About: Structural Bases of Coronavirus Attachment to Host Aminopeptidase N and Its Inhibition by Neutralizing Antibodies

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

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structural Bases of Coronavirus Attachment to Host Aminopeptidase N and Its Inhibition by Neutralizing Antibodies
Creator	Enjuanes, Luis Mudgal, Gaurav Reguera, Juan Casasnovas, José Ordoñ, Desiderio
Source	Medline; PMC
abstract	The coronaviruses (CoVs) are enveloped viruses of animals and humans associated mostly with enteric and respiratory diseases, such as the severe acute respiratory syndrome and 10–20% of all common colds. A subset of CoVs uses the cell surface aminopeptidase N (APN), a membrane-bound metalloprotease, as a cell entry receptor. In these viruses, the envelope spike glycoprotein (S) mediates the attachment of the virus particles to APN and subsequent cell entry, which can be blocked by neutralizing antibodies. Here we describe the crystal structures of the receptor-binding domains (RBDs) of two closely related CoV strains, transmissible gastroenteritis virus (TGEV) and porcine respiratory CoV (PRCV), in complex with their receptor, porcine APN (pAPN), or with a neutralizing antibody. The data provide detailed information on the architecture of the dimeric pAPN ectodomain and its interaction with the CoV S. We show that a protruding receptor-binding edge in the S determines virus-binding specificity for recessed glycan-containing surfaces in the membrane-distal region of the pAPN ectodomain. Comparison of the RBDs of TGEV and PRCV to those of other related CoVs, suggests that the conformation of the S receptor-binding region determines cell entry receptor specificity. Moreover, the receptor-binding edge is a major antigenic determinant in the TGEV envelope S that is targeted by neutralizing antibodies. Our results provide a compelling view on CoV cell entry and immune neutralization, and may aid the design of antivirals or CoV vaccines. APN is also considered a target for cancer therapy and its structure, reported here, could facilitate the development of anti-cancer drugs.
has issue date	2012-08-02(xsd:dateTime)
bibo:doi	10.1371/journal.ppat.1002859
bibo:pmid	22876187
has license	cc-by
sha1sum (hex)	4e8f8ad6957ffac26673761935854e6c05b7768e
schema:url	https://doi.org/10.1371/journal.ppat.1002859
resource representing a document's title	Structural Bases of Coronavirus Attachment to Host Aminopeptidase N and Its Inhibition by Neutralizing Antibodies
has PubMed Central identifier	PMC3410853
has PubMed identifier	22876187
schema:publication	PLoS Pathog
resource representing a document's body	covid:4e8f8ad6957ffac26673761935854e6c05b7768e#body_text
is schema:about of	named entity 'ENVELOPE' named entity 'RECEPTOR' named entity 'EDGE' named entity 'NEUTRALIZING ANTIBODY' named entity 'A MAJOR' named entity 'RELATED' named entity 'COMMON COLDS' named entity 'RECEPTORBINDING' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME' named entity 'ANIMALS' named entity 'APN' named entity 'BOUND' named entity 'TARGET' named entity 'SPECIFICITY' named entity 'BINDING SPECIFICITY' named entity 'DATA' named entity 'INFORMATION' named entity 'RESPIRATORY' named entity 'COMPLEX' named entity 'DETAILED' named entity 'ASSOCIATED' named entity 'OUR' named entity 'STRAINS' named entity 'PORCINE' named entity 'TARGETED' named entity 'IMMUNE' named entity 'CELL SURFACE' named entity 'COMPARISON' named entity 'VACCINES' named entity 'DESIGN' named entity 'NEUTRALIZING ANTIBODIES' named entity 'anti-cancer drugs' named entity 'neutralizing antibody' named entity 'envelope' named entity 'RBDs' named entity 'major' named entity 'Inhibition' named entity 'Attachment' named entity 'INHIBITION' named entity 'PROVIDE' named entity 'VIRUSES' named entity 'STRUCTURE' named entity 'INTERACTION' named entity 'SURFACES' named entity 'ARCHITECTURE' named entity 'MEMBRANE' named entity 'BINDING' named entity 'ENTRY' named entity 'THESE' named entity 'HERE' named entity 'MEDIATES' named entity 'HOST' named entity 'BASES' named entity 'STRUCTURAL' named entity 'ITS' named entity 'CORONAVIRUS' named entity 'AMINOPEPTIDASE N' named entity 'ECTODOMAIN' named entity 'BLOCKED' named entity 'CONSIDERED' named entity 'HUMANS' named entity 'ATTACHMENT' named entity 'NEUTRALIZING ANTIBODIES' named entity 'REPORTED' named entity 'CONTAINING' named entity 'CANCER THERAPY' named entity 'DEVELOPMENT' named entity 'DISTAL REGION' named entity 'CANCER' named entity 'VIRUS PARTICLES' named entity 'VIRUS' named entity 'RESULTS' named entity 'STRUCTURES' named entity 'ENTERIC' named entity 'DRUGS' named entity 'VIEW' named entity 'IS A'

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