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Receptor-activated human α2-macroglobulin interacts with the envelope protein of dengue virus and protects virions from temperature-induced inactivation through multivalent binding. | LitMetric

AI Article Synopsis

  • The study investigates how proteins in human plasma interact with the dengue virus (DENV), focusing on the envelope protein domain III (DIIIE2).
  • Using affinity chromatography, two novel binding proteins, serum amyloid P (SAP) and α2-macroglobulin (α2M), were identified and confirmed to specifically bind to DIIIE2.
  • The research shows that the receptor-activated form of α2M (α2M*) can bind to all four DENV serotypes, protecting the virus from inactivation and increasing its infectivity, which highlights the importance of these interactions in DENV infections.

Article Abstract

Based on the hypothesis that interactions between virions and serum components may influence the outcome of dengue virus (DENV) infections, we decided to use affinity chromatography with domain III from the envelope (E) protein of DENV2 (DIIIE2) as a ligand to isolate virus-binding proteins from human plasma. This approach yielded serum amyloid P (SAP) and α2-macroglobulin (α2M) as novel viral interactors. After confirming the specific binding of both SAP and α2M to DIIIE2 by ELISA, the latter interaction was examined in greater detail. We obtain evidence suggesting that the binding species was actually the receptor-activated form of α2M (α2M*), that α2M* could bind monovalently to recombinant domain III from all four DENV serotypes with affinities in the micromolar range ranking as DENV4>DENV1~DENV2>DENV3 and that this interaction exhibited a strong avidity effect when multivalent binding was favoured (KD 8 × 10(-8) M for DIIIE2). We also showed that α2M* bound to DENV virions of the four serotypes, protecting the virus from temperature-induced inactivation in the absence of serum and enhancing infectivity. The latter effect exhibited an ED50 of 2.9 × 10(-8) M, also suggesting an avidity effect due to multivalent binding. These results will further contribute to the characterization of the virus-host factor interaction network during human DENV infection.

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Source
http://dx.doi.org/10.1099/vir.0.068544-0DOI Listing

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