Lyb-8.2: A new B cell antigen defined and characterized with a monoclonal antibody

Symington, Frank W.; Bondada, Subbarao; Mosier, Donald E.; Sprent, Jonathan

doi:10.1007/bf00372098

Cited by 41 publications

(21 citation statements)

References 36 publications

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“…38 Mouse CD22 (mCD22) is detected in the cytoplasm early in B-cell development, is absent from the surface of newly emerging IgM ϩ B cells, is present at a low density on the immature B220 lo IgM hi B cells, and is fully expressed by mature B220 hi IgD ϩ B cells of the BM. 39,40 In the periphery, mCD22 is expressed at high levels on all B-cell subsets including follicular and marginal zone B cells and peritoneal B1 cells. However, a minor subset of immature B cells in the spleen recently derived from BM, expresses low density CD22.…”

Section: Discussionmentioning

confidence: 99%

B-cell depletion inhibits arthritis in a collagen-induced arthritis (CIA) model, but does not adversely affect humoral responses in a respiratory syncytial virus (RSV) vaccination model

Dunussi-Joannopoulos¹,

Hancock²,

Kunz³

et al. 2005

Blood

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IntroductionThe pathogenesis of autoimmune diseases involves a complicated network of tissue-damaging mechanisms that are governed primarily by recognition of self-antigens and an imbalance in cytokine production. 1,2 In rheumatoid arthritis (RA), major cell types responsible for chronic inflammation and subsequent cartilage destruction and bone erosion in the joints are macrophages, synovial fibroblasts, neutrophils, and lymphocytes. Recent studies demonstrated that T and B lymphocytes that infiltrate inflamed synovial tissues are often organized into structures that resemble lymphoid follicles. [3][4][5][6][7] Normally, in T-dependent immune responses antigen-activated B cells migrate into lymphoid follicles of lymphoid organs and form germinal centers. Within the unique milieu of the germinal center, hypermutation leads to diversification and selection of the B-cell repertoire for high affinity and differentiation into antibody-secreting plasma cells or memory B cells. [8][9][10] Molecular analysis of B cells isolated from synovial follicular structures during rheumatoid arthritis demonstrated the importance of B cells in local antigen-driven specific immune responses and increased production of rheumatoid factor (RF), the high-affinity antibodies with self-reactivity. 5 Positivity for RF is associated with more aggressive articular disease and higher frequency of extraarticular manifestations. 11 Studies using RA synovium-severe combined immunodeficiency (SCID) mouse chimeras showed that activation of synovial germinal center CD4 ϩ T cells required the presence of B cells, but not macrophages and dendritic cells, raising the possibility that B cells provided critical function in T-cell activation or harbored the relevant antigens. 12 The significance of extranodal lymphoid follicle formation in inflamed RA joints is unknown, and it remains to be defined whether the reaction is a bystander effect induced by the local chronic inflammation or results from an autoimmune reaction directly related to the pathogenesis of the disease.Intriguing evidence on the pathogenic contribution of B cells in the development of arthritis was recently provided using K/BxN T-cell receptor (TCR) transgenic mice, which spontaneously develop joint disorders with many of the clinical, histologic, and immunologic characteristics of human RA. 13 The articular manifestations are caused by arthritogenic antibodies directed against glucose-6-phosphate isomerase, which develop at high titers in K/BxN transgenic mice. [14][15][16] More convincing evidence regarding the pathogenicity of B cells in RA was recently obtained from clinical trials in patients with refractory disease by using B-cell ablation with rituximab (Rituxan), a human chimeric anti-CD20 monoclonal antibody (mAb). 17,18 Expression of CD20, a B-cellspecific transmembrane glycoprotein with similar patterns of expression and function in humans and in mice, emerges on late pre-B cells and is extinguished on plasma cells. 19,20 Anti-CD20 therapy has also been tested in several ot...

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Section: Discussionmentioning

confidence: 99%

B-cell depletion inhibits arthritis in a collagen-induced arthritis (CIA) model, but does not adversely affect humoral responses in a respiratory syncytial virus (RSV) vaccination model

Dunussi-Joannopoulos¹,

Hancock²,

Kunz³

et al. 2005

Blood

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“…The purified mouse anti-human IgG monoclonal antibody (mAb) R10Z8E9 (34) was kindly provided by Professor R. Jefferis and Dr. M. Goodall and is available from Recognition Systems (University of Birmingham Science Park, Birmingham, United Kingdom). The hybridoma CY34.1.2, which produces the mouse (IgG1) anti-mouse CD22 antibody CY34 (35), was obtained from the American Type Culture Collection (Rockville, MD).…”

Section: Methodsmentioning

confidence: 99%

“…The CY34 Epitope Includes Portions of Domains 1 and 2-CY34 is an allele-specific mouse anti-mouse CD22 mAb (35) that has been reported to bind the CD22 BALB/c allele, but not the DBA/2J allele (55). The CD22 C57Bl allele identified in the present study also binds CY34 (28).…”

Section: And D)mentioning

confidence: 99%

Localization of the Putative Sialic Acid-binding Site on the Immunoglobulin Superfamily Cell-surface Molecule CD22

