The viral protein corona directs viral pathogenesis and amyloid aggregation.

Ezzat K, Pernemalm M, Pålsson S, Roberts TC, Järver P, Dondalska A, Bestas B, Sobkowiak MJ, Levänen B, Sköld M, Thompson EA, Saher O, Kari OK, Lajunen T, Sverremark Ekström E, Nilsson C, Ishchenko Y, Malm T, Wood MJA, Power UF, Masich S, Lindén A, Sandberg JK, Lehtiö J, Spetz AL, El Andaloussi S

Nat Commun 10 (1) 2331 [2019-05-27; online 2019-05-27]

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.

Bioinformatics Compute and Storage [Service]

Proteogenomics [Technology development]

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PubMed 31133680

DOI 10.1038/s41467-019-10192-2

Crossref 10.1038/s41467-019-10192-2

10.1038/s41467-019-10192-2

pmc PMC6536551