L. J. Parent

Comparative analysis of retroviral Gag-host cell interactions: focus on the nuclear interactome

This study compares the nuclear interactomes of HIV-1 and RSV Gag proteins, identifying shared and unique host factors involved in nuclear processes like transcription and chromatin remodeling.

The Rous sarcoma virus Gag polyprotein forms biomolecular condensates driven by intrinsically-disordered regions

This study identifies that the Rous sarcoma virus Gag polyprotein forms biomolecular condensates driven by intrinsically disordered regions, which are involved in viral assembly.

HIV-1 Gag colocalizes with euchromatin histone marks at the nuclear periphery

This study shows HIV-1 Gag localizes to euchromatin near the nuclear periphery, preferentially associating with transcriptionally active histone marks in CD4+ T cells.

Influence of HIV-1 genomic RNA on the formation of Gagbiomolecular condensates

This study investigates how HIV-1 genomic RNA influences Gag biomolecular condensate formation and size, revealing salt-dependent effects of mutations and compartment-specific differences in host factors.

RNA binding domains of heterologous viral proteins substituted for basic residues in the RSV Gag NC domain restore specific packaging of genomic RNA

The paper replaces basic residues in RSV Gag NC with RNA-binding motifs from HIV-1 Rev and HSV ICP27 to study gRNA packaging, finding that while packaging efficiency is maintained, infectivity is lost.

TNPO3-mediated nuclear entry of the Rous sarcoma virus Gag protein is independent of the cargo-binding domain

This study identifies TNPO3 as a mediator of RSV Gag nuclear entry, showing that its interaction with Gag does not require the cargo-binding domain of TNPO3.