A study published in *Nature* (2011) reports the identification of 17 new monoclonal antibodies (MAbs) with broad and potent neutralizing activity against HIV. These MAbs, derived from four HIV-infected donors with exceptional neutralizing capacity, outperform previously known broadly neutralizing antibodies (bnAbs) such as PG9, PG16, and VRC01 in potency, neutralizing across multiple HIV clades. The MAbs largely recapitulate the neutralization breadth observed in the corresponding donor sera and recognize novel epitopes on the HIV envelope (Env) glycoprotein gp120, offering new targets for vaccine design. Analysis of the neutralization profiles of these MAbs reveals that certain combinations provide significantly better coverage of the diverse global HIV strains than others, suggesting their potential in active or passive immunization strategies. The study highlights the importance of eliciting bnAbs for effective HIV vaccine development, as these antibodies are critical for protection against the high genetic diversity of HIV. The research also identifies that the potency and breadth of the MAbs are influenced by their ability to bind to specific glycans on gp120, with some MAbs recognizing quaternary epitopes similar to those of previously described bnAbs. The findings suggest that the development of an effective HIV vaccine may rely on eliciting a combination of complementary bnAbs, as demonstrated by the isolation of multiple potent and diverse bnAbs from different donors. The study underscores the potential of antibody-based vaccines and provides a foundation for future vaccine design.A study published in *Nature* (2011) reports the identification of 17 new monoclonal antibodies (MAbs) with broad and potent neutralizing activity against HIV. These MAbs, derived from four HIV-infected donors with exceptional neutralizing capacity, outperform previously known broadly neutralizing antibodies (bnAbs) such as PG9, PG16, and VRC01 in potency, neutralizing across multiple HIV clades. The MAbs largely recapitulate the neutralization breadth observed in the corresponding donor sera and recognize novel epitopes on the HIV envelope (Env) glycoprotein gp120, offering new targets for vaccine design. Analysis of the neutralization profiles of these MAbs reveals that certain combinations provide significantly better coverage of the diverse global HIV strains than others, suggesting their potential in active or passive immunization strategies. The study highlights the importance of eliciting bnAbs for effective HIV vaccine development, as these antibodies are critical for protection against the high genetic diversity of HIV. The research also identifies that the potency and breadth of the MAbs are influenced by their ability to bind to specific glycans on gp120, with some MAbs recognizing quaternary epitopes similar to those of previously described bnAbs. The findings suggest that the development of an effective HIV vaccine may rely on eliciting a combination of complementary bnAbs, as demonstrated by the isolation of multiple potent and diverse bnAbs from different donors. The study underscores the potential of antibody-based vaccines and provides a foundation for future vaccine design.