The BceABRS four-component system that is essential for cell envelope stress response is involved in sensing and response to host defence peptides and is required for the biofilm formation and fitness of Streptococcus mutans

Tian, Xiaolin; Salim, Hasan; Dong, Gaofeng; Parcells, Madison; Li, Yung-Hua

doi:10.1099/jmm.0.000733

Cited by 10 publications

(8 citation statements)

References 28 publications

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“…In contrast with wild type S. mutans, mutant strains lacking each bceABRS gene failed to form biofilms in response to a sub-inhibitory concentration of β-defensin. This data suggest that BceABRS also acts as a sensor, promoting a switch to an AMP resistant phenotype upon challenge (Tian et al, 2018).…”

Section: Transport Systems and Efflux Pumpsmentioning

confidence: 76%

“…Streptococcus mutans is an important pathogen that colonizes the human oral cavity being the most important caries agent (Gold et al, 1973). Interestingly, several S. mutans strains have been described as resistant to salivary AMPs and bacitracin (Tsuda et al, 2002;Kitagawa et al, 2011;Tian et al, 2018).…”

Section: Streptococcus Mutansmentioning

confidence: 99%

“…The S. mutans bceABRS operon encodes an ABC transporter (BceAB) and a two-component system BceRS. The entire fourcomponent system was shown to be important for protection against bacitracin, defensins (α and β), LL-37 and histatin (Tian et al, 2018). In contrast with wild type S. mutans, mutant strains lacking each bceABRS gene failed to form biofilms in response to a sub-inhibitory concentration of β-defensin.…”

Section: Transport Systems and Efflux Pumpsmentioning

confidence: 99%

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Resistance Mechanisms to Antimicrobial Peptides in Gram-Positive Bacteria

et al. 2020

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With the alarming increase of infections caused by pathogenic multidrug-resistant bacteria over the last decades, antimicrobial peptides (AMPs) have been investigated as a potential treatment for those infections, directly through their lytic effect or indirectly, due to their ability to modulate the immune system. There are still concerns regarding the use of such molecules in the treatment of infections, such as cell toxicity and host factors that lead to peptide inhibition. To overcome these limitations, different approaches like peptide modification to reduce toxicity and peptide combinations to improve therapeutic efficacy are being tested. Human defense peptides consist of an important part of the innate immune system, against a myriad of potential aggressors, which have in turn developed different ways to overcome the AMPs microbicidal activities. Since the antimicrobial activity of AMPs vary between Gram-positive and Gram-negative species, so do the bacterial resistance arsenal. This review discusses the mechanisms exploited by Gram-positive bacteria to circumvent killing by antimicrobial peptides. Specifically, the most clinically relevant genera, Streptococcus spp., Staphylococcus spp., Enterococcus spp. and Gram-positive bacilli, have been explored.

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Section: Transport Systems and Efflux Pumpsmentioning

confidence: 76%

Section: Streptococcus Mutansmentioning

confidence: 99%

Section: Transport Systems and Efflux Pumpsmentioning

confidence: 99%

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Resistance Mechanisms to Antimicrobial Peptides in Gram-Positive Bacteria

et al. 2020

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“…One specific mechanism of resistance is a detoxification module, consisting of a TCS and an efflux pump belonging to the ATP-binding cassette (ABC) superfamily [48][49][50]. When the presence of LL-37 is detected, the TCS will promote the expression of the transporter, thus resulting in the extrusion of LL-37 [48].…”

Section: Efflux Pumpsmentioning

confidence: 99%

“…Examples of the detoxification modules include YxdJK-LM in Bacillus subtilis [48], and graRS-vraFG and braRSAB in S. aureus [49]. Several bceR-like systems in Gram-positive bacteria have been reported to include AMP detoxifications molecules, with one notable example being the bacitracin resistance module (bceRSAB) of B. subtilis [49,50]. Other examples include the apsRS in Staphylococcus epidermidis and graRS in S. aureus that, in addition to transporting AMPs away from the site of action, are also capable of upregulating the dlt operon and mprF to increase the bacterial cell surface charge [49].…”

Section: Efflux Pumpsmentioning

confidence: 99%

The Potential of Human Peptide LL-37 as an Antimicrobial and Anti-Biofilm Agent

2021

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The rise in antimicrobial resistant bacteria threatens the current methods utilized to treat bacterial infections. The development of novel therapeutic agents is crucial in avoiding a post-antibiotic era and the associated deaths from antibiotic resistant pathogens. The human antimicrobial peptide LL-37 has been considered as a potential alternative to conventional antibiotics as it displays broad spectrum antibacterial and anti-biofilm activities as well as immunomodulatory functions. While LL-37 has shown promising results, it has yet to receive regulatory approval as a peptide antibiotic. Despite the strong antimicrobial properties, LL-37 has several limitations including high cost, lower activity in physiological environments, susceptibility to proteolytic degradation, and high toxicity to human cells. This review will discuss the challenges associated with making LL-37 into a viable antibiotic treatment option, with a focus on antimicrobial resistance and cross-resistance as well as adaptive responses to sub-inhibitory concentrations of the peptide. The possible methods to overcome these challenges, including immobilization techniques, LL-37 delivery systems, the development of LL-37 derivatives, and synergistic combinations will also be considered. Herein, we describe how combination therapy and structural modifications to the sequence, helicity, hydrophobicity, charge, and configuration of LL-37 could optimize the antimicrobial and anti-biofilm activities of LL-37 for future clinical use.

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