scholarly journals The viral protein corona directs viral pathogenesis and amyloid aggregation

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Kariem Ezzat ◽  
Maria Pernemalm ◽  
Sandra Pålsson ◽  
Thomas C. Roberts ◽  
Peter Järver ◽  
...  
2020 ◽  
Vol 16 (S2) ◽  
Author(s):  
Kariem Ezzat ◽  
Tarja Malm ◽  
Oskar Gustafsson ◽  
Anders Lindén ◽  
Samir E.L. Andaloussi

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Emily H. Pilkington ◽  
Yanting Xing ◽  
Bo Wang ◽  
Aleksandr Kakinen ◽  
Miaoyi Wang ◽  
...  

2018 ◽  
Author(s):  
Kariem Ezzat ◽  
Maria Pernemalm ◽  
Sandra Pålsson ◽  
Thomas C. Roberts ◽  
Peter Järver ◽  
...  

AbstractArtificial 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 (Aβ42), 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.


2009 ◽  
Vol 00 (00) ◽  
pp. 090918014014004-11
Author(s):  
Maria Antonietta Panaro ◽  
Rosa Calvello ◽  
Sabrina Lisi ◽  
Matteo Saccia ◽  
Antonia Cianciulli ◽  
...  

INEOS OPEN ◽  
2020 ◽  
Vol 3 ◽  
Author(s):  
S. A. Sorokina ◽  
◽  
Yu. Yu. Stroilova ◽  
V. I. Muronets ◽  
Z. B. Shifrina ◽  
...  

Among the compounds able to efficiently inhibit the amyloid aggregation of proteins and decompose the amyloid aggregates that cause neurodegenerative diseases, of particular interest are dendrimers, which represent individual macromolecules with the hypercrosslinked architectures and given molecular parameters. This short review outlines the peculiarities of the antiamyloid activity of dendrimers and discusses the effect of dendrimer structures and external factors on their antiamyloid properties. The potential of application of dendrimers in further investigations on the aggregation processes of amyloid proteins as the compounds that exhibit the remarkable antiamyloid activity is evaluated.


2019 ◽  
Vol 484 (1) ◽  
pp. 104-108
Author(s):  
G. F. Makhaeva ◽  
E. F. Shevtsova ◽  
N. P. Boltneva ◽  
N. V. Kovaleva ◽  
E. V. Rudakova ◽  
...  

This study presents the synthesis of binary tetrohydro-γ-carbolines with ditriazol spacers of varying length, which exhibit anticholinesterase and antioxidant activity, as compared to the original Dimebon prototype. Anticholinesterase activity suggests the potential ability of the new compounds to block β-amyloid aggregation induced by anticholinesterase, making them promising candidates for further research preparations for the treatment of Alzheimer's disease. Particular attention should be paid to the conjugate with an intertriazol hexamethylene spacer, which can be regarded as the leading compound in this series.


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