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• W3083763518 abstract "Besides the common Fc receptor (FcR)-mediated mechanism of antibody-dependent enhancement (ADE), Ebola virus (EBOV) is known to utilize the complement component C1q for ADE of infection. This mechanism is FcR-independent and mediated by cross-linking of virus-antibody-C1q complexes to cell surface C1q receptors, leading to enhanced viral entry into cells. Using confocal microscopy, we found that virus-like particles (VLPs) consisting of EBOV glycoprotein, nucleoprotein, and matrix protein attached to the surface of human kidney 293 cells more efficiently in the presence of an ADE monoclonal antibody and C1q than with the antibody or C1q alone, and that there was no significant difference in the efficiency of VLP uptake into endosomes between the C1q-mediated ADE and non-ADE entry. Accordingly, both ADE and non-ADE infection were similarly decreased by inhibitors of the signaling pathways known to be required for endocytosis. These results suggest that C1q-mediated ADE of EBOV infection is simply caused by increased attachment of virus particles to the cell surface, which is distinct from the mechanism of FcR-mediated ADE requiring intracellular signaling to promote phagocytosis/macropinocytosis." @default.
• W3083763518 created "2020-09-11" @default.
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• W3083763518 date "2020-09-04" @default.
• W3083763518 modified "2023-10-16" @default.
• W3083763518 title "A complement component C1q-mediated mechanism of antibody-dependent enhancement of Ebola virus infection" @default.
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• W3083763518 doi "https://doi.org/10.1371/journal.pntd.0008602" @default.
• W3083763518 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7497997" @default.
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• W3083763518 hasPublicationYear "2020" @default.
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