Dengue virus capsid protein interacts specifically with very low-density lipoproteins

Faustino, André F.; Carvalho, Filomena A.; Martins, Ivo C.; Castanho, Miguel A. R. B.; Mohana-Borges, Ronaldo; Almeida, Fábio C. L.; Da Poian, Andrea T.; Santos, Nuno C.

http://hdl.handle.net/10451/10709

Use this identifier to reference this record.

Name:	Description:	Size:	Format:
Dengue_VLDL.pdf		1.33 MB	Adobe PDF	Download

Send Feedback

Authors

Faustino, André F.

Carvalho, Filomena A.

Martins, Ivo C.

Castanho, Miguel A. R. B.

Mohana-Borges, Ronaldo

Almeida, Fábio C. L.

Da Poian, Andrea T.

Santos, Nuno C.

Abstract(s)

Dengue affects millions of people worldwide. No specific treatment is currently available, in part due to an incomplete understanding of the viral components' interactions with host cellular structures. We tested dengue virus (DENV) capsid protein (C) interaction with low- and very low-density lipoproteins (LDL and VLDL, respectively) using atomic force microscopy-based force spectroscopy, dynamic light scattering, NMR and computational analysis. Data reveal a specific DENV C interaction with VLDL, but not LDL. This binding is potassium-dependent and involves the DENV C N-terminal region, as previously observed for the DENV C-lipid droplets (LDs) interaction. A successful inhibition of DENV C-VLDL binding was achieved with a peptide drug lead. The similarities between LDs and VLDL, and between perilipin 3 (DENV C target on LDs) and ApoE, indicate ApoE as the molecular target on VLDL. We hypothesize that DENV may form lipoviroparticles, which would constitute a novel step on DENV life cycle.