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28. Simultaneous quantitation of 15 bioactive components in Yupingfeng granules by LC–MS/MS.

Author

Huang, Le‐yi, Chen, Dao‐feng, Wu, Tong, and Gao, Yong‐jian

Subjects
*LIQUID chromatography-mass spectrometry, *BIOACTIVE compounds, *GRADIENT elution (Chromatography), *SAPONINS, *FORMIC acid
Abstract

Yupingfeng granules (YPFG) is commonly used in the treatment of immunological diseases, inflammations, and pulmonary diseases. Several studies have found that chromones, flavones, and saponins were the major bioactive compounds of YPFG. However, few studies have reported accurate quantification methods of these compounds. This study aimed to establish a simple and rapid method by using liquid chromatography–tandem mass spectrometry (LC–MS/MS) to determine 15 bioactive compounds in YPFG. The experimental parameters including extraction methods, extraction solvents, extraction time, solid–liquid ratio, and LC–MS/MS condition were optimized. The linearity, precision, repeatability, stability, and recovery of the established method were evaluated. The contents of 15 bioactive compounds in seven batches of YPFG samples were analyzed by the established method and the results were compared with the values determined by HPLC. The optimal extraction condition was to extract 0.1 g of YPFG by ultrasound with 50 mL 50% ethanol for 30 min. A Waters ACQUITY UPLCBEH C18 column using the 0.1% formic acid water solution and acetonitrile as mobile phase with a gradient elution was applied to the chromatographic separation. The linearity, precision, repeatability, stability, and recovery of the method were within acceptable ranges. Compared with HPLC analysis methods in Chinese Pharmacopoeia and literature, the established method was faster, simpler, more accurate, and more reliable. The method of simultaneous determination of 15 components in YPFG by LC–MS might provide a basis for the study of the bioactive compounds and the improvement of the quality standard of YPFG. [ABSTRACT FROM AUTHOR]

Published
2024
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45. The P1 protein of wheat yellow mosaic virus exerts RNA silencing suppression activity to facilitate virus infection in wheat plants.

Author

Chen, Dao, Zhang, Hui‐Ying, Hu, Shu‐Ming, Tian, Meng‐Yuan, Zhang, Zong‐Ying, Wang, Ying, Sun, Li‐Ying, and Han, Cheng‐Gui

Subjects
*CUCUMBER mosaic virus, *MOSAIC viruses, *VIRUS diseases, *PHYTOPLASMAS, *WHEAT proteins, *RNA viruses
Abstract

SUMMARY: Wheat yellow mosaic virus (WYMV) causes severe wheat viral disease in Asia. However, the viral suppressor of RNA silencing (VSR) encoded by WYMV has not been identified. Here, the P1 protein encoded by WYMV RNA2 was shown to suppress RNA silencing in Nicotiana benthamiana. Mutagenesis assays revealed that the alanine substitution mutant G175A of P1 abolished VSR activity and mutant Y10A VSR activity remained only in younger leaves. P1, but not G175A, interacted with gene silencing‐related protein, N. benthamiana calmodulin‐like protein (NbCaM), and calmodulin‐binding transcription activator 3 (NbCAMTA3), and Y10A interacted with NbCAMTA3 only. Competitive Bimolecular fluorescence complementation and co‐immunoprecipitation assays showed that the ability of P1 disturbing the interaction between NbCaM and NbCAMTA3 was stronger than Y10A, Y10A was stronger than G175A. In vitro transcript inoculation of infectious WYMV clones further demonstrated that VSR‐defective mutants G175A and Y10A reduced WYMV infection in wheat (Triticum aestivum L.), G175A had a more significant effect on virus accumulation in upper leaves of wheat than Y10A. Moreover, RNA silencing, temperature, and autophagy have significant effects on the accumulation of P1 in N. benthamiana. Taken together, WYMV P1 acts as VSR by interfering with calmodulin‐associated antiviral RNAi defense to facilitate virus infection in wheat, which has provided clear insights into the function of P1 in the process of WYMV infection. Significance Statement: This study reveals that the wheat yellow mosaic virus (WYMV) P1 acts as VSR by interfering with calmodulin‐associated antiviral RNAi defense and facilitates virus infection in wheat. Results of our research provide clear insights and solutions for further understanding the role of P1 in process of WYMV infection. [ABSTRACT FROM AUTHOR]

Published
2023
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