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TitleA small-molecule SARS-CoV-2 inhibitor targeting the membrane protein.
Journal, issue, pagesNature, Vol. 640, Issue 8058, Page 506-513, Year 2025
Publish dateMar 26, 2025
AuthorsEllen Van Damme / Pravien Abeywickrema / Yanting Yin / Jiexiong Xie / Sofie Jacobs / Mandeep Kaur Mann / Jordi Doijen / Robyn Miller / Madison Piassek / Simone Marsili / Murali Subramanian / Leah Gottlieb / Rana Abdelnabi / Michiel Van Gool / Nick Van den Broeck / Ines De Pauw / Annick Diels / Peter Vermeulen / Koen Temmerman / Trevor Scobey / Melissa Mattocks / Alexandra Schäfer / Dirk Jochmans / Steven De Jonghe / Pieter Leyssen / Winston Chiu / Mayra Diosa Toro / Marleen Zwaagstra / Anouk A Leijs / Heidi L M De Gruyter / Christophe Buyck / Klaas Van Den Heede / Frank Jacobs / Christel Van den Eynde / Laura Thijs / Valerie Raeymaekers / Seth Miller / Amanda Del Rosario / Johan Neyts / Danielle Peeters / Ralph S Baric / Frank J M van Kuppeveld / Eric J Snijder / Martijn J van Hemert / Mario Monshouwer / Sujata Sharma / Ruxandra Draghia-Akli / Anil Koul / Marnix Van Loock /
PubMed AbstractThe membrane (M) protein of betacoronaviruses is well conserved and has a key role in viral assembly. Here we describe the identification of JNJ-9676, a small-molecule inhibitor targeting the ...The membrane (M) protein of betacoronaviruses is well conserved and has a key role in viral assembly. Here we describe the identification of JNJ-9676, a small-molecule inhibitor targeting the coronavirus M protein. JNJ-9676 demonstrates in vitro nanomolar antiviral activity against SARS-CoV-2, SARS-CoV and sarbecovirus strains from bat and pangolin zoonotic origin. Using cryogenic electron microscopy (cryo-EM), we determined a binding pocket of JNJ-9676 formed by the transmembrane domains of the M protein dimer. Compound binding stabilized the M protein dimer in an altered conformational state between its long and short forms, preventing the release of infectious virus. In a pre-exposure Syrian golden hamster model, JNJ-9676 (25 mg per kg twice per day) showed excellent efficacy, illustrated by a significant reduction in viral load and infectious virus in the lung by 3.5 and 4 log-transformed RNA copies and 50% tissue culture infective dose (TCID) per mg lung, respectively. Histopathology scores at this dose were reduced to the baseline. In a post-exposure hamster model, JNJ-9676 was efficacious at 75 mg per kg twice per day even when added at 48 h after infection, when peak viral loads were observed. The M protein is an attractive antiviral target to block coronavirus replication, and JNJ-9676 represents an interesting chemical series towards identifying clinical candidates addressing the current and future coronavirus pandemics.
External linksNature / PubMed:40140563 / PubMed Central
MethodsEM (single particle)
Resolution3.06 Å
Structure data

43745

8w2e

EMDB-43745, PDB-8w2e:
SARS-CoV-2 M protein dimer in complex with JNJ-9676 and Fab-B
Method: EM (single particle) / Resolution: 3.06 Å

Chemicals

PDB-1ae8:
HUMAN ALPHA-THROMBIN INHIBITION BY EOC-D-PHE-PRO-AZALYS-ONP

Source
  • homo sapiens (human)
  • sars-cov-2 pseudovirus
KeywordsVIRAL PROTEIN/Immune System / SARS-COV-2 / M protein / Inhibitor bound complex / VIRAL PROTEIN-Immune System complex

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