Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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




Journal article



Publication Date





605 - 612


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