Abstract:
:Previously, we found that a ganciclovir (GCV)-resistant clinical human cytomegalovirus (HCMV) isolate had an amino acid substitution at codon 501 (Leu --> Phe) in the delta-region C of the DNA polymerase gene. DNA polymerases have now been (partially) purified from both the GCV-resistant and sensitive parental strains and the activity of DNA polymerase and 3'-5' exonuclease compared. With respect to DNA polymerase activity, the Michaelis constant (Km) and maximum velocity (Vmax) of the GCV-resistant strain for the DNA template were lower than those of the GCV-sensitive strain. With respect to 3'-5' exonuclease activity, the Km and Vmax of the GCV-resistant strain for the DNA substrate in the presence of ammonium sulfate were lower than those of the GCV-sensitive strain, while being similar in the absence of ammonium sulfate. Although the polymerase activity of the two strains showed almost the same sensitivity for the different polymerase inhibitors, the 3'-5' exonuclease activity of the GCV-resistant strain was more resistant to these inhibitors than that of the GCV-sensitive strain.
journal_name
Antiviral Resjournal_title
Antiviral researchauthors
Kariya M,Mori S,Eizuru Ydoi
10.1016/s0166-3542(00)00063-2subject
Has Abstractpub_date
2000-02-01 00:00:00pages
115-22issue
2eissn
0166-3542issn
1872-9096pii
S0166-3542(00)00063-2journal_volume
45pub_type
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pub_type: 临床试验,杂志文章,多中心研究
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pub_type: 杂志文章
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pub_type: 杂志文章,评审
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更新日期:2015-08-01 00:00:00
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更新日期:2017-02-01 00:00:00
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更新日期:2014-09-01 00:00:00
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doi:10.1016/j.antiviral.2003.07.001
更新日期:2004-01-01 00:00:00
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doi:10.1016/j.antiviral.2010.04.015
更新日期:2010-08-01 00:00:00
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