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Human Leukocyte Antigen F Presents Peptides and Regulates Immunity through Interactions with NK Cell Receptors

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Human Leukocyte Antigen F Presents Peptides and Regulates Immunity through Interactions with NK Cell Receptors. / Dulberger, Charles L; McMurtrey, Curtis P; Hölzemer, Angelique; Neu, Karlynn E; Liu, Victor; Steinbach, Adriana M; Garcia-Beltran, Wilfredo F; Sulak, Michael; Jabri, Bana; Lynch, Vincent J; Altfeld, Marcus; Hildebrand, William H; Adams, Erin J.

In: IMMUNITY, Vol. 46, No. 6, 20.06.2017, p. 1018-1029.e7.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Dulberger, CL, McMurtrey, CP, Hölzemer, A, Neu, KE, Liu, V, Steinbach, AM, Garcia-Beltran, WF, Sulak, M, Jabri, B, Lynch, VJ, Altfeld, M, Hildebrand, WH & Adams, EJ 2017, 'Human Leukocyte Antigen F Presents Peptides and Regulates Immunity through Interactions with NK Cell Receptors', IMMUNITY, vol. 46, no. 6, pp. 1018-1029.e7. https://doi.org/10.1016/j.immuni.2017.06.002

APA

Dulberger, C. L., McMurtrey, C. P., Hölzemer, A., Neu, K. E., Liu, V., Steinbach, A. M., Garcia-Beltran, W. F., Sulak, M., Jabri, B., Lynch, V. J., Altfeld, M., Hildebrand, W. H., & Adams, E. J. (2017). Human Leukocyte Antigen F Presents Peptides and Regulates Immunity through Interactions with NK Cell Receptors. IMMUNITY, 46(6), 1018-1029.e7. https://doi.org/10.1016/j.immuni.2017.06.002

Vancouver

Dulberger CL, McMurtrey CP, Hölzemer A, Neu KE, Liu V, Steinbach AM et al. Human Leukocyte Antigen F Presents Peptides and Regulates Immunity through Interactions with NK Cell Receptors. IMMUNITY. 2017 Jun 20;46(6):1018-1029.e7. https://doi.org/10.1016/j.immuni.2017.06.002

Bibtex

@article{2300e83512714e54a7d8b029e9bccdf9,
title = "Human Leukocyte Antigen F Presents Peptides and Regulates Immunity through Interactions with NK Cell Receptors",
abstract = "Evidence is mounting that the major histocompatibility complex (MHC) molecule HLA-F (human leukocyte antigen F) regulates the immune system in pregnancy, infection, and autoimmunity by signaling through NK cell receptors (NKRs). We present structural, biochemical, and evolutionary analyses demonstrating that HLA-F presents peptides of unconventional length dictated by a newly arisen mutation (R62W) that has produced an open-ended groove accommodating particularly long peptides. Compared to empty HLA-F open conformers (OCs), HLA-F tetramers bound with human-derived peptides differentially stained leukocytes, suggesting peptide-dependent engagement. Our in vitro studies confirm that NKRs differentiate between peptide-bound and peptide-free HLA-F. The complex structure of peptide-loaded β2m-HLA-F bound to the inhibitory LIR1 revealed similarities to high-affinity recognition of the viral MHC-I mimic UL18 and a docking strategy that relies on contacts with HLA-F as well as β2m, thus precluding binding to HLA-F OCs. These findings provide a biochemical framework to understand how HLA-F could regulate immunity via interactions with NKRs.",
keywords = "Antigen Presentation, Antigens, Antigens, CD, Biological Evolution, Crystallography, X-Ray, Female, HEK293 Cells, Histocompatibility Antigens Class I, Humans, Killer Cells, Natural, Leukocyte Immunoglobulin-like Receptor B1, Molecular Mimicry, Mutation, Peptide Fragments, Pregnancy, Protein Binding, Protein Conformation, Receptors, Immunologic, Receptors, Natural Killer Cell, Viral Proteins, Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't",
author = "Dulberger, {Charles L} and McMurtrey, {Curtis P} and Angelique H{\"o}lzemer and Neu, {Karlynn E} and Victor Liu and Steinbach, {Adriana M} and Garcia-Beltran, {Wilfredo F} and Michael Sulak and Bana Jabri and Lynch, {Vincent J} and Marcus Altfeld and Hildebrand, {William H} and Adams, {Erin J}",
note = "Copyright {\textcopyright} 2017 Elsevier Inc. All rights reserved.",
year = "2017",
month = jun,
day = "20",
doi = "10.1016/j.immuni.2017.06.002",
language = "English",
volume = "46",
pages = "1018--1029.e7",
journal = "IMMUNITY",
issn = "1074-7613",
publisher = "Cell Press",
number = "6",

