / art field,
discipline and subdiscipline		BIOMEDICINE AND HEALTHCARE
Basic Medical Sciences
Abstract (english)
We used recombinant vaccinia viruses (rVV) containing the UL97 open reading frame (ORF) of the human cytomegalovirus (HCMV) to investigate the UL97-dependent phosphorylation of different nucleoside analogs. The rVV T1 expressed the wild-type UL97 protein whereas rVV A5 contained a 12 bp deletion in the UL97 which had been known to be responsible for resistance of HCMV to ganciclovir (GCV). The rVV T1opal was generated which contained a stop codon at position 1089 of the UL97 ORF and which expressed a truncated UL97 protein. We quantitatively analyzed the capability of these rVVs to phosphorylate GCV, penciclovir (PCV), aciclovir (ACV) and 2-amino-7-[(1, 3-dihydroxy-2-propoxy)methyl] purine (S2242) as well as the natural nucleosides deoxycytidine and deoxythymidine. Moreover, we compared their phosphorylating capability with that of herpes simplex virus type 1 strains. In thymidine kinase (TK)-deficient 143B cells infected with rVV T1, the three compounds GCV, ACV and PCV were phosphorylated with different efficiency whereas in cells infected with the rVV A5 a markedly reduced but not completely abolished phosphorylation of these compounds was observed. In rVV T1opal-infected cells no specific phosphorylation of the compounds was detectable at all. Neither S2242 nor the natural substrates of TKs were phosphorylated by any of the vaccinia recombinants. The rVVs proved to be a suitable tool for analysis of UL97-dependent phosphorylation of nucleoside analogs and also allowed to quantitatively study the influence of UL97 mutations on drug phosphorylation.
Keywords (english)
Languageenglish
Publication typeScientific paper - Original scientific paper
Publication statusPublished
Peer reviewPeer review - international
Publication versionPublished version
Journal titleAntiviral Research
Numberingvol. 36, no. 1, pp. 35-42
p-ISSN0166-3542
DOIhttps://doi.org/10.1016/S0166-3542(97)00034-X
URN:NBNurn:nbn:hr:184:740874
Publication1997
Document URLhttp://bib.irb.hr/811823
Type of resourceText
Access conditionsInstitutional access
Terms of useLicence In copyright icon
Created on2022-04-20 14:05:48