The B cell antigen receptor of class IgD induces a stronger and more prolonged protein tyrosine phosphorylation than that of class IgM.

Kim, Kwang‐Myong; Reth, Michael

doi:10.1084/jem.181.3.1005

Cited by 56 publications

(36 citation statements)

References 61 publications

(87 reference statements)

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“…Potential Ags for IgM a B cells should be no different between 3H9-and 3H9R Tg BWF 1 mice; however, IgM a B cells in 3H9R but not 3H9-Tg BWF 1 mice expressed IgD and could switch V H 3H9 or a different V H generated by editing on the Tg allele to IgG or other constant regions. Recently reported results have indicated that IgD may be important for B cell activation and germinal center formation (37,38). Likewise, signaling through B cell surface IgG is more effective for signaling activation, and consequently, the induction of more clonal expansion than signaling through IgM (39).…”

Section: Anergy In Igm Aϩ B Cells In Conventional 3⌯9-and Knock-in 3hmentioning

confidence: 99%

Tolerance to DNA in (NZB × NZW)F1 Mice That Inherit an Anti-DNA VH as a Conventional μ H Chain Transgene but Not as a VH Knock-in Transgene

Steeves

Marion

2004

The Journal of Immunology

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Lupus-prone (NZB × NZW)F1 (BWF1) mice were made transgenic (Tg) for an anti-DNA Ab inherited either as a conventional VH3H9-μ H chain Tg (3H9-μ) with or without a conventional Vκ8-κ Tg, or a VH3H9 VH knock-in Tg allele (3H9R) with or without a Vκ4 Vκ knock-in Tg allele (Vκ4R). VH3H9 yields an anti-DNA Ab with most L chains including an anti-ssDNA with the Vκ8 Tg and an anti-dsDNA with the Vκ4 Tg. BWF1 mice that inherited the conventional 3H9-μ had normal serum IgM, little to none of which was encoded by 3H9-μ, and only a small percentage of those mice had serum anti-DNA, none of which was transgene encoded. B cells expressing the conventional 3H9-μ Tg were anergic. BWF1 mice that inherited the knock-in 3H9R Tg allele also had normal serum IgM, one-half of which was encoded by 3H9R, and produced anti-DNA encoded by the Tg allele. Most B cells expressing the knock-in 3H9R Tg also had an anergic phenotype. The results indicate that autoimmune-prone BWF1 mice initially develop effective B cell tolerance to DNA through anergy, and anergy was sustained in 3H9-μ Tg peripheral B cells but not in 3H9R Tg B cells. B cells expressing the 3H9R knock-in Tg allele were able to achieve an activation threshold that B cells expressing the 3H9-μ conventional Tg could not. The maintenance of B cell tolerance to DNA in autoimmune-prone BWF1 mice appears to differ from both normal mice and autoimmune-prone MRLlpr/lpr mice.

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Section: Anergy In Igm Aϩ B Cells In Conventional 3⌯9-and Knock-in 3hmentioning

confidence: 99%

Tolerance to DNA in (NZB × NZW)F1 Mice That Inherit an Anti-DNA VH as a Conventional μ H Chain Transgene but Not as a VH Knock-in Transgene

Steeves

Marion

2004

The Journal of Immunology

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“…[8][9][10][11] Attachment of bulky oligosaccharides to V-region glycosylation sites may affect antigen binding. For this study, we first investigated the consequence of FL-type glycosylation for the interaction with antigen of the model BCRs B1-8, specific for hapten 4-hydroxy-3-nitrophenylacetic acid or 4-hydroxy-3-iodo-5-nitrophenylacetyl (NIP) [31][32][33] and for the HyHEL10 (Hy10) BCR specific for hen egg lysozyme (HEL). 34 We therefore introduced N-glycosylation sequons into the model BCRs based on alignments to our own and published sequences.…”

Section: V-region Mannosylation Interferes With Antigen Binding Of Momentioning

confidence: 99%

Lectins from opportunistic bacteria interact with acquired variable-region glycans of surface immunoglobulin in follicular lymphoma

