Evidence map›Paper›PMID 42443199›Full record

ArticleNature communications2026

Antibody reveals conformational latch regulating dimerization in β- and γ-herpesvirus proteases.

Marcell A Zimanyi, Kaitlin R Hulce, Markus-Frederik Bohn, Jordan Norman, Peter J Rohweder, Tyler C Detomasi, Yifan Cheng, Charles S Craik

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Marcell A ZimanyiDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA.ORCID http://orcid.org/0000-0003-1981-1244
Kaitlin R HulceChemistry and Chemical Biology Graduate Program, University of California, San Francisco, CA, USA.
Markus-Frederik BohnDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA.
Jordan NormanMedical Scientist Training Program, University of California, San Francisco, CA, USA.
Peter J RohwederDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA.ORCID http://orcid.org/0000-0002-3194-689X
Tyler C DetomasiDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA.
Yifan ChengDepartment of Biochemistry and Biophysics, University of California, San Francisco, CA, USA. yifan.cheng@ucsf.edu.ORCID http://orcid.org/0000-0001-9535-0369
Charles S CraikDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA. charles.craik@ucsf.edu.ORCID http://orcid.org/0000-0001-7704-9185

Funding

Project 3U54AI170792 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Nevan J Krogan · 2022 to 2026
$35.7M
NIAID NIH HHS U54 AI170792U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases (NIAID) U54AI170792
6 · The paper itself

Abstract

Human herpesvirus (HHV) replication depends on the HHV protease (HHV Pr), an enzyme essential for capsid maturation. Because HHV Pr must transition from an inactive monomer to an active dimer, disrupting dimerization is a promising antiviral strategy. We isolate Fab5, a conformationally selective antibody from a naïve Fab-phage library that recognizes monomeric human cytomegalovirus protease (HCMV) Pr. A 2.6 Å cryo-EM structure reveals Fab5 binds a "latch loop" distal to the active site and dimer interface that secures the C-terminal tail in dimers. Structure-guided mutagenesis in both HCMV Pr and Kaposi's Sarcoma-associated herpesvirus (KSHV) Pr confirms the functional importance of a 3-residue motif present in β- and γ-HHV Pr latch loops, validating the mechanistic role of the latch loop in dimerization and activity. Because the latch loop is structurally conserved in all HHV Prs, the cryptic sites they form present an avenue for allosteric inhibitor development.

Indexed as

CytomegalovirusHerpesvirus 8, HumanImmunoglobulin Fab FragmentsPeptide HydrolasesViral ProteinsCryoelectron MicroscopyHumansModels, MolecularProtein ConformationProtein MultimerizationImmunoglobulin Fab FragmentsPeptide HydrolasesViral Proteins

Identifiers

PMID42443199
PMCPMC13486704

What OpenQuestion holds

Textmetadata
Read underepoch 390

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 OpenQuestion graph.