期刊
CELL HOST & MICROBE
卷 8, 期 2, 页码 186-195出版社
CELL PRESS
DOI: 10.1016/j.chom.2010.07.007
关键词
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资金
- National Institutes of Allergy and Infectious Diseases (NIAID)
- National Institutes of Health (NIH) [R01 AI073755]
- Midwest Regional Center of Excellence for Biodefense and Emerging Infectious Diseases Research [U54 AI057160]
- Medical Research Council [G0700859, G0801952] Funding Source: researchfish
- MRC [G0700859] Funding Source: UKRI
An intact complement system is crucial for limiting West Nile virus (WNV) dissemination. Herein, we define how complement directly restricts flavivirus infection in an antibody-independent fashion. Mannose-binding lectin (MBL) recognized N-linked glycans on the structural proteins of WNV and Dengue virus (DENV), resulting in neutralization through a C3- and C4-dependent mechanism that utilized both the canonical and bypass lectin activation pathways. For WNV, neutralization occurred with virus produced in insect cells, whereas for DENV, neutralization of insect and mammalian cell-derived virus was observed. Mechanism of action studies suggested that the MBL-dependent neutralization occurred, in part, by blocking viral fusion. Experiments in mice showed an MBL-dependent accelerated intravascular clearance of DENV or a WNV mutant with two N-linked glycans on its E protein, but not with wild-type WNV. Our studies show that MBL recognizes terminal mannose-containing carbohydrates on flaviviruses, resulting in neutralization and efficient clearance in vivo.
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