Cutting edge: CD43 functions as a T cell counterreceptor for the macrophage adhesion receptor sialoadhesin (Siglec-1)

T K van den Berg, D Nath, H J Ziltener, D Vestweber, M Fukuda, I van Die, P R Crocker

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Sialoadhesin (Siglec-1) is a macrophage-restricted sialic acid-binding receptor that mediates interactions with hemopoietic cells, including lymphocytes. In this study, we identify sialoadhesin counterreceptors on T lymphocytes. Several major glycoproteins (85, 130, 240 kDa) were precipitated by sialoadhesin-Fc fusion proteins from a murine T cell line (TK-1). Binding of sialoadhesin to these glycoproteins was sialic acid dependent and was abolished by mutation of a critical residue (R97A) of the sialic acid binding site in the membrane distal Ig-like domain of sialoadhesin. The 130- and 240-kDa sialoadhesin-binding glycoproteins were identified as the sialomucins CD43 and P-selectin glycoprotein ligand 1 (CD162), respectively. CD43 expressed in COS cells supported increased binding to immobilized sialoadhesin. Finally, sialoadhesin bound different glycoforms of CD43 expressed in Chinese hamster ovary cells, including unbranched (core 1) and branched (core 2) O:-linked glycans, that are normally found on CD43 in resting and activated T cells, respectively. These results identify CD43 as a T cell counterreceptor for sialoadhesin and suggest that in addition to its anti-adhesive role CD43 may promote cell-cell interactions.

Original languageEnglish
Pages (from-to)3637-40
Number of pages4
JournalJournal of Immunology
Volume166
Issue number6
Publication statusPublished - 15 Mar 2001

Cite this

van den Berg, T K ; Nath, D ; Ziltener, H J ; Vestweber, D ; Fukuda, M ; van Die, I ; Crocker, P R. / Cutting edge : CD43 functions as a T cell counterreceptor for the macrophage adhesion receptor sialoadhesin (Siglec-1). In: Journal of Immunology. 2001 ; Vol. 166, No. 6. pp. 3637-40.
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abstract = "Sialoadhesin (Siglec-1) is a macrophage-restricted sialic acid-binding receptor that mediates interactions with hemopoietic cells, including lymphocytes. In this study, we identify sialoadhesin counterreceptors on T lymphocytes. Several major glycoproteins (85, 130, 240 kDa) were precipitated by sialoadhesin-Fc fusion proteins from a murine T cell line (TK-1). Binding of sialoadhesin to these glycoproteins was sialic acid dependent and was abolished by mutation of a critical residue (R97A) of the sialic acid binding site in the membrane distal Ig-like domain of sialoadhesin. The 130- and 240-kDa sialoadhesin-binding glycoproteins were identified as the sialomucins CD43 and P-selectin glycoprotein ligand 1 (CD162), respectively. CD43 expressed in COS cells supported increased binding to immobilized sialoadhesin. Finally, sialoadhesin bound different glycoforms of CD43 expressed in Chinese hamster ovary cells, including unbranched (core 1) and branched (core 2) O:-linked glycans, that are normally found on CD43 in resting and activated T cells, respectively. These results identify CD43 as a T cell counterreceptor for sialoadhesin and suggest that in addition to its anti-adhesive role CD43 may promote cell-cell interactions.",
keywords = "Animals, Antigens, CD/metabolism, CHO Cells, COS Cells, Cell Adhesion Molecules/metabolism, Cricetinae, Humans, Interphase/immunology, Leukosialin, Lymphocyte Activation, Membrane Glycoproteins/metabolism, Mice, Protein Binding/immunology, Receptors, Immunologic/metabolism, Sialic Acid Binding Ig-like Lectin 1, Sialoglycoproteins/metabolism, T-Lymphocytes/immunology, Tumor Cells, Cultured",
author = "{van den Berg}, {T K} and D Nath and Ziltener, {H J} and D Vestweber and M Fukuda and {van Die}, I and Crocker, {P R}",
year = "2001",
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language = "English",
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Cutting edge : CD43 functions as a T cell counterreceptor for the macrophage adhesion receptor sialoadhesin (Siglec-1). / van den Berg, T K; Nath, D; Ziltener, H J; Vestweber, D; Fukuda, M; van Die, I; Crocker, P R.