}

RIS

TY - JOUR

T1 - Human Leukocyte Antigen F Presents Peptides and Regulates Immunity through Interactions with NK Cell Receptors

AU - Dulberger, Charles L

AU - McMurtrey, Curtis P

AU - Hölzemer, Angelique

AU - Neu, Karlynn E

AU - Liu, Victor

AU - Steinbach, Adriana M

AU - Garcia-Beltran, Wilfredo F

AU - Sulak, Michael

AU - Jabri, Bana

AU - Lynch, Vincent J

AU - Altfeld, Marcus

AU - Hildebrand, William H

AU - Adams, Erin J

N1 - Copyright © 2017 Elsevier Inc. All rights reserved.

PY - 2017/6/20

Y1 - 2017/6/20

N2 - Evidence is mounting that the major histocompatibility complex (MHC) molecule HLA-F (human leukocyte antigen F) regulates the immune system in pregnancy, infection, and autoimmunity by signaling through NK cell receptors (NKRs). We present structural, biochemical, and evolutionary analyses demonstrating that HLA-F presents peptides of unconventional length dictated by a newly arisen mutation (R62W) that has produced an open-ended groove accommodating particularly long peptides. Compared to empty HLA-F open conformers (OCs), HLA-F tetramers bound with human-derived peptides differentially stained leukocytes, suggesting peptide-dependent engagement. Our in vitro studies confirm that NKRs differentiate between peptide-bound and peptide-free HLA-F. The complex structure of peptide-loaded β2m-HLA-F bound to the inhibitory LIR1 revealed similarities to high-affinity recognition of the viral MHC-I mimic UL18 and a docking strategy that relies on contacts with HLA-F as well as β2m, thus precluding binding to HLA-F OCs. These findings provide a biochemical framework to understand how HLA-F could regulate immunity via interactions with NKRs.

AB - Evidence is mounting that the major histocompatibility complex (MHC) molecule HLA-F (human leukocyte antigen F) regulates the immune system in pregnancy, infection, and autoimmunity by signaling through NK cell receptors (NKRs). We present structural, biochemical, and evolutionary analyses demonstrating that HLA-F presents peptides of unconventional length dictated by a newly arisen mutation (R62W) that has produced an open-ended groove accommodating particularly long peptides. Compared to empty HLA-F open conformers (OCs), HLA-F tetramers bound with human-derived peptides differentially stained leukocytes, suggesting peptide-dependent engagement. Our in vitro studies confirm that NKRs differentiate between peptide-bound and peptide-free HLA-F. The complex structure of peptide-loaded β2m-HLA-F bound to the inhibitory LIR1 revealed similarities to high-affinity recognition of the viral MHC-I mimic UL18 and a docking strategy that relies on contacts with HLA-F as well as β2m, thus precluding binding to HLA-F OCs. These findings provide a biochemical framework to understand how HLA-F could regulate immunity via interactions with NKRs.

KW - Antigen Presentation

KW - Antigens

KW - Antigens, CD

KW - Biological Evolution

KW - Crystallography, X-Ray

KW - Female

KW - HEK293 Cells

KW - Histocompatibility Antigens Class I

KW - Humans

KW - Killer Cells, Natural

KW - Leukocyte Immunoglobulin-like Receptor B1

KW - Molecular Mimicry

KW - Mutation

KW - Peptide Fragments

KW - Pregnancy

KW - Protein Binding

KW - Protein Conformation

KW - Receptors, Immunologic

KW - Receptors, Natural Killer Cell

KW - Viral Proteins

KW - Journal Article

KW - Research Support, N.I.H., Extramural

KW - Research Support, Non-U.S. Gov't

U2 - 10.1016/j.immuni.2017.06.002

DO - 10.1016/j.immuni.2017.06.002

M3 - SCORING: Journal article

C2 - 28636952

VL - 46

SP - 1018-1029.e7

JO - IMMUNITY

JF - IMMUNITY

SN - 1074-7613

IS - 6

ER -