Evidence for an involvement of the ubiquitin-like modifier ISG15 in MHC class I antigen presentation.
Animals
Antigen Presentation
/ immunology
Cytokines
/ deficiency
HEK293 Cells
Histocompatibility Antigens Class I
/ immunology
Humans
Lymphocytic choriomeningitis virus
/ genetics
Mice
Mice, Inbred BALB C
Mice, Inbred C57BL
Mice, Knockout
Nucleocapsid Proteins
/ genetics
Proteasome Endopeptidase Complex
/ immunology
Protein Modification, Translational
/ immunology
Proteolysis
Recombinant Fusion Proteins
/ genetics
Ubiquitin Thiolesterase
/ deficiency
Ubiquitins
/ deficiency
ISG15
MHC class I
antigen presentation
proteasome
ubiquitin-like modifier
Journal
European journal of immunology
ISSN: 1521-4141
Titre abrégé: Eur J Immunol
Pays: Germany
ID NLM: 1273201
Informations de publication
Date de publication:
01 2021
01 2021
Historique:
received:
20
03
2020
revised:
16
06
2020
accepted:
14
07
2020
pubmed:
21
7
2020
medline:
23
4
2021
entrez:
21
7
2020
Statut:
ppublish
Résumé
The IFN stimulated gene 15 (ISG15) encodes a 15-kDa ubiquitin-like protein, that is induced by type I IFNs and is conjugated to the bulk of newly synthesized polypeptides at the ribosome. ISG15 functions as an antiviral molecule possibly by being covalently conjugated to viral proteins and disturbing virus particle assembly. Here, we have investigated the effect of ISGylation on degradation and antigen presentation of viral and cellular proteins. ISGylation did not induce proteasomal degradation of bulk ISG15 target proteins neither after overexpressing ISG15 nor after induction by IFN-β. The MHC class I cell surface expression of splenocytes derived from ISG15-deficient mice or mice lacking the catalytic activity of the major de-ISGylating enzyme USP18 was unaltered as compared to WT mice. Fusion of ubiquitin or FAT10 to the long-lived nucleoprotein (NP) of lymphocytic choriomeningitis virus accelerated the proteasomal degradation of NP while fusion to ISG15 did not detectably speed up NP degradation. Nevertheless, MHC-I restricted presentation of two epitopes of NP were markedly enhanced when it was fused to ISG15 similarly to fusion with ubiquitin or FAT10. Thus, we provide evidence that ISG15 can enhance the presentation of antigens on MHC-I most likely by promoting co-translational antigen processing.
Identifiants
pubmed: 32686110
doi: 10.1002/eji.202048646
doi:
Substances chimiques
Cytokines
0
FAT10 protein, mouse
0
G1p2 protein, mouse
0
Histocompatibility Antigens Class I
0
Nucleocapsid Proteins
0
Recombinant Fusion Proteins
0
Ubiquitins
0
ISG15 protein, human
60267-61-0
Usp18 protein, mouse
EC 3.4.19.-
Ubiquitin Thiolesterase
EC 3.4.19.12
Proteasome Endopeptidase Complex
EC 3.4.25.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
138-150Informations de copyright
© 2020 Wiley-VCH GmbH.
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