ArticleJournal of immunology (Baltimore, Md. : 1950)2010
Antigen-induced oligomerization of the B cell receptor is an early target of Fc gamma RIIB inhibition.
Article in Journal of immunology (Baltimore, Md. : 1950), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 69 citations in OpenAlex.
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- The Membrane Phase Transition Gives Rise to Responsive Plasma Membrane Structure and Function.Cold Spring Harbor perspectives in biology · 2023Review
- Intersection of FcγRIIB, the microbiome, and checkpoint inhibitors in antitumor immunity.Cancer immunology, immunotherapy : CII · 2021Review
- Expression of inhibitory receptors by B cells in chronic human infectious diseases restricts responses to membrane-associated antigens.Science advances · 2020Article
- The regulators of BCR signaling during B cell activation.Blood science (Baltimore, Md.) · 2019Review
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- B-cell abnormalities in HIV-1 infection: roles for IgG3 and T-bet.Current opinion in HIV and AIDS · 2019Review
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- Human B Cells Engage the NCK/PI3K/RAC1 Axis to Internalize Large Particles via the IgM-BCR.Frontiers in immunology · 2019Article
- Transmembrane domain dependent inhibitory function of FcγRIIB.Protein & cell · 2018Review
- IgG3 regulates tissue-like memory B cells in HIV-infected individuals.Nature immunology · 2018Article
- PI(4,5)P2 determines the threshold of mechanical force-induced B cell activation.The Journal of cell biology · 2018Article
- Epitope-focused immunogens against the CD4-binding site of HIV-1 envelope protein induce neutralizing antibodies against auto- and heterologous viruses.The Journal of biological chemistry · 2018Article
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- Surface engineering for lymphocyte programming.Advanced drug delivery reviews · 2017Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
The FcgammaRIIB is a potent inhibitory coreceptor that blocks BCR signaling in response to immune complexes and, as such, plays a decisive role in regulating Ab responses. The recent application of high-resolution live cell imaging to B cell studies is providing new molecular details of the earliest events in the initiation BCR signaling that follow within seconds of Ag binding. In this study, we report that when colligated to the BCR through immune complexes, the FcgammaRIIB colocalizes with the BCR in microscopic clusters and blocks the earliest events that initiate BCR signaling, including the oligomerization of the BCR within these clusters, the active recruitment of BCRs to these clusters, and the resulting spreading and contraction response. Fluorescence resonance energy transfer analyses indicate that blocking these early events may not require molecular proximity of the cytoplasmic domains of the BCR and FcgammaRIIB, but relies on the rapid and sustained association of FcgammaRIIB with raft lipids in the membrane. These results may provide novel early targets for therapies aimed at regulating the FcgammaRIIB to control Ab responses in autoimmune disease.
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Registered trials
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