Cytomegalovirus gp40/m152 Uses TMED10 as ER Anchor to Retain MHC Class I
| Autor: | Sebastian Springer, Zeynep Hein, Linda Janßen, Swapnil Subhash Ghanwat, Venkat Raman Ramnarayan, Natalia Lis |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Muromegalovirus Amino Acid Motifs Antigen presentation Vesicular Transport Proteins Endoplasmic Reticulum Major histocompatibility complex Models Biological General Biochemistry Genetics and Molecular Biology Mice Structure-Activity Relationship Viral Proteins 03 medical and health sciences symbols.namesake 0302 clinical medicine Cell Line Tumor MHC class I Animals Secretory pathway Immune Evasion biology Chemistry Endoplasmic reticulum Histocompatibility Antigens Class I Golgi apparatus Transmembrane protein Cell biology 030104 developmental biology NIH 3T3 Cells biology.protein symbols 030217 neurology & neurosurgery CD8 Protein Binding |
| Zdroj: | Cell Reports. 23:3068-3077 |
| ISSN: | 2211-1247 |
| Popis: | Summary The murine cytomegalovirus immunoevasin m152/gp40 binds major histocompatibility complex (MHC) class I molecules and retains them in the early secretory pathway by a previously unknown mechanism, preventing antigen presentation to CD8+ T cells. We show that retention of class I and of gp40 itself depends on a lumenal linker sequence in gp40. With unbiased co-immunoprecipitation and mass spectrometry, we find that, through this linker, gp40 binds to TMED10/Tmp21/p24δ1, a member of the p24 family of endoplasmic reticulum (ER)/Golgi transmembrane proteins. We show that the C-terminal KKxxx Golgi-to-ER retrieval signal of TMED10 is required for gp40-mediated retention of class I. We thus identify a viral interaction partner of the p24 proteins and their exploitation for viral immune evasion. |
| Databáze: | OpenAIRE |
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