Novel Intersubunit Interaction Critical for HIV-1 Core Assembly Defines a Potentially Targetable Inhibitor Binding Pocket

Author:

Craveur Pierrick12,Gres Anna T.345,Kirby Karen A.367,Liu Dandan36,Hammond John A.1,Deng Yisong1,Forli Stefano1,Goodsell David S.18,Williamson James R.1,Sarafianos Stefan G.3679,Olson Arthur J.1

Affiliation:

1. Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA

2. Synsight, Évry, France

3. Christopher S. Bond Life Sciences Center, University of Missouri, Columbia, Missouri, USA

4. Department of Chemistry, University of Missouri, Columbia, Missouri, USA

5. Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California, USA

6. Department of Molecular Microbiology & Immunology, University of Missouri School of Medicine, Columbia, Missouri, USA

7. Laboratory of Biochemical Pharmacology, Department of Pediatrics, Emory University School of Medicine, Atlanta, Georgia, USA

8. Center for Integrative Proteomics Research, Rutgers State University, Piscataway, New Jersey, USA

9. Department of Biochemistry, University of Missouri, Columbia, Missouri, USA

Abstract

Precise assembly and disassembly of the HIV-1 capsid core are key to the success of viral replication. The forces that govern capsid core formation and dissociation involve intricate interactions between pentamers and hexamers formed by HIV-1 CA. We identified one particular interaction between E28 of one CA and K30′ of the adjacent CA that appears more frequently in pentamers than in hexamers and that is important for capsid assembly. Targeting the corresponding site could lead to the development of antivirals which disrupt this interaction and affect capsid assembly.

Funder

HHS | NIH | National Institute of Allergy and Infectious Diseases

HHS | NIH | National Institute of General Medical Sciences

Publisher

American Society for Microbiology

Subject

Virology,Microbiology

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