title: Honing a harder-hitting hammerhead improves broadly neutralizing antibody breadth and potency.
abstract: While current HIV-1 therapies have greatly improved the quality and duration of life for infected individuals, a vaccine to prevent transmission of the virus is lacking. Broadly neutralizing monoclonal antibodies (bnmAbs) with the capacity to neutralize multiple HIV-1 variants have been isolated from HIV-1-infected individuals, and there has been a great effort to investigate how these bnmAbs arise, due their potential for HIV-1 vaccination. In this issue of the JCI, Willis and colleagues apply a computational approach to design variants of the bnmAb PG9 in an attempt to enhance potency and neutralization breadth. One of these variants was able to target multiple PG9-resistant strains, as the result of stabilization of the long heavy chain complementarity determining region 3 (HCDR3). The results of this study provide important insight and a unique approach to optimizing HIV-1 bnmABs.
authors.forename: George K
authors.initials: GK
authors.lastname: Lewis
mesh_terms: D022801:Complementarity Determining Regions / Q000737:chemistry*; D015483:HIV Antibodies / Q000737:chemistry*; D019302:HIV Envelope Protein gp160 / Q000737:chemistry*; D015497:HIV-1; D006801:Humans; D008958:Models, Molecular; D012984:Software
chemical_list: D022801:Complementarity Determining Regions; D015483:HIV Antibodies; D019302:HIV Envelope Protein gp160