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Pilus backbone protein RrgB is the primary structural component of the type 1 pilus (T1P) in Streptococcus pneumoniae, a major human pathogen responsible for pneumonia, meningitis, and sepsis (Frontiers in Cellular and Infection Microbiology, 2023; ASM, 2007). It is a high-molecular-weight polymer formed by the covalent polymerization of RrgB monomers, a process catalyzed by pilus-specific sortases (ResearchGate, 2023; NIH, 2006). Biologically, RrgB plays a critical role in bacterial pathogenesis by mediating adhesion to host epithelial cells and facilitating biofilm formation, which enhances colonization and persistence in the respiratory tract (Frontiers in Cellular and Infection Microbiology, 2023; NIH, 2023). Due to its surface exposure and role in virulence, RrgB is a prominent candidate for next-generation, serotype-independent protein-based vaccines (ASM, 2007; NIH, 2023). Experimental studies have shown that active or passive immunization with RrgB can provide protection against lethal pneumococcal challenge by inducing antibodies that block bacterial attachment and promote opsonophagocytic killing (ASM, 2007; NIH, 2023). However, the existence of multiple RrgB isoforms with limited cross-reactivity presents a challenge for broad-spectrum vaccine development (NIH, 2023).
Induction of protective immunity through neutralizing antibodies that inhibit bacterial adhesion and colonization, and promote opsonophagocytic clearance.
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