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104. Cyclophilin A‐mediated mitigation of coronavirus SARS‐CoV‐2.

Author

Sekhon, Simranjeet Singh, Shin, Woo‐Ri, Kim, Sang Yong, Jeong, Dong‐Seok, Choi, Wooil, Choi, Bong‐Keun, Min, Jiho, Ahn, Ji‐Young, and Kim, Yang‐Hoon

Subjects
SARS-CoV-2, CORONAVIRUSES, CYCLOPHILINS, CELL receptors, VIRAL proteins
Abstract

Human cyclophilin A (hCypA) is important for the replication of multiple coronaviruses (CoVs), and cyclosporine A inhibitors can suppress CoVs. The emergence of rapidly spreading severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) variants has sparked concerns that mutations affect the binding ability of the spike (S) protein to the angiotensin‐converting enzyme 2 (ACE2) cell receptor, affecting the severity of coronavirus disease (COVID‐19). Far‐western blotting and surface plasmon resonance (SPR) results revealed that hCypA interacts strongly with the viral SARS‐CoV‐2 receptor‐binding domain (RBD), with a binding affinity of 6.85 × 10−8 M. The molecular interaction between hCypA and the viral protein interface was shown using three‐dimensional structural analysis, which revealed the blocking of key residues on the RBD interface by hCypA. The RBD facilitates binding to the ACE2 receptor. The hCypA–S protein complex suppressed the binding of RBD to the ACE2 receptor, which a required event for CoV entry into the host cell. The reliability of this postulated blocking mechanism of the hCypA–SARS‐CoV2 RBD complex with ACE was confirmed by SPR and molecular interaction lateral flow (MILF) strip assay, which offers the immunochromatographic signal read‐outs. The emergence of new SARS‐CoV‐2 variants with key mutations in RBD had a negligible effect on the binding of the RBD variants to hCypA, indicating an effective mitigation strategy for SARS‐CoV‐2 variants. The MILF strip assay results also highlight the neutralizing effect of hCypA by effectively blocking RBD (wild type and its variants) from binding ACE2. Given the importance of hCypA in viral entry regulation, it has the potential to be used as a target for antiviral therapy. [ABSTRACT FROM AUTHOR]

Published
2023
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116. Effects of Extracted from Photosynthetic Bacteria on the Growth and Quality of Lettuce(Lactuca sativa L.) in a LED-Plant Factory

Author

Ju-Yong Park, Wee Ji-Hyang, Leehyein, Kim sang yong, Min Jiho, and Kim Yang-Hoon

Subjects
Rhodobacter, biology, Plant factory, food and beverages, Lactuca, biology.organism_classification, chemistry.chemical_compound, Horticulture, chemistry, Dry weight, Chlorogenic acid, Carbon dioxide, Transplanting, Photosynthetic bacteria
Abstract

Photosynthetic bacteria, Rhodobacter spharoides, can grow using carbon dioxide as a carbon source and produce physiologically active compounds. This study was carried out to investigate the impact of R. sphaeroides extract on the growth and quality of lettuce(Lactuca sativa L.) in the LED-plant factory. The concentrations of R. sphaeroides extracts(0, 4, 8 and 12 mg/L) were supplemented in medium on one day and 14 days after transplanting, respectively. The growth of lettuce as affected by extract amount was evaluated at 14, 28 and 35 days after transplanting and the contents of minerals and chlorogenic acid were analyzed at 35 days after transplanting. As a result, higher growth was obtained in the treatment with R. sphaeroides extract than the control. The extract of R. sphaeroides showed the best growth at 4 mg/L concentration(leaf width- 120%, leaf length- 109%, number of leaves- 113%, total leaf area- 144%, fresh weight- top: 153%, root: 142%, dry weight- top: 137%, root: 120%) and the highest effect at the early stage of growth on 14 days after transplanting(leaf width- 115%, leaf length- 123%, number of leaves- 124%, total leaf area- 158%, fresh weight- top: 139%, root: 120%, dry weight- top: 130%, root: 139%). In addition, the extract of 4 mg/L concentration improved the content of minerals and chlorogenic acid contained in lettuce. Therefore, R. sphaeroides extract suggested the possibility of producing high-value crops through promotion of growth and quality improvement of lettuce.

Published
2020

117. Additional file 1 of Structure based innovative approach to analyze aptaprobe–GPC3 complexes in hepatocellular carcinoma

Author

Shin, Woo-Ri, Park, Dae-Young, Kim, Ji Hun, Lee, Jin-Pyo, Thai, Nguyen Quang, Oh, In-Hwan, Sekhon, Simranjeet Singh, Choi, Wooil, Kim, Sung Yeon, Cho, Byung-Kwan, Kim, Sun Chang, Min, Jiho, Ahn, Ji-Young, and Kim, Yang-Hoon

Abstract

Additional file 1: Figure S1. SELEX round eluted aptamer concentration. Figure S2. Surface plasmon resonance (SPR) analysis of the interaction of GPC3 and GPC3 aptamer candidates (GPC3_1 to GPC3_12) using a Biacore X100. Figure S3. Schematic of the GPC3 protein. Figure S4. Comparing the GPC3 protein and aptamer complex conformation by docking simulation. Figures S5. Ligplot+ molecular interaction analysis of aptaprobes with the GPC3. Figures S6. Aptablotting assay and immunodot blot assay. Figures S7. Confocal imaging and fluorescence intensity quantification of FAM-labeled GPC3 aptaprobes in cell line. Figures S8. mRNA expression test to confirm GPC3 expression of in Hela cells, liver cancer cells (HepG2 and Hep3B), and pancreatic cancer cells (PANC-1 and MIA-PaCa). Figures S9. Cell viability using 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide salt (MTT) assay and Seahorse analysis for HepG2 cells treated with different aptaprobe concentrations. Figures S10. Schematic demonstrating the experimental workflow of in vivo GPC3_3 labeling in an intravenously hepatocellular carcinoma (HCC) xenograft model. Figures S11. Representative images of HCC xenograft model. Table S1. Amino acid residue involved in hydrophobic contact of the between GPC3 protein and aptamer candidate. Table S2. Features of biomolecules for interventional fluorescence imaging of tumors in preclinical studies.

Published
2022
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120. Interspersing CeOx Clusters to the Pt–TiO2 Interfaces for Catalytic Promotion of TiO2-Supported Pt Nanoparticles

Author

Yoo, Mi, primary, Kang, Eunji, additional, Ha, Hyunwoo, additional, Yun, Jieun, additional, Choi, Hyuk, additional, Lee, Ju Hyeok, additional, Kim, Tae Jun, additional, Min, Jiho, additional, Choi, Jin-Seok, additional, Lee, Kug-Seung, additional, Jung, Namgee, additional, Kim, Sungtak, additional, Kim, Chunjoong, additional, Yu, Young-Sang, additional, and Kim, Hyun You, additional

Published
2022
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121. Structure Based Innovative Approach to Analyze Aptaprobe-GPC3 Complexes in Hepatocellular Carcinoma

Author

Shin, Woo-Ri, primary, Park, Dae-Young, additional, Kim, Ji Hun, additional, Lee, Jin-Pyo, additional, Thai, Nguyen Quang, additional, Oh, In-Hwan, additional, Sekhon, Simranjeet Singh, additional, Choi, Wooil, additional, Kim, Sung Yeon, additional, Cho, Byung-Kwan, additional, Kim, Sun Chang, additional, Min, Jiho, additional, Ahn, Ji-Young, additional, and Kim, Yang-Hoon, additional

Published
2022
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