Structural basis for immunization with postfusion respiratory syncytial virus fusion F glycoprotein (RSV F) to elicit high neutralizing antibody titers

By K. Swanson, E. Settembre, C. Shaw, Antu K Dey, R. Rappuoli, C. Mandl, P. Dormitzer, A. Carfi. 2011

274 citations recorded by the source corpus.

Subfields: Epidemiology, Infectious Diseases

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Epidemiology

1. F. Sallusto
2. A. Lanzavecchia
3. D. Veesler

In Infectious Diseases

1. David Baker
2. D. Veesler

Citations in the corpus

• Induction of Potent Neutralizing Antibody Responses by a Designed Protein Nanoparticle Vaccine for Respiratory Syncytial Virus (2019, background): “Crystal structures of both the prefusion and postfusion forms of RSV F have provided key insights into antigenicity (McLellan et al., 2011, 2013a; Swanson et al., 2011) and spurred the development of next-generation vaccine candidates based on prefusion F.”
• Nonviral delivery of self-amplifying RNA vaccines (2012, methodology): “RSV-F–specific IgG, neutralizing antibody titers and T cell responses were determined essentially as described previously (29) and are included in SI Materials and Methods.”
• Influence of Respiratory Syncytial Virus F Glycoprotein Conformation on Induction of Protective Immune Responses (2016, background): “Recently, soluble forms of hRSV F stabilized in the prefusion conformation were shown to induce higher levels of neutralizing antibodies in mice (30, 32), cotton rats (32), and nonhuman primates (30) (rhesus macaques) than those induced by soluble postfusion F; however, postfusion soluble F, which h”
• Rapid profiling of RSV antibody repertoires from the memory B cells of naturally infected adult donors (2016, unknown): “Subsequent refolding of F into a stable, elongated postfusion conformation (postF) (11, 12) results in fusion of the viral and host-cell membranes.”
• Neutralizing antibodies against the preactive form of respiratory syncytial virus fusion protein offer unique possibilities for clinical intervention (2012, background): “The structure of hRSV_F in the postfusion conformation has been solved recently by X-ray crystallography (26, 27).”
• Structural insights into coronavirus entry (2019, unknown): “3) (McLellan et al., 2011; Swanson et al., 2010 Swanson et al., , 2011 Walls et al., 2016b; Yin et al., 2005) .”
• Respiratory Syncytial Virus Fusion Glycoprotein Expressed in Insect Cells Form Protein Nanoparticles That Induce Protective Immunity in Cotton Rats (2012, background): “Because the hydrophobic C-terminal transmembrane region was left intact, RSV F oligomers formed protein-protein nanoparticles unlike, for example, a soluble RSV F with the fusion, transmembrane, and cytoplasmic domains deleted [13].”