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A complement component C1q-mediated mechanism of antibody-dependent enhancement of Ebola virus infection

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Title: A complement component C1q-mediated mechanism of antibody-dependent enhancement of Ebola virus infection
Authors: Furuyama, Wakako Browse this author
Nanbo, Asuka Browse this author →KAKEN DB
Maruyama, Junki Browse this author
Marzi, Andrea Browse this author
Takada, Ayato Browse this author →KAKEN DB
Issue Date: Sep-2020
Publisher: PLOS
Journal Title: PLoS neglected tropical diseases
Volume: 14
Issue: 9
Start Page: e0008602
Publisher DOI: 10.1371/journal.pntd.0008602
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. Author summary Ebola virus (EBOV) utilizes the complement component C1q for antibody-dependent enhancement (ADE) of infection. We found that an ADE antibody increased viral attachment in the presence of C1q and that there was no significant difference in the efficiency of viral 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 for endocytosis. These results suggest that C1q-mediated ADE of EBOV infection is simply caused by increased viral attachment to the cell surface, most likely via cross-linking of virus-antibody-C1q complexes to cellular C1q receptors.
Rights: https://creativecommons.org/publicdomain/zero/1.0/
Type: article
URI: http://hdl.handle.net/2115/79681
Appears in Collections:国際連携研究教育局 : GI-CoRE (Global Institution for Collaborative Research and Education : GI-CoRE) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

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