Immunons revisited: Binding of multivalent antigens to B cells

Sulzer, Bernhard; Perelson, Alan S.

doi:10.1016/s0161-5890(96)00096-x

Cited by 50 publications

(49 citation statements)

References 11 publications

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“…The structural characteristics of BLS could explain the strong B-cell response elicited when mice were immunized with rBLS. The polymeric nature of BLS (i.e., that of a repetitive and spatially ordered array of the same epitopes) would produce strong signal transduction mediated by B-cell receptors, as has been described previously for a study using haptens as model antigens (32). In this sense, the three-dimensional structure of BLS shows that any given epitope would be presented at five different points separated from each other at a distance of about 50 Å (10).…”

Section: Discussionmentioning

confidence: 80%

BrucellaLumazine Synthase Elicits a Mixed Th1-Th2 Immune Response and Reduces Infection in Mice Challenged withBrucella abortus544 Independently of the Adjuvant Formulation Used

et al. 2003

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Section: Discussionmentioning

confidence: 80%

BrucellaLumazine Synthase Elicits a Mixed Th1-Th2 Immune Response and Reduces Infection in Mice Challenged withBrucella abortus544 Independently of the Adjuvant Formulation Used

et al. 2003

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“…[238][239][240][241][242] The binding of a multivalent antigen to the B cell receptors (BCRs) can activate B cell signaling. To test how the valency of T-cell independent antigens influences antibody production, a series of multivalent ligands were generated using polyacrylamide, dextran, carboxymethyl cellulose, and polyvinyl alcohol as scaffolds.…”

Section: 3a B Cell Antigenmentioning

confidence: 99%

Synthetic Multivalent Ligands as Probes of Signal Transduction

2006

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Cell surface receptors acquire information from the extracellular environment and coordinate intracellular responses. Evidence from biochemical and structural studies indicates that many receptors do not operate as individual entities, but rather as part of higher-order complexes (e.g. dimers and oligomers). Coupling the functions of multiple receptors may endow signaling pathways with the sensitivity and malleability required to govern cellular responses. Moreover, multireceptor signaling complexes may provide a means of spatially segregating otherwise degenerate signaling cascades. Despite the proposed importance of receptor-receptor processes in cellular signaling, questions concerning the mechanisms, extent, and consequences of receptor co-localization and interreceptor communication remain unanswered.Chemical synthesis can provide a variety of compounds with which to address the role of receptor assembly in signal transduction. The focus of this review is one such approach -the use of synthetic multivalent ligands to characterize receptor function. Multivalent ligands can be generated that possess a variety of sizes, shapes, valencies, orientations, and densities of binding elements. Their unique architectures imbue multivalent ligands with the ability to access binding modes not available to monovalent compounds. Multivalent ligands, therefore, are capable of illuminating aspects of inter-receptor processes that are not readily probed using conventional approaches. We suggest that, as focus shifts from investigations of the function of individual proteins and toward the analysis of multi-receptor signaling complexes, multivalent ligands will become even more valuable tools with which to ask sophisticated mechanistic questions. Further, multivalent ligands may provide new opportunities for manipulating receptor systems for the deconvolution of pathways, diagnosis, and, ultimately, the treatment of disease.

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“…230 B cell receptor. Similar to the TCR-induced signaling, the BCR activation signal is shown to be triggered by cross-linking of receptors through multivalent antigen, 10,54,56,[166][167][168]237 thus confirming the necessity of BCR clustering for competent signaling and cell activation. 232 Interestingly, as shown for the pre-BCR in 2007, the ability of the purified recombinant receptor to dimerize indicates that accessory protein(s) are not required for dimerization, and by extension, pre-BCR signaling through multimerization can occur in a ligand-independent fashion.…”

Section: Supportive Evidence For the School Model Of Multichain Recepmentioning

confidence: 65%

The SCHOOL of nature: I. Transmembrane signaling

2010

Self/Nonself

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Cell surface receptors are integral membrane proteins and, as such, consist of three basic domains: extracellular (EC) ligandbinding domains, transmembrane (TM) domains and cytoplasmic (CYTO) signaling (or effector) domains. Upon recognition and binding of a specific ligand, cell surface receptors transmit this information into the interior of the cell, activating intracellular signaling pathways and resulting in a cellular response such as proliferation, differentiation, apoptosis, degranulation, the secretion of preformed and newly formed mediators,

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Immunons revisited: Binding of multivalent antigens to B cells

Cited by 50 publications

References 11 publications

BrucellaLumazine Synthase Elicits a Mixed Th1-Th2 Immune Response and Reduces Infection in Mice Challenged withBrucella abortus544 Independently of the Adjuvant Formulation Used

BrucellaLumazine Synthase Elicits a Mixed Th1-Th2 Immune Response and Reduces Infection in Mice Challenged withBrucella abortus544 Independently of the Adjuvant Formulation Used

Synthetic Multivalent Ligands as Probes of Signal Transduction

The SCHOOL of nature: I. Transmembrane signaling

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