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Broadly neutralizing antibodies are highly specialized antibodies capable of neutralizing multiple divergent strains of viruses with high antigenic variability, such as HIV, influenza, hepatitis C, and coronaviruses[3][5][9]. They exert their effect by binding to conserved protein surfaces on viral envelope proteins, often using unique structural features such as long complementarity-determining region loops or glycan accommodation[1][7][8]. Discovered primarily in rare individuals with chronic infection, bNAbs are the focus of vaccine and therapeutic strategies because, unlike most immune-generated antibodies, they can protect against many viral variants. Their use as drugs is being explored for prevention, early treatment, and possibly cure, due to their dual action of direct viral neutralization and immune modulation[9]. While not conventional molecular targets, bNAbs are both an object of antibody engineering and a set of reagents used to guide vaccine design to elicit similar broadly protective responses.
Direct neutralization of virus by binding conserved protein domains and blocking entry into host cells\nEngagement of immune effector functions (e.g., antibody-dependent cellular cytotoxicity, phagocytosis)\nPotentially supporting viral clearance by activating T cells or innate immunity
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