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Structural Basis for Broad and Potent Neutralization of HIV-1 by Antibody VRC01
Designer Anti-HIV Developing a protective HIV vaccine remains a top global health priority. One strategy to identify potential vaccine candidates is to isolate broadly neutralizing antibodies fromExpand
Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
Variable regions 1 and 2 (V1/V2) of human immunodeficiency virus-1 (HIV-1) gp120 envelope glycoprotein are critical for viral evasion of antibody neutralization, and are themselves protected byExpand
Structure of RSV Fusion Glycoprotein Trimer Bound to a Prefusion-Specific Neutralizing Antibody
Building Better Vaccines Vaccines are one of the most effective tools to protect against infectious diseases. Unfortunately, vaccines for diseases with the highest global health burdens, such as HIV,Expand
Focused Evolution of HIV-1 Neutralizing Antibodies Revealed by Structures and Deep Sequencing
Broadly neutralizing antibodies to HIV with similar specificities can be found in multiple HIV-infected individuals. Antibody VRC01 is a human immunoglobulin that neutralizes about 90% of HIV-1Expand
Structure-Based Design of a Fusion Glycoprotein Vaccine for Respiratory Syncytial Virus
Designer Vaccine Respiratory syncytial virus (RSV) is one of the last remaining childhood diseases without an approved vaccine. Using a structure-based approach, McLellan et al. (p. 592) designedExpand
Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies
Antibodies capable of neutralizing HIV-1 often target variable regions 1 and 2 (V1V2) of the HIV-1 envelope, but the mechanism of their elicitation has been unclear. Here we define the developmentalExpand
Structure of Respiratory Syncytial Virus Fusion Glycoprotein in the Postfusion Conformation Reveals Preservation of Neutralizing Epitopes†
ABSTRACT Respiratory syncytial virus (RSV) invades host cells via a type I fusion (F) glycoprotein that undergoes dramatic structural rearrangements during the fusion process. Neutralizing monoclonalExpand
Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G
The HIV-1-envelope (Env) trimer is covered by a glycan shield of ∼90 N-linked oligosaccharides, which comprises roughly half its mass and is a key component of HIV evasion from humoral immunity. ToExpand
Crystal Structure of PG16 and Chimeric Dissection with Somatically Related PG9: Structure-Function Analysis of Two Quaternary-Specific Antibodies That Effectively Neutralize HIV-1
ABSTRACT HIV-1 resists neutralization by most antibodies. Two somatically related human antibodies, PG9 and PG16, however, each neutralize 70 to 80% of circulating HIV-1 isolates. Here we present theExpand
Crystal structure, conformational fixation, and entry-related interactions of mature ligand-free HIV-1 Env
As the sole viral antigen on the HIV-1–virion surface, trimeric Env is a focus of vaccine efforts. Here we present the structure of the ligand-free HIV-1–Env trimer, fix its conformation andExpand