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Biology subjects

Cha, J. S.

Publications and source records attributed to Cha, J. S..

2 recordsLinked to original sources

Bridging in vitro and in vivo insights: A PKPD model for effective phage therapy against multidrug-resistant Pseudomonas aeruginosa

Bacteriophage therapy provides a promising solution for multidrug-resistant Pseudomonas aeruginosa. However, optimizing phage combinations and dosages remains challenging. Here, we developed and validated a pharmacokinetic-pharmacodynamic (PKPD) model integrating in vitro and in vivo efficacy data using three phage strains (MP-A, PP-A, and PP-B), administered both alone and in combination. In vitro phage resistance was substantially delayed by combining phages that exhibit collateral sensitivity. However, multiple phage resistance eventually emerged. In vivo, growth of phage-resistant mutants was minimal. Our model suggests that this outcome was due to an initial phage-induced reduction in bacterial load, followed by immune clearance of the phage-resistant bacteria. Simulations indicated that higher phage exposure at the site of infection caused a faster decline in bacterial levels below the immune clearance threshold and prevented excessive immune activation. Overall, this study offers crucial guidance for treatment strategies and highlights the importance of mathematical modeling in advancing phage therapy.

microbiology↗

Computationally-guided design and affinity improvement of a protein binder targeting a specific site on HER2

A protein binder with a desired epitope and binding affinity is critical to the development of therapeutic agents. Here we present computationally-guided design and affinity improvement of a protein binder recognizing a specific site on domain IV of human epidermal growth factor receptor 2 (HER2). As a model, a protein scaffold composed of Leucine-rich repeat (LRR) modules was used. We designed protein binders which appear to bind a target site on domain IV using a computational method. Top 10 designs were expressed and tested with binding assays, and a lead with a low micro-molar binding affinity was selected. Binding affinity of the selected lead was further increased by two-orders of magnitude through mutual feedback between computational and experimental methods. The utility and potential of our approach was demonstrated by determining the binding interface of the developed protein binder through its crystal structure in complex with the HER2 domain IV.

biochemistry↗