Journal of Microbiology

Research Article

LasB activation in Pseudomonas aeruginosa: Quorum sensing-mediated release of an auto-activation inhibitor: Cheol Seung Lee, Xi-Hui Li, Chae-Ran Jeon, Joon-Hee Lee; J. Microbiol. 2025;63(2):e2411005. Published online February 27, 2025; DOI: https://doi.org/10.71150/jm.2411005

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Abstract PDF: Pseudomonas aeruginosa secretes three major proteases: elastase B (LasB), protease IV (PIV), and elastase A (LasA), which play crucial roles in infection and pathogenesis. These proteases are activated sequentially from LasB in a proteolytic cascade, and LasB was previously thought to undergo auto-activation. However, our previous study suggested that LasB cannot auto-activate independently but requires additional quorum sensing (QS)-dependent factors for activation, as LasB remained inactive in QS-deficient P. aeruginosa (QS-) even under artificial overexpression. In this study, we provide evidence for the existence of a LasB inhibitor in QS- mutants: inactive LasB overexpressed in QS- strains was in its processed form and could be reactivated upon purification; when full-length LasB was overexpressed in Escherichia coli, a heterologous bacterium lacking both LasB activators and inhibitors, the protein underwent normal processing and activation; and purified active LasB was significantly inhibited by culture supernatant (CS) from QS- strains but not by CS from QS+ strains. These findings demonstrate that a LasB inhibitor exists in QS- strains, and in its absence, LasB can undergo auto-activation without requiring an activator. Based on these results, we propose an updated hypothesis: the QS-dependent LasB activator functions by removing the LasB inhibitor rather than acting directly on LasB itself, thus preventing premature LasB activation until QS response is initiated.

Journal Articles

Mutational analysis on stable expression and LasB inhibition of LasB propeptide in Pseudomonas aeruginosa: Youngsun Shin , Xi-Hui Li , Cheol Seung Lee , Joon-Hee Lee; J. Microbiol. 2022;60(7):727-734. Published online May 25, 2022; DOI: https://doi.org/10.1007/s12275-022-1671-5

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Abstract: Three major proteases, elastase B (LasB), protease IV (PIV), and elastase A (LasA) expressed in Pseudomonas aeruginosa play important roles in infections and pathogeneses. These are activated by a proteolytic cascade initiated by the activation of LasB. In this study, we investigated whether LasB could be inhibited using its propeptide (LasBpp). Although LasA and PIV were inhibited by their propeptides, LasB was not inhibited by purified LasBpp because LasB degraded LasBpp. To address this problem, mutant LasBpp variants were constructed to obtain a mutant LasBpp resistant to LasB degradation. A C-terminal deletion series of LasBpp was tested in vivo, and two positive candidates, T2 and T2-1, were selected. However, both caused growth retardation and were unstably expressed in vivo. Since deleting the C-terminal end of LasBpp significantly affected its stable expression, substitution mutations were introduced at the two amino acids near the truncation site of T2-1. The resulting mutants, LasBppE172D, LasBppG173A, and LasBppE172DG173A, significantly diminished LasB activity when overexpressed in vivo and were stably expressed in MW1, a quorum sensing mutant that does not produce LasB. In vitro analysis showed that purified LasBppE172DG173A inhibited LasB activity to a small extent. Summarizing, Cterminal modification of LasBpp profoundly affected the stable expression of LasBpp, and little enhanced the ability of LasBpp to resist degradation by LasB.

Characterization of components of a reducing system for SoxR in the cytoplasmic membrane of Escherichia coli: Kang-Lok Lee , Kyung-Chang Lee , Joon-Hee Lee , Jung-Hye Roe; J. Microbiol. 2022;60(4):387-394. Published online March 28, 2022; DOI: https://doi.org/10.1007/s12275-022-1667-1

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Abstract

A reducing system of SoxR, a regulator of redox-active molecules, was identified as rsxABCDGE gene products and RseC in Escherichia coli through genetic studies. We found that ApbE was an additional component of the reducer system. Bacterial two hybrid analysis revealed that these proteins indeed had multiple interactions among themselves. RseC and RsxB formed the core of the complex, interacting with more than five other components. RsxC, the only cytoplasmic component of the system, interacted with SoxR. It might be linked with the rest of the complex via RsxB. Membrane fractions containing the wild type complex but not the mutant complex reduced purified SoxR using NADH as an electron source. These results suggest that Rsx genes, RseC, and ApbE can form a complex using NAD(P)H to reduce SoxR.

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Antibiofilm effect of biofilm-dispersing agents on clinical isolates of Pseudomonas aeruginosa with various biofilm structures: Soo-Kyoung Kim , Xi-Hui Li , Hyeon-Ji Hwang , Joon-Hee Lee; J. Microbiol. 2018;56(12):902-909. Published online October 25, 2018; DOI: https://doi.org/10.1007/s12275-018-8336-4

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Abstract

Pseudomonas aeruginosa, an opportunistic human pathogen, causes many biofilm-mediated chronic infections. In this study, biofilm structures of various clinical strains of P. aeruginosa isolated from hospitalized patients were examined and their influence on the biofilm-dispersing effects of chemicals was investigated. The clinical isolates formed structurally distinct biofilms that could be classified into three different groups: 1) mushroom-like, 2) thin flat, and 3) thick flat structures. A dispersion of these differently structured biofilms was induced using two biofilm-dispersing agents, anthranilate and sodium nitroprusside (SNP). Although both SNP and anthranilate could disperse all types of biofilms, the thick flat biofilms were dispersed less efficiently than the biofilms of other structures. This suggests that biofilm-dispersing agents have higher potency on the biofilms of porous structures than on densely packed biofilms.

