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A signal peptide de...
A signal peptide derived from hsp60 binds HLA-E and interferes with CD94/NKG2A recognition
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- Michaelsson, J (författare)
- Karolinska Institutet
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de Matos, CT (författare)
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- Achour, A (författare)
- Karolinska Institutet
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Lanier, LL (författare)
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- Karre, K (författare)
- Karolinska Institutet
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Soderstrom, K (författare)
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(creator_code:org_t)
- 2002-12-02
- 2002
- Engelska.
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Ingår i: The Journal of experimental medicine. - : Rockefeller University Press. - 0022-1007 .- 1540-9538. ; 196:11, s. 1403-1414
- Relaterad länk:
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http://jem.rupress.o...
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http://kipublication...
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https://doi.org/10.1...
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Abstract
Ämnesord
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- Human histocompatibility leukocyte antigen (HLA)-E is a nonclassical major histocompatibility complex (MHC) class I molecule which presents a restricted set of nonameric peptides, derived mainly from the signal sequence of other MHC class I molecules. It interacts with CD94/NKG2 receptors expressed on the surface of natural killer (NK) cells and T cell subsets. Here we demonstrate that HLA-E also presents a peptide derived from the leader sequence of human heat shock protein 60 (hsp60). This peptide gains access to HLA-E intracellularly, resulting in up-regulated HLA-E/hsp60 signal peptide cell-surface levels on stressed cells. Notably, HLA-E molecules in complex with the hsp60 signal peptide are no longer recognized by CD94/NKG2A inhibitory receptors. Thus, during cellular stress an increased proportion of HLA-E molecules may bind the nonprotective hsp60 signal peptide, leading to a reduced capacity to inhibit a major NK cell population. Such stress induced peptide interference would gradually uncouple CD94/NKG2A inhibitory recognition and provide a mechanism for NK cells to detect stressed cells in a peptide-dependent manner.
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