2026-05-21T23:11:56Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/87262024-09-27T23:23:03Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609
Repisalud
author
Lorente, Elena
author
Barriga, Alejandro
author
Johnstone, Carolina
author
Mir-Gerrero, Carmen
author
Jimenez, Mercedes
author
Lopez, Daniel
funder
Ministerio de Ciencia e Innovación (España)
2019-12-02T13:11:44Z
2019-12-02T13:11:44Z
2013
PLoS One. 2013 Nov 1;8(11):e79596.
10.1371/journal.pone.0079596
1932-6203
1932-6203
PloS one
24223975
http://hdl.handle.net/20.500.12105/8726
In the classical human leukocyte antigen (HLA) class I antigen processing and presentation pathway, the antigenic peptides are generated from viral proteins by multiple proteolytic cleavages of the proteasome (and in some cases other cytosolic proteases) and transported to the endoplasmic reticulum (ER) lumen where they are exposed to aminopeptidase activity. In human cells, two different ER-resident enzymes, ERAP1 and ERAP2, can trim the N-terminally extended residues of peptide precursors. In this study, the possible cooperative effect of generating five naturally processed HLA-B27 ligands by both proteases was analyzed. We identified differences in the products obtained with increased detection of natural HLA-B27 ligands by comparing double versus single enzyme digestions by mass spectrometry analysis. These in vitro data suggest that each enzyme can use the degradation products of the other as a substrate for new N-terminal trimming, indicating concerted aminoproteolytic activity of ERAP 1 and ERAP2.
eng
Concerted in vitro trimming of viral HLA-B27-restricted ligands by human ERAP1 and ERAP2 aminopeptidases
journal article
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URL
https://repisalud.isciii.es/bitstreams/49daeb9b-fbbc-4b97-b7fb-4031667d2bc1/download
File
MD5
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application/pdf
ConcertedInVitroTrimming_2013.pdf
URL
https://repisalud.isciii.es/bitstreams/e26939c4-60d2-404d-a56b-f59c654975fe/download
File
MD5
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text/plain
ConcertedInVitroTrimming_2013.pdf.txt