Human cytomegalovirus UL40 signal peptide regulates cell surface expression of the NK cell ligands HLA-E and gpUL18
Human CMV (HCMV)-encoded NK cell-evasion functions include an MHC class I homolog (UL18) with high affinity for the leukocyte inhibitory receptor-1 (CD85j, ILT2, or LILRB1) and a signal peptide (SPUL40) that acts by upregulating cell surface expression of HLA-E. Detailed characterization of SPUL40 r...
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| Hauptverfasser: | , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
March 15, 2012
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| In: |
The journal of immunology
Year: 2012, Jahrgang: 188, Heft: 6, Pages: 2794-2804 |
| ISSN: | 1550-6606 |
| DOI: | 10.4049/jimmunol.1102068 |
| Online-Zugang: | Verlag, Volltext: http://dx.doi.org/10.4049/jimmunol.1102068 Verlag, Volltext: http://www.jimmunol.org/content/188/6/2794 
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| Verfasserangaben: | Virginie Prod’homme, Peter Tomasec, Charles Cunningham, Marius K. Lemberg, Richard J. Stanton, Brian P. McSharry, Eddie C.Y. Wang, Simone Cuff, Bruno Martoglio, Andrew J. Davison, Véronique M. Braud, and Gavin W.G. Wilkinson |
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| 520 | |a Human CMV (HCMV)-encoded NK cell-evasion functions include an MHC class I homolog (UL18) with high affinity for the leukocyte inhibitory receptor-1 (CD85j, ILT2, or LILRB1) and a signal peptide (SPUL40) that acts by upregulating cell surface expression of HLA-E. Detailed characterization of SPUL40 revealed that the N-terminal 14 aa residues bestowed TAP-independent upregulation of HLA-E, whereas C region sequences delayed processing of SPUL40 by a signal peptide peptidase-type intramembrane protease. Most significantly, the consensus HLA-E-binding epitope within SPUL40 was shown to promote cell surface expression of both HLA-E and gpUL18. UL40 was found to possess two transcription start sites, with utilization of the downstream site resulting in translation being initiated within the HLA-E-binding epitope (P2). Remarkably, this truncated SPUL40 was functional and retained the capacity to upregulate gpUL18 but not HLA-E. Thus, our findings identify an elegant mechanism by which an HCMV signal peptide differentially regulates two distinct NK cell-evasion pathways. Moreover, we describe a natural SPUL40 mutant that provides a clear example of an HCMV clinical virus with a defect in an NK cell-evasion function and exemplifies issues that confront the virus when adapting to immunogenetic diversity in the host. | ||
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