The proteolytic activity of Listeria monocytogenes HtrA

Abfalter, Carmen M.; Bernegger, Sabine; Jarzab, Miroslaw; Posselt, Gernot; Ponnuraj, Karthe; Weßler, Silja

doi:10.1186/s12866-019-1633-1

Cited by 10 publications

(7 citation statements)

References 32 publications

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“…Meanwhile, their chaperon activity might facilitate the repair of damaged DNA or altered DNA and RNA structures arising in osmotic stress exposed L. monocytogenes cells. The two-component regulatory system LisRK and the chaperone and serine protease high-temperature requirement A (HtrA) are known to play roles in osmosensing, osmoregulation, and osmotolerance in L. monocytogenes [ 21 , 78 ]. Csps might also exert their influences through these systems.…”

Section: Role Of Csps In L Monocytogenes Stress Tolerancementioning

confidence: 99%

Listeria monocytogenes Cold Shock Proteins: Small Proteins with A Huge Impact

2021

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Listeria monocytogenes has evolved an extensive array of mechanisms for coping with stress and adapting to changing environmental conditions, ensuring its virulence phenotype expression. For this reason, L. monocytogenes has been identified as a significant food safety and public health concern. Among these adaptation systems are cold shock proteins (Csps), which facilitate rapid response to stress exposure. L. monocytogenes has three highly conserved csp genes, namely, cspA, cspB, and cspD. Using a series of csp deletion mutants, it has been shown that L. monocytogenes Csps are important for biofilm formation, motility, cold, osmotic, desiccation, and oxidative stress tolerance. Moreover, they are involved in overall virulence by impacting the expression of virulence-associated phenotypes, such as hemolysis and cell invasion. It is postulated that during stress exposure, Csps function to counteract harmful effects of stress, thereby preserving cell functions, such as DNA replication, transcription and translation, ensuring survival and growth of the cell. Interestingly, it seems that Csps might suppress tolerance to some stresses as their removal resulted in increased tolerance to stresses, such as desiccation for some strains. Differences in csp roles among strains from different genetic backgrounds are apparent for desiccation tolerance and biofilm production. Additionally, hierarchical trends for the different Csps and functional redundancies were observed on their influences on stress tolerance and virulence. Overall current data suggest that Csps have a wider role in bacteria physiology than previously assumed.

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Section: Role Of Csps In L Monocytogenes Stress Tolerancementioning

confidence: 99%

Listeria monocytogenes Cold Shock Proteins: Small Proteins with A Huge Impact

2021

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“…Moreover, a similar study on a different Gram-positive pathogen, Staphylococcus aureus , showed that it is required for motility and growth at high temperatures (Savijoki et al, 2020 ). Lmo0292 protein, also known as “high temperature requirement A” (HtrA), acts as a chaperone and serine protease (Abfalter et al, 2019 ). ClpP and Lmo0292 were present in all conditions.…”

Section: Discussionmentioning

confidence: 99%

A comprehensive investigation of protein expression profiles in L. monocytogenes exposed to thermal abuse, mild acid, and salt stress conditions

D'Onofrio,

Schirone,

Krasteva

et al. 2023

Front. Microbiol.

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Preventing L. monocytogenes infection is crucial for food safety, considering its widespread presence in the environment and its association with contaminated RTE foods. The pathogen's ability to persist under adverse conditions, for example, in food processing facilities, is linked to virulence and resistance mechanisms, including biofilm formation. In this study, the protein expression patterns of two L. monocytogenes 1/2a strains, grown under environmental stressors (mild acidic pH, thermal abuse, and high concentration of NaCl), were investigated. Protein identification and prediction were performed by nLC-ESI-MS/MS and nine different bioinformatic software programs, respectively. Gene enrichment analysis was carried out by STRING v11.05. A total of 1,215 proteins were identified, of which 335 were non-cytosolic proteins and 265 were immunogenic proteins. Proteomic analysis revealed differences in protein expression between L. monocytogenes strains in stressful conditions. The two strains exhibited unique protein expression profiles linked to stress response, virulence, and pathogenesis. Studying the proteomic profiles of such microorganisms provides information about adaptation and potential treatments, highlighting their genetic diversity and demonstrating the utility of bioinformatics and proteomics for a broader analysis of pathogens.

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“…Later, in order to optimize the binding kinetics and functional activity, a more potent H. pylori HtrA inhibitor (Table 1, compound 4) is discovered by computer-assisted de novo molecular design [64]. Even more surprising is that the activity of L. monocytogenes HtrA can also be effectively blocked by compound 4, which suggests the broad-spectrum applicability of this compound [65]. In addition, JO146 (Boc-Val-Pro-ValP (OPh) 2) (Table 1) is screened by targeting the in vitro protease activity of Chlamydia trachomatis HtrA, which completely prevent the formation of viable Chlamydia elementary bodies when used during the replicative phase of development Fig.…”

Section: The Pros and Cons Of Exploiting Htra Inhibitors In Antibacterial Drug Developmentmentioning

confidence: 99%

HtrA family proteases of bacterial pathogens: pros and cons for their therapeutic use

Xue¹,

Liu²,

Xiao

et al. 2021

Clinical Microbiology and Infection

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Background: Because there is an urgent need to develop antibacterial therapies other than antibiotics, research has increasingly focused on the high-temperature-requirement protein A (HtrA) family proteases, which have both serine protease and chaperone activities.Objectives: The research progresses of the role of HtrA family proteases in the pathogenesis of bacterial infections are summarized, and the pros and cons of exploiting HtrA inhibitors in antibacterial drug development are proposed. Sources: A search of PubMed was performed to identify relevant studies. Content: HtrA is essential for bacteria to survive in harsh environments, based on the degradation and refolding of misfolded proteins. Moreover, HtrA family protease can lyse the epithelial cell barrier to promote invasion and can also act as or assist virulence factors to enhance pathogenicity. On the other hand, HtrA secreted by certain bacteria can also affect intra-and interspecies biofilm formation (the mechanism of its promotion or inhibition has not yet been proven). Overall, in view of the role of the HtrA family in promoting bacterial pathogenicity, effective HtrA inhibitors may be an exciting direction for drug development. Therefore, the research progress regarding HtrA inhibitors are summarized and the risks of their application are discussed. Implications: This review will be useful both for investigators involved in the HtrA field as well as those wishing to acquire a basic understanding of the role and potential implementations of HtrA. Ruo-Yi Xue,

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The proteolytic activity of Listeria monocytogenes HtrA

Cited by 10 publications

References 32 publications

Listeria monocytogenes Cold Shock Proteins: Small Proteins with A Huge Impact

Listeria monocytogenes Cold Shock Proteins: Small Proteins with A Huge Impact

A comprehensive investigation of protein expression profiles in L. monocytogenes exposed to thermal abuse, mild acid, and salt stress conditions

HtrA family proteases of bacterial pathogens: pros and cons for their therapeutic use

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