Citation
Zhao, Peng, et al. "Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor." Cell Host & Microbe, vol. 28, no. 4, 2020, pp. 586-601.e6.
Zhao P, Praissman JL, Grant OC, et al. Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor. Cell Host Microbe. 2020;28(4):586-601.e6.
Zhao, P., Praissman, J. L., Grant, O. C., Cai, Y., Xiao, T., Rosenbalm, K. E., Aoki, K., Kellman, B. P., Bridger, R., Barouch, D. H., Brindley, M. A., Lewis, N. E., Tiemeyer, M., Chen, B., Woods, R. J., & Wells, L. (2020). Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor. Cell Host & Microbe, 28(4), 586-e6. https://doi.org/10.1016/j.chom.2020.08.004
Zhao P, et al. Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor. Cell Host Microbe. 2020 10 7;28(4):586-601.e6. PubMed PMID: 32841605.
TY - JOUR
T1 - Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor.
AU - Zhao,Peng,
AU - Praissman,Jeremy L,
AU - Grant,Oliver C,
AU - Cai,Yongfei,
AU - Xiao,Tianshu,
AU - Rosenbalm,Katelyn E,
AU - Aoki,Kazuhiro,
AU - Kellman,Benjamin P,
AU - Bridger,Robert,
AU - Barouch,Dan H,
AU - Brindley,Melinda A,
AU - Lewis,Nathan E,
AU - Tiemeyer,Michael,
AU - Chen,Bing,
AU - Woods,Robert J,
AU - Wells,Lance,
Y1 - 2020/08/24/
PY - 2020/06/26/received
PY - 2020/07/22/revised
PY - 2020/08/10/accepted
PY - 2020/8/26/pubmed
PY - 2020/10/27/medline
PY - 2020/8/26/entrez
KW - 3D modeling
KW - ACE2
KW - COVID-19
KW - SARS-CoV-2
KW - Spike protein
KW - coronavirus
KW - glycoprotein
KW - glycosylation
KW - mass spectrometry
KW - molecular dynamics
SP - 586
EP - 601.e6
JF - Cell host & microbe
JO - Cell Host Microbe
VL - 28
IS - 4
N2 - The SARS-CoV-2 betacoronavirus uses its highly glycosylated trimeric Spike protein to bind to the cell surface receptor angiotensin converting enzyme 2 (ACE2) glycoprotein and facilitate host cell entry. We utilized glycomics-informed glycoproteomics to characterize site-specific microheterogeneity of glycosylation for a recombinant trimer Spike mimetic immunogen and for a soluble version of human ACE2. We combined this information with bioinformatics analyses of natural variants and with existing 3D structures of both glycoproteins to generate molecular dynamics simulations of each glycoprotein both alone and interacting with one another. Our results highlight roles for glycans in sterically masking polypeptide epitopes and directly modulating Spike-ACE2 interactions. Furthermore, our results illustrate the impact of viral evolution and divergence on Spike glycosylation, as well as the influence of natural variants on ACE2 receptor glycosylation. Taken together, these data can facilitate immunogen design to achieve antibody neutralization and inform therapeutic strategies to inhibit viral infection.
SN - 1934-6069
UR - https://www.unboundmedicine.com/medline/citation/32841605/Virus_Receptor_Interactions_of_Glycosylated_SARS_CoV_2_Spike_and_Human_ACE2_Receptor_
L2 - https://linkinghub.elsevier.com/retrieve/pii/S1931-3128(20)30457-1
DB - PRIME
DP - Unbound Medicine
ER -