Cleavage at the nsp5-nsp6 site of SARS-CoV-2 main protease intermediate precursor is faster from a monomer than a dimer form.

Annie Aniana, Nashaat T Nashed, Rodolfo Ghirlando, Dipendra Bhandari, Andrey Kovalevsky, John M Louis

Abstract read

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Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

6 authors.

Annie AnianaLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, DHHS, Bethesda, Maryland, USA.

Nashaat T NashedLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, DHHS, Bethesda, Maryland, USA.

Rodolfo GhirlandoLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, DHHS, Bethesda, Maryland, USA.

Dipendra BhandariNeutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.

Andrey KovalevskyNeutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.

John M LouisLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, DHHS, Bethesda, Maryland, USA. Electronic address: johnl@niddk.nih.gov.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Our previous studies of severe acute respiratory syndrome coronavirus 2 main protease (MPro) precursor monomer indicate that the initial N-terminal nonstructural protein (nsp)4/nsp5 cleavage occurs intramolecularly, with a small fraction of the active site loop equilibrium being in the active state. To understand the influence of dimer formation of MPro upon N-terminal cleavage on the subsequent C-terminal nsp5/nsp6 intermolecular cleavage kinetics, the stepwise processing of a monomeric, inactive precursor containing the native terminal cleavage sites of MPro (MBP-

Indexed as

Coronavirus 3C ProteasesSARS-CoV-2Viral Nonstructural ProteinsCatalytic DomainKineticsMutationProtein MultimerizationCoronavirus 3C ProteasesViral Nonstructural ProteinsAlphaFold 3 modelsenzyme kineticsmonomer–dimer equilibriumMPro precursornsp5–nsp6 cleavageprotease processing mechanismsSARS-CoV-2 main proteaseX-ray structure

Identifiers

PMID41866037

DOI10.1016/j.jbc.2026.111395

PMCPMC13125995

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LicenceCC BY-NC-ND

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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.