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Journal Article

HLA-F*01:01 presents peptides with N-terminal flexibility and a preferred length of 16 residues.

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Huyton,  Trevor
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

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Fulltext (public)

3064725.pdf
(Publisher version), 876KB

Supplementary Material (public)

3064725_Suppl_1.pdf
(Supplementary material), 79KB

3064725_Suppl_2.pdf
(Supplementary material), 219KB

3064725_Suppl_3.docx
(Supplementary material), 105KB

3064725_Correction.pdf
(Supplementary material), 99KB

Citation

Ho, G. G. T., Heinen, F. J., Huyton, T., Blasczy, R., & Bade-Döding, C. (2019). HLA-F*01:01 presents peptides with N-terminal flexibility and a preferred length of 16 residues. Immunogenetics, 51(5-6), 353-360. doi:10.1007/s00251-019-01112-1.


Cite as: http://hdl.handle.net/21.11116/0000-0003-B3C3-6
Abstract
HLA-F belongs to the non-classical HLA-Ib molecules with a marginal polymorphic nature and tissue-restricted distribution. HLA-F is a ligand of the NK cell receptor KIR3DS1, whose activation initiates an antiviral downstream immune response and lead to delayed disease progression of HIV-1. During the time course of HIV infection, the expression of HLA-F is upregulated while its interaction with KIR3DS1 is diminished. Understanding HLA-F peptide selection and presentation is essential to a comprehensive understanding of this dynamic immune response and the molecules function. In this study, we were able to recover stable pHLA-F*01:01 complexes and analyze the characteristics of peptides naturally presented by HLA-F. These HLA-F-restricted peptides exhibit a non-canonical length without a defined N-terminal anchor. The peptide characteristics lead to a unique presentation profile and influence the stability of the protein. Furthermore, we demonstrate that almost all source proteins of HLA-F-restricted peptides are described to interact with HIV proteins. Understanding the balance switch between HLA-Ia and HLA-F expression and peptide selection will support to understand the role of HLA-F in viral pathogenesis.