Two human ULBP/RAET1 molecules with transmembrane regions are ligands for NKG2D

Louise Bacon; Robert A Eagle; Martina Meyer; Nicholas Easom; Neil Thomas Young; John Trowsdale

Two human ULBP/RAET1 molecules with transmembrane regions are ligands for NKG2D

Louise Bacon, Robert A Eagle, Martina Meyer, Nicholas Easom, Neil Thomas Young, John Trowsdale

Applied Medicine

Research output: Contribution to journal › Article › peer-review

147 Citations (Scopus)

Abstract

We characterized two novel members of the RAET1/ULBP gene cluster, RAET1E and RAET1G. The encoded proteins were similar to the ULBP in their class I-like alpha1 and alpha2 domains, but differed in that, instead of being GPI-anchored, their sequences were type 1 membrane-spanning molecules. Both proteins were capable of being expressed at the cell surface. Both proteins bound the activating receptor NKG2D, and RAET1G bound the human CMV protein UL16. The expression of diverse NKG2D-binding molecules in different tissues and with different properties is consistent with multiple modes of infection- or stress-induced activation.

Original language	English
Pages (from-to)	1078-1084
Number of pages	7
Journal	The Journal of Immunology
Volume	173
Issue number	2
Publication status	Published - 15 Jul 2004

Keywords

Alternative Splicing
Amino Acid Sequence
Carrier Proteins
Cytomegalovirus
Histocompatibility Antigens Class I
Humans
Killer Cells, Natural
Ligands
Membrane Proteins
Molecular Sequence Data
Multigene Family
NK Cell Lectin-Like Receptor Subfamily K
Phylogeny
Protein Isoforms
Receptors, Immunologic
Receptors, Natural Killer Cell
Viral Proteins

Cite this

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title = "Two human ULBP/RAET1 molecules with transmembrane regions are ligands for NKG2D",

abstract = "We characterized two novel members of the RAET1/ULBP gene cluster, RAET1E and RAET1G. The encoded proteins were similar to the ULBP in their class I-like alpha1 and alpha2 domains, but differed in that, instead of being GPI-anchored, their sequences were type 1 membrane-spanning molecules. Both proteins were capable of being expressed at the cell surface. Both proteins bound the activating receptor NKG2D, and RAET1G bound the human CMV protein UL16. The expression of diverse NKG2D-binding molecules in different tissues and with different properties is consistent with multiple modes of infection- or stress-induced activation.",

keywords = "Alternative Splicing, Amino Acid Sequence, Carrier Proteins, Cytomegalovirus, Histocompatibility Antigens Class I, Humans, Killer Cells, Natural, Ligands, Membrane Proteins, Molecular Sequence Data, Multigene Family, NK Cell Lectin-Like Receptor Subfamily K, Phylogeny, Protein Isoforms, Receptors, Immunologic, Receptors, Natural Killer Cell, Viral Proteins",

author = "Louise Bacon and Eagle, {Robert A} and Martina Meyer and Nicholas Easom and Young, {Neil Thomas} and John Trowsdale",

year = "2004",

month = jul,

day = "15",

language = "English",

volume = "173",

pages = "1078--1084",

journal = "The Journal of Immunology",

issn = "0022-1767",

publisher = "American Association of Immunologists",

number = "2",

}

TY - JOUR

T1 - Two human ULBP/RAET1 molecules with transmembrane regions are ligands for NKG2D

AU - Bacon, Louise

AU - Eagle, Robert A

AU - Meyer, Martina

AU - Easom, Nicholas

AU - Young, Neil Thomas

AU - Trowsdale, John

PY - 2004/7/15

Y1 - 2004/7/15

N2 - We characterized two novel members of the RAET1/ULBP gene cluster, RAET1E and RAET1G. The encoded proteins were similar to the ULBP in their class I-like alpha1 and alpha2 domains, but differed in that, instead of being GPI-anchored, their sequences were type 1 membrane-spanning molecules. Both proteins were capable of being expressed at the cell surface. Both proteins bound the activating receptor NKG2D, and RAET1G bound the human CMV protein UL16. The expression of diverse NKG2D-binding molecules in different tissues and with different properties is consistent with multiple modes of infection- or stress-induced activation.

AB - We characterized two novel members of the RAET1/ULBP gene cluster, RAET1E and RAET1G. The encoded proteins were similar to the ULBP in their class I-like alpha1 and alpha2 domains, but differed in that, instead of being GPI-anchored, their sequences were type 1 membrane-spanning molecules. Both proteins were capable of being expressed at the cell surface. Both proteins bound the activating receptor NKG2D, and RAET1G bound the human CMV protein UL16. The expression of diverse NKG2D-binding molecules in different tissues and with different properties is consistent with multiple modes of infection- or stress-induced activation.

KW - Alternative Splicing

KW - Amino Acid Sequence

KW - Carrier Proteins

KW - Cytomegalovirus

KW - Histocompatibility Antigens Class I

KW - Humans

KW - Killer Cells, Natural

KW - Ligands

KW - Membrane Proteins

KW - Molecular Sequence Data

KW - Multigene Family

KW - NK Cell Lectin-Like Receptor Subfamily K

KW - Phylogeny

KW - Protein Isoforms

KW - Receptors, Immunologic

KW - Receptors, Natural Killer Cell

KW - Viral Proteins

M3 - Article

C2 - 15240696

SN - 0022-1767

VL - 173

SP - 1078

EP - 1084

JO - The Journal of Immunology

JF - The Journal of Immunology

IS - 2

ER -

Two human ULBP/RAET1 molecules with transmembrane regions are ligands for NKG2D

Abstract

Keywords

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