Biotin–rhizavidin interface (MAPS interface)

The biotin–rhizavidin interface is the fundamental structural linkage within the Multiple Antigen Presenting System (MAPS), a vaccine technology platform designed to induce broad and potent immune responses (Zhang et al., 2013). This interface utilizes the exceptionally high-affinity, non-covalent interaction between biotin (Vitamin B7) and rhizavidin, a dimeric avidin-like protein derived from Rhizobium etli (He et al., 2007). In the MAPS architecture, polysaccharides are chemically conjugated to rhizavidin, which then serves as a scaffold to capture biotinylated protein antigens, creating a stable multivalent complex. This system allows for the simultaneous presentation of T-cell independent (polysaccharide) and T-cell dependent (protein) antigens, mimicking the complexity of whole-cell vaccines while maintaining the precision of subunit vaccines (Luo et al., 2022). While the interface itself is not a therapeutic target for pharmacological inhibition, it is a critical component for the assembly and efficacy of clinical-stage vaccines, such as the 24-valent pneumococcal candidate ASP3772 (GSK, 2022). The stability of the biotin-rhizavidin bond ensures that the complex remains intact in vivo, facilitating the co-delivery of antigens to the same antigen-presenting cell to maximize synergistic immune activation.

Other names

Biotin-rhizavidin complexMAPS scaffold interfaceRhizavidin-biotin couplingMultiple Antigen Presenting System interface

The interface facilitates the non-covalent, high-affinity assembly of biotinylated antigens onto a rhizavidin-functionalized polysaccharide scaffold, enabling co-delivery to antigen-presenting cells.