bioRxivMicrobiology
The Viral Protein Corona Directs Viral Pathogenesis and Amyloid Aggregation
K. Ezzat, M. Pernemalm, S. Palsson, T. C. Roberts, P. Jarver, A. Dondalska, B. Bestas, M. J. Sobkowiak, B. Levanen, M. Skold, E. A. Thompson, O. Saher, O. K. Kari, T. Lajunen, E. Sverremark Ekstrom, C. Nilsson, Y. Ishchenko, T. Malm, M. J. A. Wood, U. F. Power, S. Masich, A. Linden, J. K. Sandberg, J. Lehtio, A.-L. Spetz, S. E. Andaloussi
Abstract
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 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. Additionally, 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 beta peptide (A{beta}42), a major constituent of amyloid plaques in Alzheimers 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.
- organism: human
- organism: mouse
- assay: proteomics
- research focus: host-pathogen & immune response
- research focus: protein folding & dynamics
- approach: experimental assay
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