Antibacterial mechanism of high-mobility group nucleosomal-binding domain 2 on the Gram-negative bacteria Escherichia coli

Li, Heng; Shen, Xiaofei; Zhou, Xianghong; Shi, Yan-E; Deng, Lijing; Ma, Yi; Wang, Xiaoying; Li, Jingyu; Huang, Ning

doi:10.1631/jzus.b1600139

Cited by 7 publications

(5 citation statements)

References 38 publications

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“…In several instances, the isolated alpha-helical domain peptide of HMGN2 has been shown to possess the same antimicrobial activity as full length HMGN2 [81]. In addition, HMGN2 seems to induce autophagy, a novel antimicrobial pathway, and protects bladder epithelial cells from infection by E. coli and other Gram-negative bacteria [82][83][84]. In agreement, recent studies indicated that deficiency in HMGN2 affected macrophage polarization and non-tuberculosis mycobacterial survival in macrophages [85].…”

Section: Immune Functionssupporting

confidence: 53%

Biological Functions of HMGN Chromosomal Proteins

Nanduri

Furusawa

Bustin

2020

IJMS

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Chromatin plays a key role in regulating gene expression programs necessary for the orderly progress of development and for preventing changes in cell identity that can lead to disease. The high mobility group N (HMGN) is a family of nucleosome binding proteins that preferentially binds to chromatin regulatory sites including enhancers and promoters. HMGN proteins are ubiquitously expressed in all vertebrate cells potentially affecting chromatin function and epigenetic regulation in multiple cell types. Here, we review studies aimed at elucidating the biological function of HMGN proteins, focusing on their possible role in vertebrate development and the etiology of disease. The data indicate that changes in HMGN levels lead to cell type-specific phenotypes, suggesting that HMGN optimize epigenetic processes necessary for maintaining cell identity and for proper execution of specific cellular functions. This manuscript contains tables that can be used as a comprehensive resource for all the English written manuscripts describing research aimed at elucidating the biological function of the HMGN protein family.

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Section: Immune Functionssupporting

confidence: 53%

Biological Functions of HMGN Chromosomal Proteins

Nanduri

Furusawa

Bustin

2020

IJMS

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“…Yonezawa [ 53 ] reported that tachyplesin I exerts its antimicrobial activity by binding to DNA, thus inhibiting the synthesis of macromolecules. Moreover, the antimicrobial activity of HMGN2 against E. coli might be associated with its ability to bind to DNA [ 54 ]. Therefore, BCp12 can bind to DNA in vitro and affect gene transcription and translation, consistent with expression changes of cell membrane-related protein findings.…”

Section: Resultsmentioning

confidence: 99%

iTRAQ-Based Quantitative Proteomic Analysis of Antibacterial Mechanism of Milk-Derived Peptide BCp12 against Escherichia coli

Yang

Huang

et al. 2022

Foods

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BCp12 is a novel casein-derived antibacterial peptide with a broad-spectrum antibacterial effect. However, its action mechanism against E. coli is unknown. In this study, the growth curve showed that BCp12 had excellent antibacterial activity against E. coli. Red (propidium iodide staining) and green (fluorescein isothiocyanate staining) fluorescence signals were detected at the edges of the E. coli cells treated with BCp12. scanning electron microscopy (SEM) and transmission electron microscopy (TEM) images showed that E. coli cells became rough and shrunken, and part of the cell contents leaked to form a cavity. Furthermore, the iTRAQ proteome analysis showed that 193 and 174 proteins were significantly up-regulated and down-regulated, respectively, after BCp12 treatment. Four enzymes involved in fatty acid degradation of E. coli were down-regulated, disrupting the synthesis of cell membranes. Molecular docking and gel retardation assays showed that BCp12 could bind to genes encoding four key enzymes involved in the fatty acid degradation pathway through hydrogen bonding and hydrophobic interactions, thus significantly inhibiting their activities. Overall, the results indicate that BCp12 inhibits the growth of E. coli, causing metabolic disorders, thus destroying the structure of cell membranes.

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“…Bacterial infection is still a significant cause of human disease and even death [1] . In recent years, the rapid rise in drug resistance of pathogens, coupled with the rapid emergence of new microbial pathogens, has posed a considerable threat to human health [2–4] . How to improve antibiotic resistance has become a major problem in hospitals and community settings.…”

Section: Introductionmentioning

confidence: 99%

“…[1] In recent years, the rapid rise in drug resistance of pathogens, coupled with the rapid emergence of new microbial pathogens, has posed a considerable threat to human health. [2][3][4] How to improve antibiotic resistance has become a major problem in hospitals and community settings. At present, there are a variety of antimicrobial drugs, but most of the pathogen resistance to these drugs is on the rise.…”

Section: Introductionmentioning

confidence: 99%

Design, Synthesis and Molecular Docking of 1,3,4‐Oxadiazole‐2(3H)‐thione Derivatives Containing 1,4‐Benzodioxane Skeleton as Potential FabH Inhibitors

Sun

Zhang

Chen

et al. 2023

Chemistry & Biodiversity

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Fatty acid biosynthesis is essential for bacterial survival. Of these promising targets, β‐ketoacyl‐acyl carrier protein (ACP) synthase III (FabH) is the most attractive target. A series of novel 1,3,4‐oxadiazole‐2(3H)‐thione derivatives containing 1,4‐benzodioxane skeleton targeting FabH were designed and synthesized. These compounds were determined by 1H‐NMR, 13C‐NMR, MS and further confirmed by crystallographic diffraction study for compound 7m and 7n. Most of the compounds exhibited good inhibitory activity against bacteria by computer‐assisted screening, antibacterial activity test and E. coli FabH inhibitory activity test, wherein compounds 7e and 7q exhibited the most significant inhibitory activities. Besides, compound 7q showed the best E. coli FabH inhibitory activity (IC50=2.45 μΜ). Computational docking studies also showed that compound 7q interacts with FabH critical residues in the active site.

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Antibacterial mechanism of high-mobility group nucleosomal-binding domain 2 on the Gram-negative bacteria Escherichia coli

Abstract: As an antimicrobial peptide (AMP), HMGN2 possessed a good capacity for antibacterial and antibiofilm activities on E. coli K12. This capacity might be associated with disruption of the bacterial membrane and combination of DNA, which might affect the growth and viability of E. coli.

Cited by 7 publications

References 38 publications

Biological Functions of HMGN Chromosomal Proteins

Biological Functions of HMGN Chromosomal Proteins

iTRAQ-Based Quantitative Proteomic Analysis of Antibacterial Mechanism of Milk-Derived Peptide BCp12 against Escherichia coli

Design, Synthesis and Molecular Docking of 1,3,4‐Oxadiazole‐2(3H)‐thione Derivatives Containing 1,4‐Benzodioxane Skeleton as Potential FabH Inhibitors

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