In: Journal of Immunology, Vol. 166, No. 6, 15.03.2001, p. 3637-40.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Cutting edge

T2 - CD43 functions as a T cell counterreceptor for the macrophage adhesion receptor sialoadhesin (Siglec-1)

AU - van den Berg, T K

AU - Nath, D

AU - Ziltener, H J

AU - Vestweber, D

AU - Fukuda, M

AU - van Die, I

AU - Crocker, P R

PY - 2001/3/15

Y1 - 2001/3/15

N2 - Sialoadhesin (Siglec-1) is a macrophage-restricted sialic acid-binding receptor that mediates interactions with hemopoietic cells, including lymphocytes. In this study, we identify sialoadhesin counterreceptors on T lymphocytes. Several major glycoproteins (85, 130, 240 kDa) were precipitated by sialoadhesin-Fc fusion proteins from a murine T cell line (TK-1). Binding of sialoadhesin to these glycoproteins was sialic acid dependent and was abolished by mutation of a critical residue (R97A) of the sialic acid binding site in the membrane distal Ig-like domain of sialoadhesin. The 130- and 240-kDa sialoadhesin-binding glycoproteins were identified as the sialomucins CD43 and P-selectin glycoprotein ligand 1 (CD162), respectively. CD43 expressed in COS cells supported increased binding to immobilized sialoadhesin. Finally, sialoadhesin bound different glycoforms of CD43 expressed in Chinese hamster ovary cells, including unbranched (core 1) and branched (core 2) O:-linked glycans, that are normally found on CD43 in resting and activated T cells, respectively. These results identify CD43 as a T cell counterreceptor for sialoadhesin and suggest that in addition to its anti-adhesive role CD43 may promote cell-cell interactions.

AB - Sialoadhesin (Siglec-1) is a macrophage-restricted sialic acid-binding receptor that mediates interactions with hemopoietic cells, including lymphocytes. In this study, we identify sialoadhesin counterreceptors on T lymphocytes. Several major glycoproteins (85, 130, 240 kDa) were precipitated by sialoadhesin-Fc fusion proteins from a murine T cell line (TK-1). Binding of sialoadhesin to these glycoproteins was sialic acid dependent and was abolished by mutation of a critical residue (R97A) of the sialic acid binding site in the membrane distal Ig-like domain of sialoadhesin. The 130- and 240-kDa sialoadhesin-binding glycoproteins were identified as the sialomucins CD43 and P-selectin glycoprotein ligand 1 (CD162), respectively. CD43 expressed in COS cells supported increased binding to immobilized sialoadhesin. Finally, sialoadhesin bound different glycoforms of CD43 expressed in Chinese hamster ovary cells, including unbranched (core 1) and branched (core 2) O:-linked glycans, that are normally found on CD43 in resting and activated T cells, respectively. These results identify CD43 as a T cell counterreceptor for sialoadhesin and suggest that in addition to its anti-adhesive role CD43 may promote cell-cell interactions.

KW - Animals

KW - Antigens, CD/metabolism

KW - CHO Cells

KW - COS Cells

KW - Cell Adhesion Molecules/metabolism

KW - Cricetinae

KW - Humans

KW - Interphase/immunology

KW - Leukosialin

KW - Lymphocyte Activation

KW - Membrane Glycoproteins/metabolism

KW - Mice

KW - Protein Binding/immunology

KW - Receptors, Immunologic/metabolism

KW - Sialic Acid Binding Ig-like Lectin 1

KW - Sialoglycoproteins/metabolism

KW - T-Lymphocytes/immunology

KW - Tumor Cells, Cultured

M3 - Article

VL - 166

SP - 3637

EP - 3640

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 6

ER -