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PG16 is a **broadly neutralizing human monoclonal antibody** isolated from HIV-infected individuals that specifically recognizes glycopeptide epitopes within the V1-V2 region of the HIV-1 envelope (Env) glycoprotein. Unlike most antibodies, PG16 has an unusually long and structurally distinct complementarity-determining region H3 (CDR H3), sometimes described as a "hammerhead" or "axe-shaped" domain, which allows it to penetrate the dense glycan shield of the native viral spike[1][2][3][4][7][8]. PG16 can neutralize 70–80% of circulating HIV-1 isolates across clades with high potency, acting by steric inhibition of receptor/coreceptor engagement and viral entry[3][4][6][8]. PG16 (along with its closely related antibody PG9) is a model for HIV vaccine design because of its breadth and mechanism[2][4][5]. It is not a target itself, but rather a therapeutic candidate or research tool evaluated for passive immunization and antiviral strategies[5][6][8].
Binds specifically to glycan-dependent conformational epitopes in the V1-V2 region of HIV-1 envelope glycoprotein, blocking viral entry by neutralizing virions
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