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Development and simulation of fully glycosylated molecular models of ACE2-Fc fusion proteins and their interaction with the SARS-CoV-2 spike protein binding domain.
PLoS One. 2020; 15(8):e0237295.Plos

Abstract

We develop fully glycosylated computational models of ACE2-Fc fusion proteins which are promising targets for a COVID-19 therapeutic. These models are tested in their interaction with a fragment of the receptor-binding domain (RBD) of the Spike Protein S of the SARS-CoV-2 virus, via atomistic molecular dynamics simulations. We see that some ACE2 glycans interact with the S fragments, and glycans are influencing the conformation of the ACE2 receptor. Additionally, we optimize algorithms for protein glycosylation modelling in order to expedite future model development. All models and algorithms are openly available.

Authors+Show Affiliations

Chemical Engineering, UC Davis, Davis, CA, United States of America.Materials Science and Engineering, UC Davis, Davis, CA, United States of America.Chemical Engineering, UC Davis, Davis, CA, United States of America.Chemical Engineering, UC Davis, Davis, CA, United States of America.Chemical Engineering, UC Davis, Davis, CA, United States of America. Global HealthShare Initiative, UC Davis, Davis, CA, United States of America.Chemical Engineering, UC Davis, Davis, CA, United States of America. Global HealthShare Initiative, UC Davis, Davis, CA, United States of America.Chemical Engineering, UC Davis, Davis, CA, United States of America.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

32756606

Citation

Bernardi, Austen, et al. "Development and Simulation of Fully Glycosylated Molecular Models of ACE2-Fc Fusion Proteins and Their Interaction With the SARS-CoV-2 Spike Protein Binding Domain." PloS One, vol. 15, no. 8, 2020, pp. e0237295.
Bernardi A, Huang Y, Harris B, et al. Development and simulation of fully glycosylated molecular models of ACE2-Fc fusion proteins and their interaction with the SARS-CoV-2 spike protein binding domain. PLoS One. 2020;15(8):e0237295.
Bernardi, A., Huang, Y., Harris, B., Xiong, Y., Nandi, S., McDonald, K. A., & Faller, R. (2020). Development and simulation of fully glycosylated molecular models of ACE2-Fc fusion proteins and their interaction with the SARS-CoV-2 spike protein binding domain. PloS One, 15(8), e0237295. https://doi.org/10.1371/journal.pone.0237295
Bernardi A, et al. Development and Simulation of Fully Glycosylated Molecular Models of ACE2-Fc Fusion Proteins and Their Interaction With the SARS-CoV-2 Spike Protein Binding Domain. PLoS One. 2020;15(8):e0237295. PubMed PMID: 32756606.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Development and simulation of fully glycosylated molecular models of ACE2-Fc fusion proteins and their interaction with the SARS-CoV-2 spike protein binding domain. AU - Bernardi,Austen, AU - Huang,Yihan, AU - Harris,Bradley, AU - Xiong,Yongao, AU - Nandi,Somen, AU - McDonald,Karen A, AU - Faller,Roland, Y1 - 2020/08/05/ PY - 2020/05/05/received PY - 2020/07/23/accepted PY - 2020/8/7/entrez PY - 2020/8/7/pubmed PY - 2020/8/13/medline SP - e0237295 EP - e0237295 JF - PloS one JO - PLoS One VL - 15 IS - 8 N2 - We develop fully glycosylated computational models of ACE2-Fc fusion proteins which are promising targets for a COVID-19 therapeutic. These models are tested in their interaction with a fragment of the receptor-binding domain (RBD) of the Spike Protein S of the SARS-CoV-2 virus, via atomistic molecular dynamics simulations. We see that some ACE2 glycans interact with the S fragments, and glycans are influencing the conformation of the ACE2 receptor. Additionally, we optimize algorithms for protein glycosylation modelling in order to expedite future model development. All models and algorithms are openly available. SN - 1932-6203 UR - https://www.unboundmedicine.com/medline/citation/32756606/Development_and_simulation_of_fully_glycosylated_molecular_models_of_ACE2_Fc_fusion_proteins_and_their_interaction_with_the_SARS_CoV_2_spike_protein_binding_domain_ DB - PRIME DP - Unbound Medicine ER -