Ly-49A, a receptor for H-2Dd, has a functional carbohydrate recognition domain

Brian F. Daniels; Mary C. Nakamura; Steven D. Rosen; Wayne M. Yokoyama; William E. Seaman

doi:10.1016/S1074-7613(94)80020-0

Ly-49A, a receptor for H-2D^d, has a functional carbohydrate recognition domain

Brian F. Daniels, Mary C. Nakamura, Steven D. Rosen, Wayne M. Yokoyama, William E. Seaman

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

110 Scopus citations

Abstract

Ly-49A⁺ murine natural killer (NK) cells cannot lyse target cells that express H-2D^d. We demonstrate a functional requirement for carbohydrate recognition by Ly-49A. Treatment of H-2D^d+ target cells with tunicamycin prevents their binding to Ly-49A⁺ cells and renders them susceptible to lysis by Ly-49A⁺ NK cells. Fucoidan, a sulfated polysaccharide, binds to Ly-49A in a calcium-dependent manner, and this binding is inhibited by monosaccharides, particularly sulfated hexoses. The inactivation of Ly-49A⁺ NK cells by H-2D^d+ target cells is reversed in the presence of glucose 6-SO₄. These results indicate that Ly-49A has a functional carbohydrate recognition domain and that target expression of carbohydrates alters their susceptibility to natural killing.

Original language	English
Pages (from-to)	785-792
Number of pages	8
Journal	Immunity
Volume	1
Issue number	9
DOIs	https://doi.org/10.1016/S1074-7613(94)80020-0
State	Published - Dec 1994

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@article{8bceea7c372d464f8bc95dd3d1dac2e2,

title = "Ly-49A, a receptor for H-2Dd, has a functional carbohydrate recognition domain",

abstract = "Ly-49A+ murine natural killer (NK) cells cannot lyse target cells that express H-2Dd. We demonstrate a functional requirement for carbohydrate recognition by Ly-49A. Treatment of H-2Dd+ target cells with tunicamycin prevents their binding to Ly-49A+ cells and renders them susceptible to lysis by Ly-49A+ NK cells. Fucoidan, a sulfated polysaccharide, binds to Ly-49A in a calcium-dependent manner, and this binding is inhibited by monosaccharides, particularly sulfated hexoses. The inactivation of Ly-49A+ NK cells by H-2Dd+ target cells is reversed in the presence of glucose 6-SO4. These results indicate that Ly-49A has a functional carbohydrate recognition domain and that target expression of carbohydrates alters their susceptibility to natural killing.",

author = "Daniels, {Brian F.} and Nakamura, {Mary C.} and Rosen, {Steven D.} and Yokoyama, {Wayne M.} and Seaman, {William E.}",

note = "Funding Information: S. Mallett kindly prepared the FL-fucoidan. This work was supported by the Veterans Administration and by National Institutes of Health grant CA46812 (to W. E. S.). B. F. D. is a recipient of an Arthritis Foundation Postdoctoral Fellowship.",

year = "1994",

month = dec,

doi = "10.1016/S1074-7613(94)80020-0",

language = "English",

volume = "1",

pages = "785--792",

journal = "Immunity",

issn = "1074-7613",

number = "9",

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TY - JOUR

T1 - Ly-49A, a receptor for H-2Dd, has a functional carbohydrate recognition domain

AU - Daniels, Brian F.

AU - Nakamura, Mary C.

AU - Rosen, Steven D.

AU - Yokoyama, Wayne M.

AU - Seaman, William E.

N1 - Funding Information: S. Mallett kindly prepared the FL-fucoidan. This work was supported by the Veterans Administration and by National Institutes of Health grant CA46812 (to W. E. S.). B. F. D. is a recipient of an Arthritis Foundation Postdoctoral Fellowship.

PY - 1994/12

Y1 - 1994/12

N2 - Ly-49A+ murine natural killer (NK) cells cannot lyse target cells that express H-2Dd. We demonstrate a functional requirement for carbohydrate recognition by Ly-49A. Treatment of H-2Dd+ target cells with tunicamycin prevents their binding to Ly-49A+ cells and renders them susceptible to lysis by Ly-49A+ NK cells. Fucoidan, a sulfated polysaccharide, binds to Ly-49A in a calcium-dependent manner, and this binding is inhibited by monosaccharides, particularly sulfated hexoses. The inactivation of Ly-49A+ NK cells by H-2Dd+ target cells is reversed in the presence of glucose 6-SO4. These results indicate that Ly-49A has a functional carbohydrate recognition domain and that target expression of carbohydrates alters their susceptibility to natural killing.

AB - Ly-49A+ murine natural killer (NK) cells cannot lyse target cells that express H-2Dd. We demonstrate a functional requirement for carbohydrate recognition by Ly-49A. Treatment of H-2Dd+ target cells with tunicamycin prevents their binding to Ly-49A+ cells and renders them susceptible to lysis by Ly-49A+ NK cells. Fucoidan, a sulfated polysaccharide, binds to Ly-49A in a calcium-dependent manner, and this binding is inhibited by monosaccharides, particularly sulfated hexoses. The inactivation of Ly-49A+ NK cells by H-2Dd+ target cells is reversed in the presence of glucose 6-SO4. These results indicate that Ly-49A has a functional carbohydrate recognition domain and that target expression of carbohydrates alters their susceptibility to natural killing.

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U2 - 10.1016/S1074-7613(94)80020-0

DO - 10.1016/S1074-7613(94)80020-0

M3 - Article

C2 - 7895167

AN - SCOPUS:0028675569

SN - 1074-7613

VL - 1

SP - 785

EP - 792

JO - Immunity

JF - Immunity

IS - 9

ER -

Ly-49A, a receptor for H-2D^d, has a functional carbohydrate recognition domain

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