Covalently Engineered Protein Minibinders with Enhanced Neutralization Efficacy against Escaping SARS-CoV-2 Variants.
Yu HanZhenlin YangHengrui HuHeng ZhangLong ChenKexin LiLinghao KongQianran WangBo LiuManli WangJian LinPeng R ChenPublished in: Journal of the American Chemical Society (2022)
The rapid emergence and spread of escaping mutations of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has significantly challenged our efforts in fighting against the COVID-19 pandemic. A broadly neutralizing reagent against these concerning variants is thus highly desirable for the prophylactic and therapeutic treatments of SARS-CoV-2 infection. We herein report a covalent engineering strategy on protein minibinders for potent neutralization of the escaping variants such as B.1.617.2 (Delta), B.1.617.1 (Kappa), and B.1.1.529 (Omicron) through in situ cross-linking with the spike receptor binding domain (RBD). The resulting covalent minibinder (GlueBinder) exhibited enhanced blockage of RBD-human angiotensin-converting enzyme 2 (huACE2) interaction and more potent neutralization effect against the Delta variant than its noncovalent counterpart as demonstrated on authentic virus. By leveraging the covalent chemistry against escaping mutations, our strategy may be generally applicable for restoring and enhancing the potency of neutralizing antibodies to SARS-CoV-2 and other rapidly evolving viral targets.
Keyphrases
- sars cov
- respiratory syndrome coronavirus
- angiotensin converting enzyme
- copy number
- binding protein
- angiotensin ii
- endothelial cells
- protein protein
- dengue virus
- coronavirus disease
- nuclear factor
- anti inflammatory
- immune response
- inflammatory response
- dna binding
- zika virus
- dna methylation
- small molecule
- genome wide
- transcription factor
- induced pluripotent stem cells
- quality improvement
- pluripotent stem cells