Structure of Respiratory Syncytial Virus Fusion Glycoprotein in the Postfusion Conformation Reveals Preservation of Neutralizing Epitopes

By J. McLellan, Yongping Yang, Barney S. Graham, P. Kwong. 2011

395 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. Barney S. Graham
2. F. Sallusto
3. A. Lanzavecchia
4. D. Veesler
5. M. Kanekiyo

In Infectious Diseases

1. D. Veesler
2. David Baker

Citations in the corpus

• Induction of Potent Neutralizing Antibody Responses by a Designed Protein Nanoparticle Vaccine for Respiratory Syncytial Virus (2019, background): “Due to the relative instability of the prefusion conformation, subunit vaccine candidates were until recently limited to themore stable postfusion structure (McLellan et al., 2011; Smith et al., 2012; Swanson et al., 2011).”
• 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, neutral): “3) (McLellan et al., 2011; Swanson et al., 2010 Swanson et al., , 2011 Walls et al., 2016b; Yin et al., 2005) .”
• Prefusion F–specific antibodies determine the magnitude of RSV neutralizing activity in human sera (2015, methodology): “5 mg/ml) expressed from an RSV A2 construct using previously describedmethods (9, 14) was added to 970 ml of diluted samples, whereas the positive control, 970 ml of diluted unadsorbed serum, was further diluted 1:10with 1× PBS.”
• Respiratory Syncytial Virus Fusion Glycoprotein Expressed in Insect Cells Form Protein Nanoparticles That Induce Protective Immunity in Cotton Rats (2012, background): “Deletions of 9 or 10 amino acids of the N-terminus of the F1 fusion peptide have also been reported to increase stability of postfusion F trimers [12,23].”
• Rapid profiling of RSV antibody repertoires from the memory B cells of naturally infected adult donors (2016, methodology): “Here, we have used preF- and postF-stabilized proteins (11, 15), a high-throughput antibody isolation platform, and a structure-guided collection of preF mutants to clonally dissect the human memory B cell response to RSV F in three naturally infected adult donors.”
• Influence of Respiratory Syncytial Virus F Glycoprotein Conformation on Induction of Protective Immune Responses (2016, background): “fusion peptide deleted to avoid aggregation (28, 43).”