Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen

By J. Pallesen, Nianshuang Wang, Kizzmekia S. Corbett, D. Wrapp, R. Kirchdoerfer, H. Turner, C. Cottrell, M. M. Becker, Lingshu Wang, Wei Shi and 8 more. 2017

1,071 citations recorded by the source corpus.

Subfields: Animal Science and Zoology, 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 Animal Science and Zoology

1. D. Veesler
2. A. Walls
3. M. A. Tortorici
4. J. Shang
5. Yushun Wan
6. A. Tortoricia
7. David Veeslera
8. F. Krammer

In Infectious Diseases

1. D. Veesler
2. A. Walls
3. M. A. Tortorici
4. J. Shang
5. Yushun Wan
6. Alessandro Sette
7. F. Krammer
8. Q. Geng

Citations in the corpus

• Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation (2020, positive): “Finally, the introduction of double proline substitutions, herein 2P, to prevent fusogenic conformational changes of MERS-CoV S 20 and SARS-CoV S 55 was shown to stabilize the prefusion states of these glycoproteins.”
• The human coronavirus HCoV-229E S-protein structure and receptor binding (2019, methodology): “In addition, a dual-proline mutation (Thr871Pro/Ile872Pro) was 174 introduced to stabilize the pre-fusion form as previously described (36).”
• Adaptive immunity to SARS-CoV-2 and COVID-19 (2021, neutral): “, 2020) with trimer stabilization mutations (P-P) (Pallesen et al., 2017; Wrapp et al., 2020).”
• Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2 (2018, background): “Helix linker 2 is critical for the formation of the postfusion helix core, as has been shown in a previous study, which indicated that substitution of the residues in this region with prolines retains the S glycoprotein in the prefusion conformation and prevents conformational rearrangement [7] .”
• Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant (2020, neutral): “Models of coronavirus S-mediated membrane fusion describe ACE2 binding to all three RBD domains in the open conformation as destabilizing the pre-fusion S trimer, leading to dissociation of S1 from S2 and promoting transition to the post-fusion conformation (Pallesen et al., 2017; Walls et al., 2019”
• mRNA Vaccines in the COVID-19 Pandemic and Beyond. (2021, background): “Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen.”
• SARS-CoV-2 Vaccines: Status Report (2020, background): “Unfortunately, older individuals typically respond less well to vaccination because of immune senescence (Sambhara and McElhaney, 2009).”