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PMID: 7684411 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The same epitope on CD22 of B lymphocytes mediates the adhesion of erythrocytes, T and B lymphocytes, neutrophils, and monocytes.

Journal of immunology (Baltimore, Md. : 1950) ·Vol. 150 ·No. 11 ·1993-06-01 ·Pages 4719-32

Engel P, Nojima Y, Rothstein D, Zhou LJ, Wilson GL, Kehrl JH, Tedder TF

Abstract

CD22 is a B lineage-restricted member of the Ig superfamily that serves as an adhesion receptor expressed by mature B lymphocytes. In this study, the ability of different cell types to attach to COS cells transiently transfected with a full-length CD22 cDNA (COS-CD22) was examined to determine the cellular distribution of the ligand for CD22. T and B lymphocytes, monocytes, erythrocytes, and neutrophils formed specific rosettes with COS-CD22 cells at 4 degrees C. A panel of 33 new mAb directed against CD22 were developed to examine the regions of CD22 that mediate adhesion. Four of these mAb, HB22-7, -22, -23, and -33 (at 1 to 5 micrograms/ml) specifically blocked adhesion (75 to 95%) of all cell types to COS-CD22 cells. Each of these mAb cross-blocked each other's binding, suggesting that ligand binding occurs through a single region of CD22. These mAb also identify a region of CD22 distinct from those defined by previously described CD22 mAb. CD22-mediated adhesion of cell lines to COS-CD22 cells was independent of CD45RO and CDw75 expression, and it was not inhibited by mAb against known integrins. Although alpha-2,6-linked sialic acid expressed on the surface of COS cells did not serve as a ligand for CD22, the CD22 ligand may contain a critical sialic acid determinant, as neuraminidase treatment of all target cells eliminated CD22-mediated adhesion. CD22-mediated adhesion was Ca2+/Mg2+ independent, again suggesting that integrins were not involved. An inhibitory substance for CD22-mediated adhesion was found to be present in FCS and some ascites fluid. Analysis of CD22 mRNA and protein revealed that although multiple mRNA splice variants of CD22 mRNA can be detected, only a single protein isoform was detected on the cell surface. Therefore, although the identity of the CD22 ligands remains incompletely characterized, it is possible that a single major ligand is expressed by RBC and leukocytes, which binds to a single region of CD22.

MeSH Terms
Animals Antibodies, Monoclonal/biosynthesis,pharmacology Antigens, CD/chemistry,immunology,physiology Antigens, Differentiation, B-Lymphocyte/chemistry,immunology,physiology B-Lymphocytes/immunology Base Sequence Binding Sites, Antibody/immunology Binding, Competitive/immunology Cell Adhesion/immunology Cell Adhesion Molecules/immunology Cell Line Epitopes/physiology Erythrocytes/immunology Humans Lectins Mice Mice, Inbred BALB C Molecular Sequence Data Monocytes/immunology N-Acetylneuraminic Acid Neutrophils/immunology Peptide Mapping Sialic Acid Binding Ig-like Lectin 2 Sialic Acids/metabolism T-Lymphocytes/immunology
Chemicals
Antibodies, Monoclonal Antigens, CD Antigens, Differentiation, B-Lymphocyte CD22 protein, human Cd22 protein, mouse Cell Adhesion Molecules Epitopes Lectins Sialic Acid Binding Ig-like Lectin 2 Sialic Acids N-Acetylneuraminic Acid
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Engel P
Division of Tumor Immunology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115-6084.
Nojima Y
Rothstein D
Zhou L J
Wilson G L
Kehrl J H
Tedder T F
Article Info
Journal
Journal of immunology (Baltimore, Md. : 1950)
Abbr.
J Immunol
ISSN
0022-1767
Published
1993-06-01
Pages
4719-32
Language
English
Region
United States
NLM ID
2985117R
Subset
IM
Grants
NIAID NIH HHS · AI-26872 · United States
NCI NIH HHS · CA-34183 · United States
NCI NIH HHS · CA-54464 · United States
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