About: Host-Primed Ebola Virus GP Exposes a Hydrophobic NPC1 Receptor-Binding Pocket, Revealing a Target for Broadly Neutralizing Antibodies

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About: Host-Primed Ebola Virus GP Exposes a Hydrophobic NPC1 Receptor-Binding Pocket, Revealing a Target for Broadly Neutralizing Antibodies Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Host-Primed Ebola Virus GP Exposes a Hydrophobic NPC1 Receptor-Binding Pocket, Revealing a Target for Broadly Neutralizing Antibodies
Creator	Palese, Peter Chandran, Kartik Ndungo, Esther Fusco, Marnie Bale, Shridhar Bornholdt, Zachary Crowe, James Flyak, Andrew Saphire, Erica
Source	PMC
abstract	The filovirus surface glycoprotein (GP) mediates viral entry into host cells. Following viral internalization into endosomes, GP is cleaved by host cysteine proteases to expose a receptor-binding site (RBS) that is otherwise hidden from immune surveillance. Here, we present the crystal structure of proteolytically cleaved Ebola virus GP to a resolution of 3.3 Å. We use this structure in conjunction with functional analysis of a large panel of pseudotyped viruses bearing mutant GP proteins to map the Ebola virus GP endosomal RBS at molecular resolution. Our studies indicate that binding of GP to its endosomal receptor Niemann-Pick C1 occurs in two distinct stages: the initial electrostatic interactions are followed by specific interactions with a hydrophobic trough that is exposed on the endosomally cleaved GP(1) subunit. Finally, we demonstrate that monoclonal antibodies targeting the filovirus RBS neutralize all known filovirus GPs, making this conserved pocket a promising target for the development of panfilovirus therapeutics.
has issue date	2016-02-23(xsd:dateTime)
bibo:doi	10.1128/mbio.02154-15
bibo:pmid	26908579
has license	cc-by-nc-sa
sha1sum (hex)	3f704d2ac81e0dc4e9e74ffd7d25f790baa6ebe1
schema:url	https://doi.org/10.1128/mbio.02154-15
resource representing a document's title	Host-Primed Ebola Virus GP Exposes a Hydrophobic NPC1 Receptor-Binding Pocket, Revealing a Target for Broadly Neutralizing Antibodies
has PubMed Central identifier	PMC4791852
has PubMed identifier	26908579
schema:publication	mBio
resource representing a document's body	covid:3f704d2ac81e0dc4e9e74ffd7d25f790baa6ebe1#body_text
is schema:about of	named entity 'Ebola virus' named entity 'interactions' named entity 'Target' covid:arg/3f704d2ac81e0dc4e9e74ffd7d25f790baa6ebe1 named entity 'targeting' named entity 'filovirus' named entity 'conjunction' named entity 'neutralize' named entity 'monoclonal antibodies' named entity 'panel' named entity 'RBS' named entity 'viral' named entity 'Our' named entity 'binding' named entity 'endosomal' named entity 'filovirus' named entity 'receptor' named entity 'pseudotyped viruses' named entity 'host cells' named entity 'receptor' named entity 'virus' named entity 'Receptor' named entity 'VSV' named entity 'PBS' named entity 'disulfide bridge' named entity 'Infection' named entity 'W86' named entity 'membrane fusion' named entity 'wild type' named entity 'antibody' named entity 'mutation' named entity 'EBOV' named entity 'EBOV' named entity 'eGFP' named entity 'ebolaviruses' named entity 'EBOV' named entity 'infectivity' named entity 'mutation' named entity 'EBOV' named entity 'antibody' named entity 'substrate' named entity 'ebolaviruses' named entity 'hydrophobic' named entity 'DMEM' named entity 'MAb' named entity 'phosphoramidon' named entity 'binding site' named entity 'glycan' named entity 'Thermo Scientific' named entity 'Tris-buffered saline' named entity 'Marburg virus' named entity 'cleavage' named entity 'Vero' named entity 'NIAID' named entity 'hydrophobic' named entity 'viral membrane' named entity 'receptor binding' named entity 'Flyak' named entity 'EBOV' named entity 'endosomal' named entity 'virions' named entity 'single point mutation' named entity 'infection' named entity 'EBOV' named entity 'NPC1' named entity 'cross-reacts' named entity 'NPC1' named entity 'PHASER' named entity 'EBOV' named entity 'EBOV' named entity 'proteases' named entity 'disulfide bonds' named entity 'electrostatic interactions'

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