Interaction between host G3BP and viral nucleocapsid protein regulates SARS-CoV-2 replication
Z. Yang, B. A. Johnson, V. A. Meliopoulos, X. Ju, P. Zhang, M. P. Hughes, J. Wu, K. P. Koreski, T.-C. Chang, G. Wu, J. Hixon, J. Duffner, K. Wong, R. Lemieux, K. G. Lokugamage, R. E. Alvardo, P. A. Crocquet-Valdes, D. H. Walker, K. S. Plante, J. A. Plante, S. C. Weaver, H. J. Kim, R. Meyers, S. Schultz-Cherry, Q. Ding, , J. P. Taylor
Abstract
G3BP1/2 are paralogous proteins that promote stress granule formation in response to cellular stresses, including viral infection. G3BP1/2 are prominent interactors of the nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). However, the functional consequences of the G3BP1-N interaction in the context of viral infection remain unclear. Here we used structural and biochemical analyses to define the residues required for G3BP1-N interaction, followed by structure-guided mutagenesis of G3BP1 and N to selectively and reciprocally disrupt their interaction. We found that mutation of F17 within the N protein led to selective loss of interaction with G3BP1 and consequent failure of the N protein to disrupt stress granule assembly. Introduction of SARS-CoV-2 bearing an F17A mutation resulted in a significant decrease in viral replication and pathogenesis in vivo, indicating that the G3BP1-N interaction promotes infection by suppressing the ability of G3BP1 to form stress granules.
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