Recombinant human L-ficolin directly neutralizes hepatitis C virus entryTools Hamed, Mohamed R., Brown, Richard J.P., Zothner, Carsten, Urbanowicz, Richard A., Mason, Christopher P., Krarup, Anders, McClure, C. Patrick, Irving, William L., Ball, Jonathan K., Harrison, Mark, Hickling, Timothy P. and Tarr, Alexander W. (2014) Recombinant human L-ficolin directly neutralizes hepatitis C virus entry. Journal of Innate Immunity, 6 (5). pp. 676-684. ISSN 1662-8128 Full text not available from this repository.
Official URL: https://doi.org/10.1159/000362209
AbstractL-ficolin is a soluble pattern recognition molecule expressed by the liver that contributes to innate immune defense against microorganisms. It is well described that binding of L-ficolin to specific pathogen-associated molecular patterns activates the lectin complement pathway, resulting in opsonization and lysis of pathogens. In this study, we demonstrated that in addition to this indirect effect, L-ficolin has a direct neutralizing effect against hepatitis C virus (HCV) entry. Specific, dose-dependent binding of recombinant L-ficolin to HCV glycoproteins E1 and E2 was observed. This interaction was inhibited by soluble L-ficolin ligands. Interaction of L-ficolin with E1 and E2 potently inhibited entry of retroviral pseudoparticles bearing these glycoproteins. L-ficolin also inhibited entry of cell-cultured HCV in a calcium-dependent manner. Neutralizing concentrations of L-ficolin were found to be circulating in the serum of HCV-infected individuals. This is the first description of direct neutralization of HCV entry by a ficolin and highlights a novel role for L-ficolin as a virus entry inhibitor.
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