期刊
FEBS LETTERS
卷 590, 期 5, 页码 605-612出版社
WILEY
DOI: 10.1002/1873-3468.12089
关键词
cholesterol transport; Ebola virus receptor; Ebola virus susceptibility; Niemann-Pick disease type C; NPC1; NPC2
资金
- Biostruct-X project - EU seventh Framework Programme (FP7) [283570]
- Wellcome Trust [090532/Z/09/Z]
- UK Medical Research Council [MR/N00065X/1]
- Medical Research Council [G1000099, MR/N00065X/1, G1100525] Funding Source: researchfish
- MRC [MR/N00065X/1] Funding Source: UKRI
Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses. We have determined the crystal structure of glycosylated NPC1 luminal domain C and find all seven possible sites are glycosylated. Mapping the disease mutations onto the glycosylated structure reveals a potential binding face for NPC2. Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
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