Journal
JOURNAL OF INNATE IMMUNITY
Volume 6, Issue 5, Pages 676-684Publisher
KARGER
DOI: 10.1159/000362209
Keywords
Hepatitis C virus; Ficolin; Virus entry; Neutralization; Glycosylation
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Funding
- Egyptian government, EU FP7 [Health-F4-2012-305600]
- MRC DPFS [G0801169]
- MRC [G0801169] Funding Source: UKRI
- Medical Research Council [G0801169] Funding Source: researchfish
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L-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. (C) 2014 S. Karger AG, Basel
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