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Biology subjects

Lisy, S. M.

Publications and source records attributed to Lisy, S. M..

2 recordsLinked to original sources

The Incoming Influenza Genome Assembles a Host RBP Network that Orchestrates Viral RNA Synthesis

Influenza A virus (IAV) replication initiates within minutes of entry, yet the earliest host determinants acting on the incoming viral genome remain undefined. Here, using VIR-CLASP to capture protein interactions with progenitor vRNA prior to any detectable viral transcription, we map the first host-viral RNA interface and identify [~]700 human RNA binding proteins (RBPs) proactively recruited by the negative-sense genome. These factors are enriched in pathways essential for RNA metabolism, chromatin remodeling, transcriptional regulation, and nuclear condensate organization, revealing that the vRNA engages a far broader host network than previously appreciated. Functional interrogation of top candidates demonstrates that GMPS, TOP2A, SRRM2, and SPEN serve as critical proviral factors operating at distinct stages of the IAV synthesis program: GMPS and SPEN are required for efficient production of vRNA, cRNA, and mRNA; TOP2A promotes mRNA capping and early transcript accumulation; and SRRM2, together with SR-proteins, coordinates splicing of viral M and NS transcripts. These findings support a model in which the incoming vRNA acts not merely as a transcriptional template but as a scaffold that initiates assembly of nuclear machinery required for productive viral replication. By defining the pre-replicative viral RNA interactome and its functional consequences, this work exposes an unrecognized layer of host control over IAV permissivity and establishes new points of vulnerability for antiviral intervention.

molecular biology↗

Dengue and Zika virus infection are impaired by small molecule ER proteostasis regulator 147 in an ATF6-independent manner

Flaviviruses, including Dengue and Zika, are widespread human pathogens, however, no broadly active therapeutics exist to fight infection. Here, we establish the recently discovered pharmacologic modulator of ER proteostasis 147 as an effective host-centered antiviral strategy. Compound 147 reduces infection by attenuating viral replication without causing toxicity in host cells. 147 is a preferential activator of the ATF6 pathway of the unfolded protein response, which requires targeting of cysteine residues primarily on protein disulfide isomerases (PDIs). We find that the antiviral activity of 147 is independent of ATF6 induction but does require modification of reactive thiols on protein targets. Targeting PDIs using RNAi and other PDI small molecule inhibitors was unable to recapitulate the antiviral effects, suggesting additional identified protein targets of 147 may mediate the activity. Importantly, 147 can impair infection of multiple strains of Dengue and Zika virus, indicating that it is suitable as a broad-spectrum antiviral agent.

biochemistry↗