Evaluation of Amyloid Inhibitor Efficiency to Block Bacterial Survival

Busi, Florent; Turbant, Florian; Waeytens, Jehan; Hamoui, Omar El; Wien, Frank; Arluison, Véronique

doi:10.1007/978-1-0716-2529-3_11

Cited by 4 publications

(3 citation statements)

References 54 publications

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“…As expected, the SRCD spectra showed that, in the absence of EGCG, MccE492 progressively changed its conformation over time with a negative peak at ~218 nm, which is typical of the amyloid β-sheets found in the amyloid cross-beta structure (Figure 4A) [26]. In contrast, in the condition with EGCG, a markedly reduced signal around 218 nm was observed even 48 h after starting the assay (Figure 4B).…”

Section: Egcg Interferes With Mcce492 Secondary Structure Transitions...supporting

confidence: 67%

“…Bacterial functional amyloids may be an alternative simple model for developing and testing potential anti-amyloid molecules. Moreover, since some of these functional amyloids have also been related to bacterial virulence (i.e., biofilm formation, toxins reservoirs), they could also serve as a model to test anti-virulence agents [26]. MccE492 is one candidate protein that could serve this purpose, as it forms typical amyloid fibers in the extracellular space of the producing cells and, thus, can easily be purified from E. coli culture supernatants.…”

Section: Discussionmentioning

confidence: 99%

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The Green Tea Polyphenol Epigallocatechin-Gallate (EGCG) Interferes with Microcin E492 Amyloid Formation

Aguilera,

Berríos-Pastén,

Veloso

et al. 2023

Molecules

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Microcin E492 (MccE492) is an antimicrobial peptide and proposed virulence factor produced by some Klebsiella pneumoniae strains, which, under certain conditions, form amyloid fibers, leading to the loss of its antibacterial activity. Although this protein has been characterized as a model functional amyloid, the secondary structure transitions behind its formation, and the possible effect of molecules that inhibit this process, have not been investigated. In this study, we examined the ability of the green tea flavonoid epigallocatechin gallate (EGCG) to interfere with MccE492 amyloid formation. Aggregation kinetics followed by thioflavin T binding were used to monitor amyloid formation in the presence or absence of EGCG. Additionally, synchrotron radiation circular dichroism (SRCD) and transmission electron microscopy (TEM) were used to study the secondary structure, thermal stability, and morphology of microcin E492 fibers. Our results showed that EGCG significantly inhibited the formation of the MccE492 amyloid, resulting in mainly amorphous aggregates and small oligomers. However, these aggregates retained part of the β-sheet SRCD signal and a high resistance to heat denaturation, suggesting that the aggregation process is sequestered or deviated at some stage but not completely prevented. Thus, EGCG is an interesting inhibitor of the amyloid formation of MccE492 and other bacterial amyloids.

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Section: Egcg Interferes With Mcce492 Secondary Structure Transitions...supporting

confidence: 67%

Section: Discussionmentioning

confidence: 99%

The Green Tea Polyphenol Epigallocatechin-Gallate (EGCG) Interferes with Microcin E492 Amyloid Formation

Aguilera,

Berríos-Pastén,

Veloso

et al. 2023

Molecules

Self Cite

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show abstract

“…In this light, it is also worth mentioning that Hfq has been proposed as a potential target to fight different Gram-negative pathogenic bacteria [53]. Moreover, recent studies have demonstrated that it is involved in the E. coli response to antibiotics [54].…”

Section: Discussionmentioning

confidence: 99%

Interactions and Insertion of Escherichia coli Hfq into Outer Membrane Vesicles as Revealed by Infrared and Orientated Circular Dichroism Spectroscopies

Turbant,

Waeytens,

Blache

et al. 2023

IJMS

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The possible carrier role of Outer Membrane Vesicles (OMVs) for small regulatory noncoding RNAs (sRNAs) has recently been demonstrated. Nevertheless, to perform their function, these sRNAs usually need a protein cofactor called Hfq. In this work we show, by using a combination of infrared and circular dichroism spectroscopies, that Hfq, after interacting with the inner membrane, can be translocated into the periplasm, and then be exported in OMVs, with the possibility to be bound to sRNAs. Moreover, we provide evidence that Hfq interacts with and is inserted into OMV membranes, suggesting a role for this protein in the release of sRNA outside the vesicle. These findings provide clues to the mechanism of host–bacteria interactions which may not be defined solely by protein–protein and protein–outer membrane contacts, but also by the exchange of RNAs, and in particular sRNAs.

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Inhibition of Amyloid Protein Aggregation Using Selected Peptidomimetics

Maity

2022

ChemMedChem

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Aberrant protein aggregation leads to the formation of amyloid fibrils. This phenomenon is linked to the development of more than 40 irremediable diseases such as Alzheimer's disease, Parkinson's disease, type 2 diabetes, and cancer. Plenty of research efforts have been given to understanding the underlying mechanism of protein aggregation, associated toxicity, and the development of amyloid inhibitors. Recently, the peptidomimetic approach has emerged as a potential tool to modulate several protein‐protein interactions (PPIs). In this review, we discussed selected peptidomimetic‐based approaches for the modulation of important amyloid proteins (Islet Amyloid Polypeptide, Amyloid Beta, α‐synuclein, mutant p53, and insulin) aggregation. This approach holds a powerful platform for creating an essential stepping stone for the vital development of anti‐amyloid therapeutic agents.

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Evaluation of Amyloid Inhibitor Efficiency to Block Bacterial Survival

Cited by 4 publications

References 54 publications

The Green Tea Polyphenol Epigallocatechin-Gallate (EGCG) Interferes with Microcin E492 Amyloid Formation

The Green Tea Polyphenol Epigallocatechin-Gallate (EGCG) Interferes with Microcin E492 Amyloid Formation

Interactions and Insertion of Escherichia coli Hfq into Outer Membrane Vesicles as Revealed by Infrared and Orientated Circular Dichroism Spectroscopies

Inhibition of Amyloid Protein Aggregation Using Selected Peptidomimetics

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