ArticleAntimicrobial agents and chemotherapy2021
Characteristics of Helicase-Primase Inhibitor Amenamevir-Resistant Herpes Simplex Virus.
Article in Antimicrobial agents and chemotherapy, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Article
- Mechanisms of HSV-1 helicase-primase inhibition and replication fork complex assembly.bioRxiv : the preprint server for biology · 2025Article
- Structural and mechanistic insights into the herpes simplex virus type 1 helicase-primase primosome.Cell discovery · 2025Article
- Structural and mechanistic insights into herpesvirus helicase-primase and its therapeutic inhibitors.Nature microbiology · 2025Article
- Inhibiting KSHV replication by targeting the essential activities of KSHV processivity protein, PF-8.Journal of medical virology · 2024Review
- Combined use of pritelivir with acyclovir or foscarnet suppresses evolution of HSV-1 drug resistance.Virus evolution · 2024Article
- Viral replication organelles: the highly complex and programmed replication machinery.Frontiers in microbiology · 2024Review
- Current landscape in antiviral drug development against herpes simplex virus infections.Smart medicine · 2022Review
- 40 Years after the Registration of Acyclovir: Do We Need New Anti-Herpetic Drugs?International journal of molecular sciences · 2022Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The antiherpetic drug amenamevir (AMNV) inhibits the helicase-primase complex of herpes simplex virus 1 (HSV-1), HSV-2, and varicella-zoster virus directly as well as inhibiting the replication of these viruses. Although several mutated HSV viruses resistant to helicase-primase inhibitors have been reported, the mutations contributing to the resistance remain unclear, as recombinant viruses containing a single mutation have not been analyzed. We obtained AMNV-resistant viruses with amino acid substitutions by several passages under AMNV treatment. Twenty HSV-1 and 19 HSV-2 mutants with mutation(s) in UL5 helicase and/or UL52 primase, but not in cofactor UL8, were isolated. The mutations in UL5 were located downstream of motif IV, with UL5 K356N in HSV-1 and K355N in HSV-2, in particular, identified as having the highest frequency, which was 9/20 and 9/19, respectively. We generated recombinant AMNV-resistant HSV-1 with a single amino acid substitution using bacterial artificial chromosome (BAC) mutagenesis. As a result, G352C in UL5 helicase and F360C/V and N902T in UL52 primase were identified as novel mutations. The virus with K356N in UL5 showed 10-fold higher AMNV resistance than did other mutants and showed equivalent viral growth
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