Skip to main content
Figure 4 | Veterinary Research

Figure 4

From: The serine-48 residue of nucleolar phosphoprotein nucleophosmin-1 plays critical role in subcellular localization and interaction with porcine circovirus type 3 capsid protein

Figure 4

Serine-48 of NPM1 is critical for binding to PCV3 Cap. A Schematic representation of the OligoD, HistonD, and NBD of NPM1 and their truncation mutants used in this study. B, C The OligoD of NPM1 (aa 1–117) interacted with PCV3 Cap. HEK293T cells were cotransfected with plasmid GFP-NPM1-WT or serial GFP-NPM1 truncated mutants D1 to D6, along with Flag-PCV3-Cap and Flag-gst-PCV3-Cap expression vectors. The cell lysates were subjected to immunoprecipitation or GST pull-down and immunoblotting using the indicated antibodies. D Prediction of binding pattern of N-terminal OligoD from NPM1 with NoLS of PCV3 Cap using PyMOL software. E The N-terminal amino acid sequence of the OligoD of NPM1. Serine (S) or threonine (T) residues are marked in red. F, G Mapping the crucial amino acids of OligoD responsible for binding to PCV3 Cap. HEK293T cells were cotransfected with NPM1 or NPM1 mutants (-S48A, -S48E, -S88A, -S88E, -T95A, or -T95D), along with Flag-PCV3-Cap and Flag-gst-PCV3-Cap expression vectors, and the cell lysates were subjected to immunoprecipitation or GST pull-down and immunoblotting using the indicated antibodies.

Back to article page

Veterinary Research

ISSN: 1297-9716