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Presence of a SARS-CoV-2 Protein Enhances Amyloid Formation of Serum Amyloid A.
Jana, Asis K; Greenwood, Augustus B; Hansmann, Ulrich H E.
  • Jana AK; Department of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
  • Greenwood AB; Department of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
  • Hansmann UHE; Department of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
J Phys Chem B ; 125(32): 9155-9167, 2021 08 19.
Article in English | MEDLINE | ID: covidwho-1347913
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ABSTRACT
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 SARS-CoV-2 protein segment on SAA amyloid formation. Sampling over 40 µs, 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.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: COVID-19 / Amyloidosis Type of study: Prognostic study Limits: Humans Language: English Journal: J Phys Chem B Journal subject: Chemistry Year: 2021 Document Type: Article Affiliation country: Acs.jpcb.1c04871

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Full text: Available Collection: International databases Database: MEDLINE Main subject: COVID-19 / Amyloidosis Type of study: Prognostic study Limits: Humans Language: English Journal: J Phys Chem B Journal subject: Chemistry Year: 2021 Document Type: Article Affiliation country: Acs.jpcb.1c04871