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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.

Original publication

DOI

10.1002/1873-3468.12089

Type

Journal article

Journal

FEBS Lett

Publication Date

03/2016

Volume

590

Pages

605 - 612

Keywords

Ebola virus receptor, Ebola virus susceptibility, NPC1, NPC2, Niemann-Pick disease type C, cholesterol transport, Amino Acid Sequence, Animals, Carrier Proteins, Ebolavirus, Glycoproteins, Glycosylation, HEK293 Cells, Humans, Membrane Glycoproteins, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary