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Mechanical disassembly of human picobirnavirus like particles indicates that cargo retention is tuned by the RNA-coat protein interaction

Fig. 6 from María J. Rodríguez-Espinosa et al. 2023: Model depicting the RNA cargo retention for each VLP variant. The Δ45-CP VLP structure (A) does not show externalized cargo. The CP VLP structure (B) shows shorter N-terminals compared to the Ht-CP structure (C), which implies less RNA cargo retention compared to the Ht-CP structure. The cartoons in blue, green and pink colors represent coat protein, RNA and N-terminal, respectively. For mechanical fatigue experiments, rectangular AFM cantilevers (NANOSENSORS™, uniqprobe qp-BioAC AFM probes with three different AFM cantilevers per chip) with nominal spring constants of 0.05 and 0.1 N m−1 were used. The AFM cantilevers were calibrated using Sader's method.

The idea of using virus-like particles as nanocarriers for heterologous cargo transport and delivery requires controlling the stability of the container–cargo system.* In particular, the… Read More »Mechanical disassembly of human picobirnavirus like particles indicates that cargo retention is tuned by the RNA-coat protein interaction