Presence of a SARS-CoV-2 Protein Enhances Amyloid Formation of Serum Amyloid A

被引:33
作者
Jana, Asis K. [1 ]
Greenwood, Augustus B. [1 ]
Hansmann, Ulrich H. E. [1 ]
机构
[1] Univ Oklahoma, Dept Chem & Biochem, Norman, OK 73019 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
AA AMYLOIDOSIS; AGGREGATION; MECHANISM; FRAGMENT;
D O I
10.1021/acs.jpcb.1c04871
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
A marker for the severeness and disease progress of COVID-19 is overexpression of serum amyloid A (SAA) to levels that in other diseases are associated with a risk for SAA amyloidosis. To understand whether SAA amyloidosis could also be a long-term risk of SARS-CoV-2 infections, we have used long all-atom molecular dynamic simulations to study the effect of a SARSCoV-2 protein segment on SAA amyloid formation. Sampling over 40 mu s, we find that the presence of the nine-residue segment SK9, located at the C-terminus of the envelope protein, increases the propensity for SAA fibril formation by three mechanisms: it reduces the stability of the lipid-transporting hexamer shifting the equilibrium toward monomers, it increases the frequency of aggregation-prone configurations in the resulting chains, and it raises the stability of SAA fibrils. Our results therefore suggest that SAA amyloidosis and related pathologies may be a long-term risk of SARS-CoV-2 infections.
引用
收藏
页码:9155 / 9167
页数:13
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