N-linked carbohydrate on human leukocyte antigen-C and recognition by natural killer cell inhibitory receptors

Eishi Baba; Robert Erskine; Jonathan E. Boyson; George B. Cohen; Daniel M. Davis; Pratap Malik; Ofer Mandelboim; Hugh T. Reyburn; Jack L. Strominger

doi:10.1016/S0198-8859(00)00184-1

N-linked carbohydrate on human leukocyte antigen-C and recognition by natural killer cell inhibitory receptors

Eishi Baba
, Robert Erskine
, Jonathan E. Boyson
, George B. Cohen
, Daniel M. Davis
, Pratap Malik
, Ofer Mandelboim
, Hugh T. Reyburn
, Jack L. Strominger^*

^*Corresponding author for this work

Department of Immunology and Cancer Research

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

14 Scopus citations

Abstract

The possible role of carbohydrate in the interaction of HLA-C with a human inhibitory natural Killer cell Immunoglobulin-like Receptor with two Ig domains, KIR2DL1, was investigated. Transfectants of 721.221 (a class I MHC-negative human B cell line) expressing only HLA-Cw4 or -Cw6 or their respective non-glycosylated mutants (N86Q, S88A) were made. The binding of a KIR2DL1-Ig fusion protein to the nonglycosylated mutant HLA-Cw4- or -Cw6-expressing cells was markedly decreased compared to the wild type-expressing cells. The ability to induce an inhibitory signal in the NK tumor line YTS transfected with KIR2DL1 was also impaired in the nonglycosylated mutant expressing cells. Furthermore, in a second functional assay, mutant HLA-Cw4 and -Cw6 molecules had impaired ability to induce signal transduction in BW cells expressing a KIR2DL1-CD3 zeta chain chimeric protein. Thus, the deletion of the N-linked glycosylation signal in HLA-Cw4 and -Cw6 greatly reduced recognition by KIR2DL1. Alternative interpretations of the data are discussed.

Original language	English
Pages (from-to)	1202-1218
Number of pages	17
Journal	Human Immunology
Volume	61
Issue number	12
DOIs	https://doi.org/10.1016/S0198-8859(00)00184-1
State	Published - 2000

Bibliographical note

Funding Information:
This work was supported by a National Institutes of Health research grant (R35-CA47554); a postdoctoral fellowship from The Irvington Institute for Immunological Research, New York to D.M. Davis; and the Cancer Research Fund of The Damon Runyon-Walter Winchell Foundation Fellowship grant No. DRG1454 to O. Mandelboim.

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Carbohydrate
Inhibitory receptor
MHC
NK cells

Access to Document

10.1016/S0198-8859(00)00184-1

Cite this

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title = "N-linked carbohydrate on human leukocyte antigen-C and recognition by natural killer cell inhibitory receptors",

abstract = "The possible role of carbohydrate in the interaction of HLA-C with a human inhibitory natural Killer cell Immunoglobulin-like Receptor with two Ig domains, KIR2DL1, was investigated. Transfectants of 721.221 (a class I MHC-negative human B cell line) expressing only HLA-Cw4 or -Cw6 or their respective non-glycosylated mutants (N86Q, S88A) were made. The binding of a KIR2DL1-Ig fusion protein to the nonglycosylated mutant HLA-Cw4- or -Cw6-expressing cells was markedly decreased compared to the wild type-expressing cells. The ability to induce an inhibitory signal in the NK tumor line YTS transfected with KIR2DL1 was also impaired in the nonglycosylated mutant expressing cells. Furthermore, in a second functional assay, mutant HLA-Cw4 and -Cw6 molecules had impaired ability to induce signal transduction in BW cells expressing a KIR2DL1-CD3 zeta chain chimeric protein. Thus, the deletion of the N-linked glycosylation signal in HLA-Cw4 and -Cw6 greatly reduced recognition by KIR2DL1. Alternative interpretations of the data are discussed.",

keywords = "Carbohydrate, Inhibitory receptor, MHC, NK cells",

author = "Eishi Baba and Robert Erskine and Boyson, \{Jonathan E.\} and Cohen, \{George B.\} and Davis, \{Daniel M.\} and Pratap Malik and Ofer Mandelboim and Reyburn, \{Hugh T.\} and Strominger, \{Jack L.\}",

