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Identification of the ligand-binding domains of CD22, a member of the immunoglobulin superfamily that uniquely binds a sialic acid-dependent ligand.
J Exp Med. 1995 Apr 01; 181(4):1581-6.JE

Abstract

CD22 is a B cell-restricted member of the immunoglobulin (Ig) superfamily that functions as an adhesion receptor for leukocytes and erythrocytes. CD22 is unique among members of the Ig superfamily in that it has been suggested to bind a series of sialic acid-dependent ligands, potentially through different functional domains expressed by different splice variants of CD22. In this study, the epitopes identified by a large panel of function-blocking and non-function-blocking CD22 monoclonal antibodies were localized to specific Ig-like domains, revealing that all function-blocking monoclonal antibodies bound to the first and/or second Ig-like domains. Consistent with a single ligand-binding region, the two amino-terminal domains were the functional unit that mediated CD22 adhesion with lymphocytes, neutrophils, monocytes, and erythrocytes. The predominant cell surface species of CD22 was a full length 140,000 relative molecular mass seven Ig-like domain glycoprotein and a minor 130,000 relative molecular mass form lacking the fourth domain. While the two amino-terminal Ig-like domains of CD22 are structurally similar to those found in other members of the Ig superfamily involved in cell adhesion and containing an amino acid sequence motif associated with integrin recognition, site-directed mutagenesis of critical residues surrounding this motif did not disrupt CD22-mediated adhesion. These results demonstrate that the unique ligand-binding properties of CD22 are distinct from those of other members of the Ig superfamily involved in integrin-mediated cell adhesion.

Authors+Show Affiliations

Department of Immunology, Duke University Medical Center, Durham, North Carolina 27710, USA.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

7535343

Citation

Engel, P, et al. "Identification of the Ligand-binding Domains of CD22, a Member of the Immunoglobulin Superfamily That Uniquely Binds a Sialic Acid-dependent Ligand." The Journal of Experimental Medicine, vol. 181, no. 4, 1995, pp. 1581-6.
Engel P, Wagner N, Miller AS, et al. Identification of the ligand-binding domains of CD22, a member of the immunoglobulin superfamily that uniquely binds a sialic acid-dependent ligand. J Exp Med. 1995;181(4):1581-6.
Engel, P., Wagner, N., Miller, A. S., & Tedder, T. F. (1995). Identification of the ligand-binding domains of CD22, a member of the immunoglobulin superfamily that uniquely binds a sialic acid-dependent ligand. The Journal of Experimental Medicine, 181(4), 1581-6.
Engel P, et al. Identification of the Ligand-binding Domains of CD22, a Member of the Immunoglobulin Superfamily That Uniquely Binds a Sialic Acid-dependent Ligand. J Exp Med. 1995 Apr 1;181(4):1581-6. PubMed PMID: 7535343.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Identification of the ligand-binding domains of CD22, a member of the immunoglobulin superfamily that uniquely binds a sialic acid-dependent ligand. AU - Engel,P, AU - Wagner,N, AU - Miller,A S, AU - Tedder,T F, PY - 1995/4/1/pubmed PY - 1995/4/1/medline PY - 1995/4/1/entrez SP - 1581 EP - 6 JF - The Journal of experimental medicine JO - J Exp Med VL - 181 IS - 4 N2 - CD22 is a B cell-restricted member of the immunoglobulin (Ig) superfamily that functions as an adhesion receptor for leukocytes and erythrocytes. CD22 is unique among members of the Ig superfamily in that it has been suggested to bind a series of sialic acid-dependent ligands, potentially through different functional domains expressed by different splice variants of CD22. In this study, the epitopes identified by a large panel of function-blocking and non-function-blocking CD22 monoclonal antibodies were localized to specific Ig-like domains, revealing that all function-blocking monoclonal antibodies bound to the first and/or second Ig-like domains. Consistent with a single ligand-binding region, the two amino-terminal domains were the functional unit that mediated CD22 adhesion with lymphocytes, neutrophils, monocytes, and erythrocytes. The predominant cell surface species of CD22 was a full length 140,000 relative molecular mass seven Ig-like domain glycoprotein and a minor 130,000 relative molecular mass form lacking the fourth domain. While the two amino-terminal Ig-like domains of CD22 are structurally similar to those found in other members of the Ig superfamily involved in cell adhesion and containing an amino acid sequence motif associated with integrin recognition, site-directed mutagenesis of critical residues surrounding this motif did not disrupt CD22-mediated adhesion. These results demonstrate that the unique ligand-binding properties of CD22 are distinct from those of other members of the Ig superfamily involved in integrin-mediated cell adhesion. SN - 0022-1007 UR - https://www.unboundmedicine.com/medline/citation/7535343/Identification_of_the_ligand_binding_domains_of_CD22_a_member_of_the_immunoglobulin_superfamily_that_uniquely_binds_a_sialic_acid_dependent_ligand_ L2 - https://rupress.org/jem/article-lookup/doi/10.1084/jem.181.4.1581 DB - PRIME DP - Unbound Medicine ER -