About: Open and Closed Structures Reveal Allostery and Pliability in the HIV-1 Envelope Spike

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About: Open and Closed Structures Reveal Allostery and Pliability in the HIV-1 Envelope Spike 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	Open and Closed Structures Reveal Allostery and Pliability in the HIV-1 Envelope Spike
Creator	Pallesen, Jesper Copps, Jeffrey Cupo, Albert Lyumkis, Dmitry Ozorowski, Gabriel Pugach, Pavel Cottrell, Christopher Moore, John Ward, Andrew Wilson, Ian De Val, Natalia Stanfield, Robyn Torres, Jonathan
Source	Medline; PMC
abstract	For many enveloped viruses, binding to a receptor(s) on a host cell acts as a first step in a series of events culminating in fusion with the host cell membrane and transfer of genetic material for replication [for review see(1,2)]. The envelope glycoprotein (Env) trimer on the surface of HIV is responsible for receptor binding and fusion. While Env can tolerate a high degree of mutation in five variable regions (V1-V5), and also at N-linked glycosylation sites that contribute roughly half the mass of Env, the functional sites for recognition of receptor CD4 and co-receptor CXCR4/CCR5 are conserved and essential for viral fitness. Soluble SOSIP Env trimers are structural and antigenic mimics of the pre-fusion native, surface-presented Env(3,4), targets of broadly neutralizing antibodies (bnAbs). Thus, they are attractive immunogens for vaccine development [for review see(5–8)]. Here we present high-resolution cryo-electron microscopy (cryoEM) structures of subtype B B41 SOSIP Env trimers in complex with CD4 and antibody 17b, or with antibody b12, at resolutions of ~3.7 Å and ~3.6 Å, respectively, and compare them to cryoEM reconstructions of ligand-free B41 SOSIP Env trimers or in complex with either CD4 or CD4bs antibody PGV04, at ~5.6 Å, ~5.2 Å and ~7.4 Å, respectively. Consequently, we present the most complete description and understanding of the CD4/17b-induced intermediate and provide the molecular basis of the receptor-binding induced conformational change required for HIV-1 entry into host cells. Both CD4 and b12 induce large, previously uncharacterized conformational rearrangements in the gp41 subunits, and the fusion peptide becomes more buried in a newly formed pocket. These structures provide key details on the biological function of the type I viral fusion machine from HIV-1 as well as new templates for inhibitor design.
has issue date	2017-07-12(xsd:dateTime)
bibo:doi	10.1038/nature23010
bibo:pmid	28700571
has license	no-cc
sha1sum (hex)	aeb2fd035cedb1adb0f4498c351310f5f2fea5a8
schema:url	https://doi.org/10.1038/nature23010
resource representing a document's title	Open and Closed Structures Reveal Allostery and Pliability in the HIV-1 Envelope Spike
has PubMed Central identifier	PMC5538736
has PubMed identifier	28700571
schema:publication	Nature
resource representing a document's body	covid:aeb2fd035cedb1adb0f4498c351310f5f2fea5a8#body_text
is schema:about of	named entity 'events' named entity 'transfer' named entity 'Env' named entity 'PLIABILITY' named entity 'ALLOSTERY' named entity 'ENVELOPE' named entity 'SPIKE' named entity 'OPEN' named entity 'FUSION' named entity 'CONDITIONS' named entity 'CD4' named entity 'SOLUBLE' named entity 'MASS' named entity 'PRINT' named entity 'VARIABLE' named entity 'CCR5' named entity 'ENVELOPE GLYCOPROTEIN' named entity 'REGIONS' named entity 'STRUCTURAL' named entity 'TRANSFER' named entity 'FIRST STEP' named entity 'CONSERVED' named entity 'N-LINKED GLYCOSYLATION' named entity 'MUTATION' named entity 'REVIEW' named entity 'ESSENTIAL' named entity 'HALF' named entity '28S' named entity 'CULMINATING' named entity 'USERS' named entity 'SUBJECT' named entity 'EVENTS' named entity 'HIV' named entity 'HTTP' named entity 'CLOSED' named entity 'REVEAL' named entity 'HIV-1' named entity 'STRUCTURES' named entity 'RECOGNITION' named entity 'USE' named entity 'SURFACE' named entity 'COPY' named entity 'TRIMER' named entity 'BINDING' named entity 'NATURE' named entity 'GENETIC MATERIAL' named entity 'TEXT' named entity 'CONTRIBUTE ' named entity 'VIRUSES' named entity 'ENV' named entity 'CXCR4' named entity 'REPLICATION' named entity 'HOST CELL' named entity 'ACADEMIC' named entity 'FUNCTIONAL SITES' named entity 'VIRAL FITNESS' named entity 'MAY VIEW' named entity 'HOST CELL MEMBRANE' named entity 'RESEARCH' named entity 'SERIES' named entity 'RESPONSIBLE' named entity 'RECEPTOR' named entity 'DOCUMENTS' named entity 'RECEPTOR BINDING' named entity 'SITES' named entity 'DATA' named entity 'CONTENT' named entity 'ACTS' named entity 'HIGH'

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