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PG16 is a potent, broadly neutralizing human monoclonal antibody (bNAb) that targets the HIV-1 envelope glycoprotein. It was discovered through a collaborative effort involving the International AIDS Vaccine Initiative (IAVI), Scripps Research, and Theraclone Sciences, isolated from an HIV-infected donor using high-throughput neutralization screening. PG16 specifically recognizes a conserved, quaternary, glycan-dependent epitope located at the apex of the V1/V2 loops of the gp120 subunit of the viral envelope trimer. A distinctive structural feature of PG16 is its exceptionally long heavy-chain complementarity-determining region 3 (HCDR3), which contains a sulfated tyrosine motif that allows the antibody to penetrate the dense glycan shield of the virus. PG16 is primarily investigated for its potential in passive immunization to prevent HIV infection and as a therapeutic component in combination regimens designed to suppress viral replication and prevent viral escape.
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