Emily Happy Miller

TL;DR: These findings support a model in which GP cleavage by endosomal cysteine proteases unmasks the binding site for NPC1, and GP–NPC1 engagement within lysosomes promotes a late step in entry proximal to viral escape into the host cytoplasm.

TL;DR: This review summarizes the understanding of the filovirus entry mechanism, with emphasis on recent findings.

TL;DR: It is found that an EboV C-peptide conjugated to the arginine-rich sequence from HIV-1 Tat specifically inhibited viral entry mediated by filovirus GP proteins and infection by authentic filoviruses.

TL;DR: VLP-based entry assays demonstrate that a GP mutant, GP-F88A, which is defective for entry into a variety of human cell types, including antigen-presenting cells (APCs), such as macrophages and dendritic cells, can mediate viral entry into mouse CD11b+ APCs, and suggest an important role for NPC1 in the differential entry of GP- F88A into mouse versus human APCs.

TL;DR: It is shown that Niemann-Pick C1-like1 (NPC1L1), an NPC1 paralog and hepatitis C virus entry factor, lacks filovirus receptor activity, and the central role of the luminal domain C of NPC1 inFilovirus entry is highlighted and the direct involvement of N–terminal domain C sequences in NPC1’s function as a filov virus receptor is revealed.