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

Autor: Funmilola J. Heinen, Gia-Gia T Hò, Trevor Huyton, Rainer Blasczyk, Christina Bade-Döding
Rok vydání: 2019
Předmět:
Zdroj: Immunogenetics. 71:361-361
ISSN: 1432-1211
0093-7711
DOI: 10.1007/s00251-019-01116-x
Popis: 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.
Databáze: OpenAIRE
Externí odkaz: