Evidence map›Paper›PMID 41202142›Full record

ArticleScience advances2025

Structural basis of herpesvirus helicase-primase inhibition by pritelivir and amenamevir.

Andrey G Baranovskiy, Qixiang He, Yoshiaki Suwa, Lucia M Morstadt, Nigar D Babayeva, Ci Ji Lim, Tahir H Tahirov

Abstract read
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Andrey G BaranovskiyEppley Institute for Research in Cancer and Allied Diseases, Fred & Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE, USA.ORCID 0000-0002-8017-6932
Qixiang HeDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI, USA.ORCID 0000-0002-0738-679X
Yoshiaki SuwaEppley Institute for Research in Cancer and Allied Diseases, Fred & Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE, USA.ORCID 0009-0006-1488-3256
Lucia M MorstadtEppley Institute for Research in Cancer and Allied Diseases, Fred & Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE, USA.ORCID 0000-0002-4972-6086
Nigar D BabayevaEppley Institute for Research in Cancer and Allied Diseases, Fred & Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE, USA.ORCID 0000-0002-4410-1327
Ci Ji LimDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI, USA.ORCID 0000-0003-3327-1926
Tahir H TahirovEppley Institute for Research in Cancer and Allied Diseases, Fred & Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE, USA.ORCID 0000-0002-1238-0069

Funding

DNA Replication Machines: Structure-function Studies Administrative SupplementR35GM152032 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Tahir H Tahirov · 2024 to 2026
$1.7M
Mechanism of the Human Telomere C-Strand Fill-In Machinery Assembly and Activation at Chromosome EndsR01GM153806 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Ci Ji Lim · 2024 to 2026
$933k
NIGMS NIH HHS R01 GM153806NIGMS NIH HHS R35 GM152032
6 · The paper itself

Abstract

Widespread herpesvirus infections are associated with various diseases. DNA replication of human herpes simplex virus type 1 (HSV-1) requires a helicase-primase (HP) complex of three core proteins: UL5, UL52, and UL8. This complex unwinds viral DNA and synthesizes primers for DNA replication, making it an attractive antiviral target. Although HP inhibitors pritelivir and amenamevir were identified through screening, their binding mechanisms remain unclear. Here, we report cryo-electron microscopy structures of HSV-1 HP bound to a forked DNA template alone and in complex with pritelivir or amenamevir. The structures reveal a bilobed architecture highlighting HP coordinated action at the replication fork and providing a structural basis for HP inhibition by illustrating precisely how pritelivir and amenamevir block helicase activity. Data lay a solid foundation for the development of improved antiviral therapies.

Indexed as

Antiviral AgentsDNA HelicasesDNA PrimaseDNA ReplicationViral ProteinsVirus ReplicationAnimalsCryoelectron MicroscopyDNA, ViralHerpes SimplexHerpesvirus 1, HumanHumansMolecular Docking SimulationOxadiazolesProtein BindingSf9 CellsAntiviral AgentsASP2151DNA HelicasesDNA PrimaseDNA, Viralhelicase-primase, Human herpesvirus 1OxadiazolespritelivirSulfonamidesThiazolesViral Proteins

Identifiers

PMID41202142
PMCPMC12594203

What Socratic holds

Textmetadata
LicenceCC BY-NC
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.