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Reviews

[Minireview] Antibiofilm agents: A new perspective for antimicrobial strategy: Xi-Hui Li , Joon-Hee Lee; J. Microbiol. 2017;55(10):753-766. Published online September 28, 2017; DOI: https://doi.org/10.1007/s12275-017-7274-x

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Abstract

Biofilms are complex microbial architectures that attach to surfaces and encase microorganisms in a matrix composed of self-produced hydrated extracellular polymeric substances (EPSs). In biofilms, microorganisms become much more resistant to antimicrobial treatments, harsh environmental conditions, and host immunity. Biofilm formation by microbial pathogens greatly enhances survival in hosts and causes chronic infections that result in persistent inflammation and tissue damages. Currently, it is believed over 80% of chronic infectious diseases are mediated by biofilms, and it is known that conventional antibiotic medications are inadequate at eradicating these biofilm-mediated infections. This situation demands new strategies for biofilm-associated infections, and currently, researchers focus on the development of antibiofilm agents that are specific to biofilms, but are nontoxic, because it is believed that this prevents the development of drug resistance. Here, we review the most promising antibiofilm agents undergoing intensive research and development.

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MINIREVIEW] Biofilm dispersion in Pseudomonas aeruginosa: Soo-Kyoung Kim , Joon-Hee Lee; J. Microbiol. 2016;54(2):71-85. Published online February 2, 2016; DOI: https://doi.org/10.1007/s12275-016-5528-7

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Abstract

In recent decades, many researchers have written numerous articles about microbial biofilms. Biofilm is a complex community of microorganisms and an example of bacterial group behavior. Biofilm is usually considered a sessile mode of life derived from the attached growth of microbes to surfaces, and most biofilms are embedded in self-produced extracellular matrix composed of extracellular polymeric substances (EPSs), such as polysaccharides, extracellular DNAs (eDNA), and proteins. Dispersal, a mode of biofilm detachment indicates active mechanisms that cause individual cells to separate from the biofilm and return to planktonic life. Since biofilm cells are cemented and surrounded by EPSs, dispersal is not simple to do and many researchers are now paying more attention to this active detachment process. Unlike other modes of biofilm detachment such as erosion or sloughing, which are generally considered passive processes, dispersal occurs as a result of complex spatial differentiation and molecular events in biofilm cells in response to various environmental cues, and there are many biological reasons that force bacterial cells to disperse from the biofilms. In this review, we mainly focus on the spatial differentiation of biofilm that is a prerequisite for dispersal, as well as environmental cues and molecular events related to the biofilm dispersal. More specifically, we discuss the dispersal-related phenomena and mechanisms observed in Pseudomonas aeruginosa, an important opportunistic human pathogen and representative model organism for biofilm study.

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Editorial

EDITORIAL] Perspectives towards antibiotic resistance: from molecules to population: Joon-Hee Lee; J. Microbiol. 2019;57(3):181-184.; DOI: https://doi.org/10.1007/s12275-019-0718-8

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Abstract

For a long time, antibiotics have been ‘magical weapons’ to combat pathogenic microbes. The success of antibiotics is now greatly threatened by resistance to antibiotics and many scientists have already talked about the coming of the postantibiotic era. This special issue is prepared to understand recent research findings and new concepts about antibiotic resistance. Above all, this special issue explores mechanisms for the generation, selection, and spread of antibiotic resistance, and gives insight into what to target to prevent the development of antibiotic resistance. Just as antibiotics came from the concept of “magic bullet”, a breakthrough will come from a new concept based on a profound understanding of antibiotic resistance.

Citations

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Regulation of the sufABCDSE Operon by Fur: Joon-Hee Lee , Won-Sik Yeo , Jung-Hye Roe; J. Microbiol. 2003;41(2):109-114.

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Abstract: A promoter that is inducible by paraquat and menadione, the superoxide generators, independently of soxRS has been found in front of the sufABCDSE operon in Escherichia coli. Based on the observation that SufA is a holomog of IscA that functions in the assembly of iron sulfur cluster and the sufA promoter (sufAp) contains a putative Fur-binding consensus, we investigated whether this gene is regulated by Fur, a ferric uptake regulator. When examined in several sufAp-lacZ chromosomal fusion strains, sufAp was induced by EDTA, an iron chelator and a well-known Fur-inducer. The basal level of sufA expression increased dramatically in fur mutant, suggesting repression of sufAp by Fur. The derepression in fur mutant and EDTA-induction of sufA expression required nucleotides up to -61, where a putative Fur box is located. Purified Fur protein bound to the DNA fragment containing the putative Fur box between -35 and -10 promoter elements. The regulation by Fur and menadione induction of sufAp acted independently. The rpoS mutation increased sufA induction by menadione, suggesting that the stationary sigma factor RpoS acts negatively on sufA induction.

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