Schneider

Minden

Alkhatib

et al. 2015

Blood

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Key Points• BCR variable-region mannoses in follicular lymphoma are recognized by lectins of common opportunistic bacteria.• Introduction of N-linked sugars into the BCR variable region interferes with antigen recognition.B-cell antigen receptor (BCR) expression is a key feature of most B-cell lymphomas, but the mechanisms of BCR signal induction and the involvement of autoantigen recognition remain unclear. In follicular lymphoma (FL) B cells, BCR expression is retained despite a chromosomal translocation that links the antiapoptotic gene BCL2 to the regulatory elements of immunoglobulin genes, thereby disrupting 1 heavy-chain allele. A remarkable feature of FL-BCRs is the acquisition of potential N-glycosylation sites during somatic hypermutation. The introduced glycans carry mannose termini, which create potential novel binding sites for mannose-specific lectins. Here, we investigated the effect of N-linked variable-region glycosylation for BCR interaction with cognate antigen and with lectins of different origins. N-glycans were found to severely impair BCR specificity and affinity to the initial cognate antigen. In addition, we found that lectins from Pseudomonas aeruginosa and Burkholderia cenocepacia bind and stimulate FL cells. Human exposure to these bacteria can occur by contact with soil and water. In addition, they represent opportunistic pathogens in susceptible hosts. Understanding the role of bacterial lectins might elucidate the pathogenesis of FL and establish novel therapeutic approaches. (Blood. 2015;125(21):3287-3296)

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“…This would indicate that IgM and IgD are redundant receptors. In contrast, differences in tyrosine phosphorylations mediated by IgM or IgD have been observed in transfected B cell lines [30] or between mature and immature B cells [31], respectively. More data will be needed to finally resolve this enigma.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Components of the Murine B Cell Receptor Complex and Their Role in Anti‐Ig Stimulation

1997

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Signal transduction in B cells is mediated by B cell receptor (BCR) complexes that are composed of membrane immunoglobulins (mIg) and additional proteins (e.g. Ig-a and Ig-b) that have been implicated with several aspects of B cell activation. In this paper, experiments are described that have been designed to characterize new components of the BCR and to elucidate their involvement in B cell activation directly after the binding of anti-Ig. The data obtained prove the assumption that IgM is degraded after internalization. Neither immunoglobulin nor the Ig-a/b heterodimer are re-expressed after they have disappeared from the cell surface. The newly detected Ig-associated proteins are neither degradation products of immunoglobulins nor different forms of Ig-a or Ig-b. In addition, they are not recognized by antibodies against any of the kinases known to date. The mIg molecules are linked to the cytoskeleton and internalized. On the other hand, the additional Ig-associated proteins as well as the Ig-a/b heterodimer could not be detected in the detergentinsoluble fraction. The former molecules remain on the B cell surface where they are attached to the unaffected isotype and might interact with downstream members of the signalling cascade. In addition, evidence is presented that the internalization of the receptor complex is not necessary for signal transduction and B cell activation. From these results the authors conclude that the BCR complexes are removed from the cell surface after binding of ligands, probably to prevent further activation of this cell, while the Ig-associated proteins interact with the intracellular components of the signal transduction pathway to promote the further activation of the B cells.

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The B cell antigen receptor of class IgD induces a stronger and more prolonged protein tyrosine phosphorylation than that of class IgM.

Cited by 56 publications

References 61 publications

Tolerance to DNA in (NZB × NZW)F1 Mice That Inherit an Anti-DNA VH as a Conventional μ H Chain Transgene but Not as a VH Knock-in Transgene

Tolerance to DNA in (NZB × NZW)F1 Mice That Inherit an Anti-DNA VH as a Conventional μ H Chain Transgene but Not as a VH Knock-in Transgene

Lectins from opportunistic bacteria interact with acquired variable-region glycans of surface immunoglobulin in follicular lymphoma

Characterization of Components of the Murine B Cell Receptor Complex and Their Role in Anti‐Ig Stimulation

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