note = "Funding Information: This work was supported by a National Institutes of Health research grant (R35-CA47554); a postdoctoral fellowship from The Irvington Institute for Immunological Research, New York to D.M. Davis; and the Cancer Research Fund of The Damon Runyon-Walter Winchell Foundation Fellowship grant No. DRG1454 to O. Mandelboim. ",

year = "2000",

doi = "10.1016/S0198-8859(00)00184-1",

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volume = "61",

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journal = "Human Immunology",

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number = "12",

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T1 - N-linked carbohydrate on human leukocyte antigen-C and recognition by natural killer cell inhibitory receptors

AU - Baba, Eishi

AU - Erskine, Robert

AU - Boyson, Jonathan E.

AU - Cohen, George B.

AU - Davis, Daniel M.

AU - Malik, Pratap

AU - Mandelboim, Ofer

AU - Reyburn, Hugh T.

AU - Strominger, Jack L.

N1 - Funding Information: This work was supported by a National Institutes of Health research grant (R35-CA47554); a postdoctoral fellowship from The Irvington Institute for Immunological Research, New York to D.M. Davis; and the Cancer Research Fund of The Damon Runyon-Walter Winchell Foundation Fellowship grant No. DRG1454 to O. Mandelboim.

PY - 2000

Y1 - 2000

N2 - The possible role of carbohydrate in the interaction of HLA-C with a human inhibitory natural Killer cell Immunoglobulin-like Receptor with two Ig domains, KIR2DL1, was investigated. Transfectants of 721.221 (a class I MHC-negative human B cell line) expressing only HLA-Cw4 or -Cw6 or their respective non-glycosylated mutants (N86Q, S88A) were made. The binding of a KIR2DL1-Ig fusion protein to the nonglycosylated mutant HLA-Cw4- or -Cw6-expressing cells was markedly decreased compared to the wild type-expressing cells. The ability to induce an inhibitory signal in the NK tumor line YTS transfected with KIR2DL1 was also impaired in the nonglycosylated mutant expressing cells. Furthermore, in a second functional assay, mutant HLA-Cw4 and -Cw6 molecules had impaired ability to induce signal transduction in BW cells expressing a KIR2DL1-CD3 zeta chain chimeric protein. Thus, the deletion of the N-linked glycosylation signal in HLA-Cw4 and -Cw6 greatly reduced recognition by KIR2DL1. Alternative interpretations of the data are discussed.

AB - The possible role of carbohydrate in the interaction of HLA-C with a human inhibitory natural Killer cell Immunoglobulin-like Receptor with two Ig domains, KIR2DL1, was investigated. Transfectants of 721.221 (a class I MHC-negative human B cell line) expressing only HLA-Cw4 or -Cw6 or their respective non-glycosylated mutants (N86Q, S88A) were made. The binding of a KIR2DL1-Ig fusion protein to the nonglycosylated mutant HLA-Cw4- or -Cw6-expressing cells was markedly decreased compared to the wild type-expressing cells. The ability to induce an inhibitory signal in the NK tumor line YTS transfected with KIR2DL1 was also impaired in the nonglycosylated mutant expressing cells. Furthermore, in a second functional assay, mutant HLA-Cw4 and -Cw6 molecules had impaired ability to induce signal transduction in BW cells expressing a KIR2DL1-CD3 zeta chain chimeric protein. Thus, the deletion of the N-linked glycosylation signal in HLA-Cw4 and -Cw6 greatly reduced recognition by KIR2DL1. Alternative interpretations of the data are discussed.

KW - Carbohydrate

KW - Inhibitory receptor

KW - MHC

KW - NK cells

UR - https://www.scopus.com/pages/publications/0034488050

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JO - Human Immunology

JF - Human Immunology

IS - 12

ER -

N-linked carbohydrate on human leukocyte antigen-C and recognition by natural killer cell inhibitory receptors

Abstract

Bibliographical note

UN SDGs

Keywords

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