Abstract
The cross-linking of the BCR in a multivalent fashion represents a more physiologic means, relative to using unconjugated bivalent anti-Ig, for studying the functional consequences of B cell encounter with specific antigens in vivo. This reflects either the repeating epitope nature of polysaccharides, or the display of a given intact protein in multiple copies on the surface of follicular dendritic cells, macrophages and dendritic cells where they are encountered by B cells.
Highlights
Anti-Ig-dex was originally conceived as a means for modeling B cell receptors (BCR)-mediated B cell activation in response to polysaccharides [1]
Polysaccharides consist of long chains of repeating sugars that are capable of multivalent cross-linking of BCR on the surface of polysaccharide-specific B cells [2]
The conjugation of multiple anti-murine or anti-human Ig antibodies to a high molecular weight polysaccharide such as dextran allows for the highly efficient study of multivalent BCR cross linking, as they can engage virtually all normal B cells derived from the host
Summary
Anti-Ig-dex was originally conceived as a means for modeling BCR-mediated B cell activation in response to polysaccharides [1]. The conjugation of multiple anti-murine or anti-human Ig antibodies to a high molecular weight polysaccharide such as dextran allows for the highly efficient study of multivalent BCR cross linking, as they can engage virtually all normal B cells derived from the host.
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