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.

Keywords

Carbohydrate
Inhibitory receptor
MHC
NK cells

UN SDGs

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

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10.1016/S0198-8859(00)00184-1

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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. ",

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

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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

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

Abstract

Bibliographical note

Keywords

UN SDGs

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