About: Human molecular chaperones share with SARS-CoV-2 antigenic epitopes potentially capable of eliciting autoimmunity against endothelial cells: possible role of molecular mimicry in COVID-19

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Human molecular chaperones share with SARS-CoV-2 antigenic epitopes potentially capable of eliciting autoimmunity against endothelial cells: possible role of molecular mimicry in COVID-19 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
title	Human molecular chaperones share with SARS-CoV-2 antigenic epitopes potentially capable of eliciting autoimmunity against endothelial cells: possible role of molecular mimicry in COVID-19
Creator	Cappello, Francesco Macario, Alberto Conway De Macario, Everly Marino Gammazza, Antonella Angileri, Francesca Légaré, Sébastien Fucarino, Alberto Bosco, Lo Giosuè, &
source	Medline; PMC
abstract	Severe acute respiratory syndrome corona virus 2 (SARS-CoV-2), the cause of COVID-19 disease, has the potential to elicit autoimmunity because mimicry of human molecular chaperones by viral proteins. We compared viral proteins with human molecular chaperones, many of which are heat shock proteins, to determine if they share amino acid-sequence segments with immunogenic-antigenic potential, which can elicit cross-reactive antibodies and effector immune cells with the capacity to damage-destroy human cells by a mechanism of autoimmunity. We identified the chaperones that can putatively participate in molecular mimicry phenomena after SARS-CoV-2 infection, focusing on those for which endothelial cell plasma-cell membrane localization has already been demonstrated. We also postulate that post-translational modifications, induced by physical (shear) and chemical (metabolic) stress caused respectively by the risk factors hypertension and diabetes, might have a role in determining plasma-cell membrane localization and, in turn, autoimmune-induced endothelial damage. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s12192-020-01148-3) contains supplementary material, which is available to authorized users.
has issue date	2020-08-04(xsd:dateTime)
bibo:doi	10.1007/s12192-020-01148-3
bibo:pmid	32754823
has license	no-cc
sha1sum (hex)	c632cd426b4386866295eeb424874f9085fd1add
schema:url	https://doi.org/10.1007/s12192-020-01148-3
resource representing a document's title	Human molecular chaperones share with SARS-CoV-2 antigenic epitopes potentially capable of eliciting autoimmunity against endothelial cells: possible role of molecular mimicry in COVID-19
has PubMed Central identifier	PMC7402394
has PubMed identifier	32754823
schema:publication	Cell Stress Chaperones
resource representing a document's body	covid:c632cd426b4386866295eeb424874f9085fd1add#body_text
is schema:about of	named entity 'stress' named entity 'physical' named entity 'SARS-CoV-2' named entity 'effector' named entity 'COVID-19' named entity 'epitopes' named entity 'SEQUENCE' named entity 'potential' named entity 'determining' named entity 'hypertension' named entity 'SARS-CoV-2' named entity 'infection' named entity 'caused' named entity 'endothelial cells' named entity 'molecular mimicry' named entity 'viral proteins' named entity 'viral proteins' named entity 'endothelial cell' named entity 'molecular mimicry' named entity 'hypertension' named entity 'chaperones' named entity 'plasma' named entity 'immunogenic' named entity 'molecular chaperones' named entity 'autoimmune' named entity 'epitopes' named entity 'SARS-CoV-2' named entity 'T lymphocytes' named entity 'endothelial cells' named entity 'molecular mimicry' named entity 'immunogenic' named entity 'cross-reactive' named entity 'immune reaction' named entity 'molecular chaperones' named entity 'plasma' named entity 'COVID' named entity 'amino acids' named entity 'cell membrane' named entity 'diabetes' named entity 'autoimmune' named entity 'inflammation' named entity 'endothelium' named entity 'University of Palermo' named entity 'molecular chaperones' named entity 'Lucchese' named entity 'cross-reactivity' named entity 'Université PSL' named entity 'metabolic' named entity 'COVID' named entity 'viral proteins' named entity 'endothelial cells' named entity 'autoimmune response' named entity 'disseminated intravascular coagulation' named entity 'SARS-CoV-2' named entity 'protein sequence' named entity 'Lucchese' named entity 'molecular chaperones' named entity 'peptides' named entity 'microbial' named entity 'plasma' named entity 'atherosclerosis' named entity 'antigenic' named entity 'Italy' named entity 'molecular mimicry' named entity 'HSP90' named entity 'corona virus' named entity 'epitope' named entity 'atherogenic' named entity 'HLA' named entity 'cell surface' named entity 'HSP70' named entity 'foreign antigens' named entity 'amino acids'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software