Merwe

Crocker

Vinson

et al. 1996

Journal of Biological Chemistry

132

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B-lymphocyte antigen CD22 is a member of the recently described sialoadhesin family of immunoglobulin-like cell-surface glycoproteins that bind glycoconjugates terminating in sialic acid. One prominent ligand for CD22 is the highly glycosylated leukocyte surface protein CD45. Using surface plasmon resonance spectroscopy, we characterized the interaction of recombinant mouse CD22 with native CD45 purified from rat thymus (CD45-thy). By in situ desialylation and resialylation of immobilized CD45-thy, we show that mouse CD22 binds to the sialoglycoconjugate NeuGc␣2-6Gal␤1-4GlcNAc carried on CD45-thy N-glycans. Previous studies have shown that the sialic acid-binding site lies within the two membrane-distal domains of CD22 (domains 1 and 2), which are V-set and C2-set immunoglobulin superfamily domains, respectively. To further localize the binding site, we have made 42 single amino acid substitutions throughout both domains. All 12 mutations that abrogated binding to CD45-thy without disrupting antibody binding were of residues within the GFCCC؆ ␤-sheet of domain 1. These residues are predicted to form a contiguous binding site centered around an arginine residue in the F strand that is conserved in all members of the sialoadhesin family. Our results provide further evidence that immunoglobulin superfamily cell adhesion molecules use the GFCCC؆ ␤-sheet of membrane-distal V-set domains to bind structurally diverse ligands, suggesting that this surface is favored for cell-cell recognition.Immunoglobulin superfamily (IgSF) 1 domains are probably the commonest domain type involved in cell-surface recognition, being present in ϳ40% of all proteins identified on the surface of leukocytes (1). One possible reason for this is that IgSF domains provide a stable, but versatile, recognition platform, capable of binding to structurally diverse ligands (2). Typically, IgSF cell adhesion molecules bind either to other IgSF molecules or to integrins (3, 4), but recent reports indicate that some IgSF cell adhesion molecules bind carbohydrate ligands (reviewed in Ref. 5). The best characterized of these lectin-like IgSF proteins are a group of homologous proteins (termed the sialoadhesin family) that bind carbohydrate structures terminating in sialic acid (5-7). Members of this family include the leukocyte proteins CD22, sialoadhesin, and CD33 as well as myelin-associated glycoprotein and Schwann cell myelin protein (5-7).CD22 is expressed on a subpopulation of mature B-cells and has been implicated in cell adhesion as well as in modulating signaling through the B-cell antigen receptor (BCR) (reviewed in Ref. 8). CD22 associates loosely with the BCR (9, 10) and is tyrosine-phosphorylated following BCR ligation (11). This leads to association with and activation of the tyrosine phosphatase SHP (12), which can inhibit signaling through the BCR (13-15). The binding of anti-CD22 antibody-coated beads to B-cells decreases the activation threshold of the BCR, presumably by removing CD22 (and associated SHP) from the vicinity of the BCR...

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“…In the BXD RI lines, this variation in the 908 structural gene was found to cosegregate with the Coh, Gpi-1, and Tam-i loci on chromosome 7 (Table 1). A recently identified B-lymphocyte antigen, Lyb-8.2, is encoded by a gene, Lyb-8, that maps to this region also (18). We have called the 908 structural gene RP2, with the designations RP2b and RP2d for alleles carried by strains C57BL/6J and DBA/2J, respectively.…”

mentioning

confidence: 99%

DNA sequence polymorphism in an androgen-regulated gene is associated with alteration in the encoded RNAs.

Elliott¹,

Berger²

1983

Proc. Natl. Acad. Sci. U.S.A.

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We have used plasmid pMK908, whose cDNA insert corresponds to. an androgen-inducible RNA from-mouse kidney, as a probe to study both the complementary genomic DNA and the encoded RNA sequences in several inbred strains ofmice. A polymorphism in the 908 structural gene, revealed by Southern blotting of HindiI-generated DNA fragments, was found to map near the Gpi-1 and Tam-i loci on chromosome 7. The 908 structural gene has been termed RP2. The 908 RNAs constitute a sequence-related group displaying extensive size heterogeneity. This heterogeneity, reflected in the size distribution of the RNA on electrophoretic blots, is controlled by a genetic site that is tightly linked to RP2. Thus, associated with polymorphism at RP2 is a change in the molecular size pattern of encoded transcripts..The mouse kidney offers several advantages in molecular studies of steroid-regulated genes (1, 2). Previously, we isolated a cDNA-containing plasmid, pMK908, that hybridizes to two kidney-specific testosterone-inducible RNAs, the 908 RNAs (3). These RNAs are induced approximately 7-to 10-fold in female mice after testosterone administration in vivo, and make up about 0.5% of the poly(A)-containing RNA in kidney after testosterone induction (3). At least one of the 908 RNAs encodes a 43,000-dalton polypeptide in vitro (3). Study of these RNAs should, therefore, be useful in addressing questions of tissue specificity and hormonal regulation of gene expression.We have been using pMK908 to probe the structure and regulation of the corresponding sequences in the DNA and RNA from several inbred mouse strains. In this paper, we report the identification of polymorphism in the genomic DNA that hybridizes to pMK908 and have used this polymorphism to map the 908 structural gene, RP2, to chromosome 7. In addition, we present evidence that the 908 RNAs are actually a heterogeneous group of RNAs The publication costs ofthis article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.

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Lyb-8.2: A new B cell antigen defined and characterized with a monoclonal antibody

Cited by 41 publications

References 36 publications

B-cell depletion inhibits arthritis in a collagen-induced arthritis (CIA) model, but does not adversely affect humoral responses in a respiratory syncytial virus (RSV) vaccination model

B-cell depletion inhibits arthritis in a collagen-induced arthritis (CIA) model, but does not adversely affect humoral responses in a respiratory syncytial virus (RSV) vaccination model

Localization of the Putative Sialic Acid-binding Site on the Immunoglobulin Superfamily Cell-surface Molecule CD22

DNA sequence polymorphism in an androgen-regulated gene is associated with alteration in the encoded RNAs.

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