Journal Article

The viral protein corona directs viral pathogenesis and amyloid aggregation

Kari, Otto K., Power, Ultan F., Thompson, Elizabeth A., Nilsson, Caroline, Ezzat, Kariem, EL Andaloussi, Samir, Ishchenko, Yevheniia, Pålsson, Sandra, Levänen, Bettina, Lindén, Anders, Dondalska, Aleksandra, Lajunen, Tatu, Bestas, Burcu, Järver, Peter, Pernemalm, Maria, Sverremark Ekström, Eva, Malm, Tarja, Masich, Sergej, Lehtiö, Janne, Roberts, Thomas C., Wood, Matthew J. A., Saher, Osama, Spetz, Anna-Lena, Sobkowiak, Michal J., Sköld, Magnus, Sandberg, Johan K.

2019

Overview

Artificial nanoparticles accumulate a protein corona layer in biological fluids, which significantly influences their bioactivity. As nanosized obligate intracellular parasites, viruses share many biophysical properties with artificial nanoparticles in extracellular environments and here we show that respiratory syncytial virus (RSV) and herpes simplex virus type 1 (HSV-1) accumulate a rich and distinctive protein corona in different biological fluids. Moreover, we show that corona pre-coating differentially affects viral infectivity and immune cell activation. In addition, we demonstrate that viruses bind amyloidogenic peptides in their corona and catalyze amyloid formation via surface-assisted heterogeneous nucleation. Importantly, we show that HSV-1 catalyzes the aggregation of the amyloid β-peptide (Aβ 42 ), a major constituent of amyloid plaques in Alzheimer’s disease, in vitro and in animal models. Our results highlight the viral protein corona as an acquired structural layer that is critical for viral–host interactions and illustrate a mechanistic convergence between viral and amyloid pathologies. The protein corona around artificial nanoparticles is known to influence activity and biological fate, the formation around viruses is less well understood. Here, the authors observe the formation of protein corona on viruses and study the effects this corona has on viral infectivity and on amyloid protein assembly.

• Publisher: Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
• Subject: 13/31 / 13/51 / 14 / 14/28 / 49 / 631/326/596/2555 / 631/378/1689/1283 / 631/61/350 / 82/58 / Agglomeration / Alzheimer Disease - immunology / Alzheimer Disease - pathology / Alzheimer Disease - virology / Amyloid beta-Peptides - metabolism / Amyloidogenesis / Animal models / Animals / Biological activity / Bronchoalveolar Lavage Fluid - virology / Cell activation / Cell Line, Tumor / Chlorocebus aethiops / Computational fluid dynamics / Disease Models, Animal / Female / Healthy Volunteers / Herpes simplex / Herpes Simplex - blood / Herpes Simplex - immunology / Herpes Simplex - pathology / Herpes viruses / Herpesvirus 1, Human - immunology / Herpesvirus 1, Human - pathogenicity / Host-Pathogen Interactions - immunology / Humanities and Social Sciences / Humans / Immune system / Infectivity / Male / Mice / Mice, Transgenic / multidisciplinary / Nanoparticles / Nucleation / Parasites / Pathogenesis / Peptide Fragments - metabolism / Peptides / Protein Aggregates - immunology / Protein Corona - immunology / Proteins / Respiratory syncytial virus / Respiratory Syncytial Virus Infections - immunology / Respiratory Syncytial Virus Infections - pathology / Respiratory Syncytial Virus Infections - virology / Respiratory Syncytial Virus, Human - immunology / Respiratory Syncytial Virus, Human - pathogenicity / Science / Science (multidisciplinary) / Senile plaques / Vero Cells / Viruses / β-Amyloid