PMID- 31717259
OWN - NLM
STAT- MEDLINE
DCOM- 20200413
LR  - 20200413
IS  - 1422-0067 (Electronic)
IS  - 1422-0067 (Linking)
VI  - 20
IP  - 22
DP  - 2019 Nov 8
TI  - HLA-F Allele-Specific Peptide Restriction Represents an Exceptional Proteomic 
      Footprint.
LID - 10.3390/ijms20225572 [doi]
LID - 5572
AB  - Peptide-dependent engagement between human leucocyte antigens class I (HLA-I) 
      molecules and their cognate receptors has been extensively analyzed. HLA-F 
      belongs to the non-classical HLA-Ib molecules with marginal polymorphic nature 
      and tissue restricted distribution. The three common allelic variants 
      HLA-F*01:01/01:03/01:04 are distinguished by polymorphism outside the peptide 
      binding pockets (residue 50, alpha1 or residue 251, alpha3) and are therefore not 
      considered relevant for attention. However, peptide selection and presentation 
      undergoes a most elaborated extraction from the whole available proteome. It is 
      known that HLA-F confers a beneficial effect on disease outcome during HIV-1 
      infections. The interaction with the NK cell receptor initiates an antiviral 
      downstream immune response and lead to delayed disease progression. During the 
      time of HIV infection, HLA-F expression is upregulated, while its interaction 
      with KIR3DS1 is diminished. The non-polymorphic nature of HLA-F facilitates the 
      conclusion that understanding HLA-F peptide selection and presentation is 
      essential to a comprehensive understanding of this dynamic immune response. 
      Utilizing soluble HLA technology we recovered stable pHLA-F*01:01, 01:03 and 
      01:04 complexes from K562 cells and analyzed the peptides presented. Utilizing a 
      sophisticated LC-MS-method, we analyzed the complete K562 proteome and matched 
      the peptides presented by the respective HLA-F subtypes with detected proteins. 
      All peptides featured a length of 8 to 24 amino acids and are not N-terminally 
      anchored; the C-terminus is preferably anchored by Lys. To comprehend the 
      alteration of the pHLA-F surface we structurally compared HLA-F variants bound to 
      selected peptides. The peptides were selected from the same cellular content; 
      however, no overlap between the proteomic source of F*01:01, 01:03 or 01:04 
      selected peptides could be observed. Recognizing the balance between HLA-F 
      expression, HLA-F polymorphism and peptide selection will support to understand 
      the role of HLA-F in viral pathogenesis.
FAU - Ho, Gia-Gia T
AU  - Ho GT
AD  - Institute for Transfusion Medicine, Hannover Medical School, Carl-Neuberg-Str. 1, 
      30625 Hannover, Germany.
FAU - Heinen, Funmilola J
AU  - Heinen FJ
AD  - Institute for Transfusion Medicine, Hannover Medical School, Carl-Neuberg-Str. 1, 
      30625 Hannover, Germany.
FAU - Blasczyk, Rainer
AU  - Blasczyk R
AD  - Institute for Transfusion Medicine, Hannover Medical School, Carl-Neuberg-Str. 1, 
      30625 Hannover, Germany.
FAU - Pich, Andreas
AU  - Pich A
AD  - Institute of Toxicology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 
      Hannover, Germany.
FAU - Bade-Doeding, Christina
AU  - Bade-Doeding C
AUID- ORCID: 0000-0002-5826-1989
AD  - Institute for Transfusion Medicine, Hannover Medical School, Carl-Neuberg-Str. 1, 
      30625 Hannover, Germany.
LA  - eng
GR  - MED1912/Hector Stiftung/
PT  - Journal Article
DEP - 20191108
PL  - Switzerland
TA  - Int J Mol Sci
JT  - International journal of molecular sciences
JID - 101092791
RN  - 0 (HLA-F antigens)
RN  - 0 (Histocompatibility Antigens Class I)
RN  - 0 (Peptides)
RN  - 0 (Receptors, Natural Killer Cell)
SB  - IM
MH  - *Alleles
MH  - Amino Acid Motifs
MH  - Gene Ontology
MH  - Histocompatibility Antigens Class I/chemistry/*genetics
MH  - Humans
MH  - K562 Cells
MH  - Peptides/*metabolism
MH  - Protein Binding
MH  - *Proteomics
MH  - Receptors, Natural Killer Cell/metabolism
PMC - PMC6888383
OTO - NOTNLM
OT  - HLA-F
OT  - peptide selection
OT  - peptides
OT  - proteome
COIS- The authors declare no conflict of interest.
EDAT- 2019/11/14 06:00
MHDA- 2020/04/14 06:00
PMCR- 2019/11/01
CRDT- 2019/11/14 06:00
PHST- 2019/10/18 00:00 [received]
PHST- 2019/11/04 00:00 [revised]
PHST- 2019/11/06 00:00 [accepted]
PHST- 2019/11/14 06:00 [entrez]
PHST- 2019/11/14 06:00 [pubmed]
PHST- 2020/04/14 06:00 [medline]
PHST- 2019/11/01 00:00 [pmc-release]
AID - ijms20225572 [pii]
AID - ijms-20-05572 [pii]
AID - 10.3390/ijms20225572 [doi]
PST - epublish
SO  - Int J Mol Sci. 2019 Nov 8;20(22):5572. doi: 10.3390/ijms20225572.