Structure of RSV Fusion Glycoprotein Trimer Bound to a Prefusion-Specific Neutralizing Antibody
By J. McLellan, Man Chen, Sherman S. Leung, Kevin W Graepel, Xiulian Du, Yongping Yang, T. Zhou, U. Baxa, E. Yasuda, T. Beaumont and 7 more. 2013
842 citations recorded by the source corpus.
Subfields: Animal Science and Zoology, Epidemiology, Infectious Diseases
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The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Animal Science and Zoology
In Epidemiology
- Barney S. Graham
- M. Kanekiyo
- Ian A. Wilson
- A. Tortoricia
- M. A. Tortorici
- David Veeslera
- A. Walls
- D. Veesler
In Infectious Diseases
- D. Veesler
- A. Walls
- M. A. Tortorici
- Ian A. Wilson
- A. Tortoricia
- David Veeslera
- David Baker
- Young-Jun Park
Citations in the corpus
- Prefusion F–specific antibodies determine the magnitude of RSV neutralizing activity in human sera (2015, background): “For N-glycan sequon design, surfaceexposed residues were identified on the RSV F molecule that were in close proximity to theD25binding site (10) or themotavizumabbinding site (18).”
- Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy (2016, background): “In the trimer, the connector domains The coronavirus S connector domain and the equivalent paramyxovirus F domain share a related topology, although their tertiary structures are different, and several structural motifs have been added to the latter domain throughout evolution 34, 35 (Fig.”
- AbDesign: an algorithm for combinatorial backbone design guided by natural conformations and sequences (2015, background): “36–38 To be sure, in certain systems selection methods were developed to isolate antibodies that bind specific epitopes on target molecules39–43; yet these capabilities are challenging and rely on specific properties of the target molecule, such as naturally high antigenic variability outside the…”
- Crystal structure of a soluble cleaved HIV-1 envelope trimer (2013, background): “In the same region, electron density also emanates from gp120 C1 (N-terminus) and C5 (C-terminus), implying a close interaction between the gp41 DSL region and the extended structure of the gp120 termini (5, 48).”
- Electron-Microscopy-Based Epitope Mapping Defines Specificities of Polyclonal Antibodies Elicited during HIV-1 BG505 Envelope Trimer Immunization (2018, background): “A different approach based on isolating functional antibodies to the pathogen by studying their interaction with their targets and then designing vaccine candidates has been described (Burton, 2002, 2017; McLellan et al., 2013; Rappuoli and De Gregorio, 2016; Walker et al., 2009).”
- Structural insights into coronavirus entry (2019, background): “edness between the viral fusion proteins of these different viruses and a conservation of their fusion mechanism (McLellan et al., 2013; Walls et al., 2016a, 2017b; Wong et al., 2016; Xu et al., 2015; Yin et al., 2006).”
- Influence of Respiratory Syncytial Virus F Glycoprotein Conformation on Induction of Protective Immune Responses (2016, background): “MAbs D25 and 5C4 were described previously as recognizing epitopes of prefusion-specific antigenic site Ø (29).”
- New Vaccine Design and Delivery Technologies (2019, background): “After solving the structure of the prefusion state in complex with the Fab [36] , mutations that introduced a disulfide bond and cavity-filling hydrophobic side chains were made to F to stabilize the protein in this conformation.”
- Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer (2016, background): “2a-d): (1) a distal moiety constituted by the S1 subunits; (2) a central stem connecting to the viral membrane formed by the S2 subunits.”
- Rapid profiling of RSV antibody repertoires from the memory B cells of naturally infected adult donors (2016, positive): “Antibodies were initially tested for competition with D25, AM14, and MPE8 [three previously described preF-specific antibodies (10, 17, 21)] and motavizumab [an affinitymatured variant of palivizumab that binds to both preF and postF (10, 11, 45)].”