About: Alternative Antigen Processing for MHC Class I: Multiple Roads Lead to Rome

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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	Alternative Antigen Processing for MHC Class I: Multiple Roads Lead to Rome
Creator	Gannagé, Monique Khanna, Rajiv Mautner, Josef Oliveira, Cláudia Van Hall, Thorbald
topic	covid:138200f99f62c51776c9afec55d856e854ea8ff1#this
Source	PMC
abstract	The well described conventional antigen-processing pathway is accountable for most peptides that end up in MHC class I molecules at the cell surface. These peptides experienced liberation by the proteasome and transport by the peptide transporter TAP. However, there are multiple roads that lead to Rome, illustrated by the increasing number of alternative processing pathways that have been reported during last years. Interestingly, TAP-deficient individuals do not succumb to viral infections, suggesting that CD8 T cell immunity is sufficiently supported by alternative TAP-independent processing pathways. To date, a diversity of viral and endogenous TAP-independent peptides have been identified in the grooves of different MHC class I alleles. Some of these peptides are not displayed by normal TAP-positive cells and we therefore called them TEIPP, for “T-cell epitopes associated with impaired peptide processing.” TEIPPs are hidden self-antigens, are derived from normal housekeeping proteins, and are processed via unconventional processing pathways. Per definition, TEIPPs are presented via TAP-independent pathways, but recent data suggest that part of this repertoire still depend on proteasome and metalloprotease activity. An exception is the C-terminal peptide of the endoplasmic reticulum (ER)-membrane-spanning ceramide synthase Trh4 that is surprisingly liberated by the signal peptide peptidase (SPP), the proteolytic enzyme involved in cleaving leader sequences. The intramembrane cleaving SPP is thereby an important contributor of TAP-independent peptides. Its family members, like the Alzheimer’s related presenilins, might contribute as well, according to our preliminary data. Finally, alternative peptide routing is an emerging field and includes processes like the unfolded protein response, the ER-associated degradation, and autophagy-associated vesicular pathways. These data convince us that there is a world to be discovered in the field of unconventional antigen processing.
has issue date	2015-06-05(xsd:dateTime)
bibo:doi	10.3389/fimmu.2015.00298
bibo:pmid	26097483
has license	cc-by
sha1sum (hex)	138200f99f62c51776c9afec55d856e854ea8ff1
schema:url	https://doi.org/10.3389/fimmu.2015.00298
resource representing a document's title	Alternative Antigen Processing for MHC Class I: Multiple Roads Lead to Rome
has PubMed Central identifier	PMC4457021
has PubMed identifier	26097483
schema:publication	Front Immunol
resource representing a document's body	covid:138200f99f62c51776c9afec55d856e854ea8ff1#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/138200f99f62c51776c9afec55d856e854ea8ff1
is schema:about of	named entity 'SUPPORTED' named entity 'PEPTIDE' named entity 'ROME' named entity 'DEFICIENT' named entity 'ASSOCIATED WITH' named entity 'UNFOLDED PROTEIN RESPONSE' named entity 'ER-' named entity 'ACCORDING' named entity 'LIBERATION' named entity 'METALLOPROTEASE ACTIVITY' named entity 'PART OF' named entity 'TRANSPORT' named entity 'TAP' named entity 'PEPTIDE TRANSPORTER' named entity 'NORMAL' named entity 'SUGGEST' named entity 'ALTERNATIVE' named entity 'PER DEFINITION' named entity 'GROOVES' named entity 'AUTOPHAGY' named entity 'CONTRIBUTOR' named entity 'DIVERSITY' named entity 'DEPEND' named entity 'SIGNAL PEPTIDE PEPTIDASE' named entity 'ANTIGEN PROCESSING' named entity 'PEPTIDES' named entity 'MEMBRANE' named entity 'EXPERIENCED' named entity 'INDEPENDENT' named entity 'ROADS' named entity 'INCREASING' named entity 'PROTEINS' named entity 'PROTEASOME' named entity 'PROCESSING' named entity 'CERAMIDE SYNTHASE' named entity 'PATHWAY' named entity 'FAMILY MEMBERS' named entity 'DIFFERENT' named entity 'ALTERNATIVE' named entity 'data' named entity 'housekeeping' named entity 'processing' named entity 'T cell' named entity 'surface' named entity 'antigen processing' named entity 'multiple' named entity 'MULTIPLE' named entity 'VESICULAR' named entity 'VIRAL INFECTIONS' named entity 'HIDDEN' named entity 'PATHWAYS' named entity 'TRH4' named entity 'SPP' named entity 'POSITIVE' named entity 'OUR' named entity 'ENDOPLASMIC RETICULUM' named entity 'BUT' named entity 'DESCRIBED' named entity 'PRELIMINARY DATA' named entity 'YEARS' named entity 'DO NOT' named entity 'EPITOPES' named entity 'RELATED' named entity 'CONVENTIONAL' named entity 'PROCESSES' named entity '27S' named entity 'ITS' named entity 'THESE' named entity 'C-TERMINAL PEPTIDE' named entity 'SEQUENCES' named entity 'SELF' named entity 'INDIVIDUALS' named entity 'ENDOGENOUS' named entity 'DATA' named entity 'CELLS'

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