Anti-Biofilm Molecules Targeting Functional Amyloids

Matilla-Cuenca, Leticia; Toledo‐Arana, Alejandro; Valle, Jaione

doi:10.3390/antibiotics10070795

Cited by 15 publications

(11 citation statements)

References 137 publications

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“…Importantly, biofilm formation enhances bacteria resistance to antibiotics. This is a big problem that increases the risk of mortality and health economic costs ( Matilla-Cuenca et al, 2021 ; Sikora and Zahra, 2021 ). These infections are mainly caused by opportunistic bacteria such as Enterococcus faecium, Staphylococcus aureus, Klebsiellapneumoniae, Acinetobacter baumannii, or Pseudomonas aeruginosa ( Ma et al, 2019 ; Matilla-Cuenca et al, 2021 ).…”

Section: Bacteria Produce Amyloids To Deal With the Surrounding Worldmentioning

confidence: 99%

“…This is a big problem that increases the risk of mortality and health economic costs ( Matilla-Cuenca et al, 2021 ; Sikora and Zahra, 2021 ). These infections are mainly caused by opportunistic bacteria such as Enterococcus faecium, Staphylococcus aureus, Klebsiellapneumoniae, Acinetobacter baumannii, or Pseudomonas aeruginosa ( Ma et al, 2019 ; Matilla-Cuenca et al, 2021 ). Between them, S. aureus is one of the most common causes of hospital-acquired bacteremia ( Jensen et al, 1999 ).…”

Section: Bacteria Produce Amyloids To Deal With the Surrounding Worldmentioning

confidence: 99%

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Microbiome Impact on Amyloidogenesis

Curto

Lopez²,

Sanchez³

et al. 2022

Front. Mol. Biosci.

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Our life is closely linked to microorganisms, either through a parasitic or symbiotic relationship. The microbiome contains more than 1,000 different bacterial species and outnumbers human genes by 150 times. Worryingly, during the last 10 years, it has been observed a relationship between alterations in microbiota and neurodegeneration. Several publications support the hypothesis that amyloid structures formed by microorganisms may trigger host proteins aggregation. In this review, we collect pieces of evidence supporting that the crosstalk between human and microbiota amyloid proteins could be feasible and, probably, a more common event than expected before. The combination of their outnumbers, the long periods of time that stay in our bodies, and the widespread presence of amyloid proteins in the bacteria Domain outline a worrying scenario. However, the identification of the exact microorganisms and the mechanisms through with they can influence human disease also opens the door to developing a new and diverse set of therapeutic strategies.

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Section: Bacteria Produce Amyloids To Deal With the Surrounding Worldmentioning

confidence: 99%

Section: Bacteria Produce Amyloids To Deal With the Surrounding Worldmentioning

confidence: 99%

Microbiome Impact on Amyloidogenesis

Curto

Lopez²,

Sanchez³

et al. 2022

Front. Mol. Biosci.

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“…At the same time, it should be borne in mind that bacteria have different mechanisms of counteracting protein aggregation, for example, by directing amyloids into inclusion bodies [35]. In addition, some bacteria are capable of using amyloids and amyloid-like protein structures in order to form biofilms [38,39]. Antimicrobial amyloidogenic peptides can be toxic not only to bacteria but also to eukaryotic cells.…”

Section: Introductionmentioning

confidence: 99%

Is It Possible to Create Antimicrobial Peptides Based on the Amyloidogenic Sequence of Ribosomal S1 Protein of P. aeruginosa?

Grishin

Domnin

Кравченко

et al. 2021

IJMS

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The development and testing of new antimicrobial peptides (AMPs) represent an important milestone toward the development of new antimicrobial drugs that can inhibit the growth of pathogens and multidrug-resistant microorganisms such as Pseudomonas aeruginosa, Gram-negative bacteria. Most AMPs achieve these goals through mechanisms that disrupt the normal permeability of the cell membrane, which ultimately leads to the death of the pathogenic cell. Here, we developed a unique combination of a membrane penetrating peptide and peptides prone to amyloidogenesis to create hybrid peptide: “cell penetrating peptide + linker + amyloidogenic peptide”. We evaluated the antimicrobial effects of two peptides that were developed from sequences with different propensities for amyloid formation. Among the two hybrid peptides, one was found with antibacterial activity comparable to antibiotic gentamicin sulfate. Our peptides showed no toxicity to eukaryotic cells. In addition, we evaluated the effect on the antimicrobial properties of amino acid substitutions in the non-amyloidogenic region of peptides. We compared the results with data on the predicted secondary structure, hydrophobicity, and antimicrobial properties of the original and modified peptides. In conclusion, our study demonstrates the promise of hybrid peptides based on amyloidogenic regions of the ribosomal S1 protein for the development of new antimicrobial drugs against P. aeruginosa.

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“…The antibody disrupted biofilms formed by S. typhimurium and eventually enhanced the efficacy of antibiotic treatment in vivo. In mice, a 3H3 injection showed antibiotic conciliated clearance of S. typhimurium biofilms in catheters [211][212][213][214]. Sun et al used a mixture of two MAbs, 12C6/12A1 and 3C1/12A1, which synergistically reduced the attachment and accumulation of S. epidermidis up to 87% [215].…”

Section: Antibodies and Macrophagesmentioning

confidence: 99%

Development of Antibiofilm Therapeutics Strategies to Overcome Antimicrobial Drug Resistance

et al. 2022

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A biofilm is a community of stable microorganisms encapsulated in an extracellular matrix produced by themselves. Many types of microorganisms that are found on living hosts or in the environment can form biofilms. These include pathogenic bacteria that can serve as a reservoir for persistent infections, and are culpable for leading to a broad spectrum of chronic illnesses and emergence of antibiotic resistance making them difficult to be treated. The absence of biofilm-targeting antibiotics in the drug discovery pipeline indicates an unmet opportunity for designing new biofilm inhibitors as antimicrobial agents using various strategies and targeting distinct stages of biofilm formation. The strategies available to control biofilm formation include targeting the enzymes and proteins specific to the microorganism and those involved in the adhesion pathways leading to formation of resistant biofilms. This review primarily focuses on the recent strategies and advances responsible for identifying a myriad of antibiofilm agents and their mechanism of biofilm inhibition, including extracellular polymeric substance synthesis inhibitors, adhesion inhibitors, quorum sensing inhibitors, efflux pump inhibitors, and cyclic diguanylate inhibitors. Furthermore, we present the structure–activity relationships (SAR) of these agents, including recently discovered biofilm inhibitors, nature-derived bioactive scaffolds, synthetic small molecules, antimicrobial peptides, bioactive compounds isolated from fungi, non-proteinogenic amino acids and antibiotics. We hope to fuel interest and focus research efforts on the development of agents targeting the uniquely complex, physical and chemical heterogeneous biofilms through a multipronged approach and combinatorial therapeutics for a more effective control and management of biofilms across diseases.

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Anti-Biofilm Molecules Targeting Functional Amyloids

Cited by 15 publications

References 137 publications

Microbiome Impact on Amyloidogenesis

Microbiome Impact on Amyloidogenesis

Is It Possible to Create Antimicrobial Peptides Based on the Amyloidogenic Sequence of Ribosomal S1 Protein of P. aeruginosa?

Development of Antibiofilm Therapeutics Strategies to Overcome Antimicrobial Drug Resistance

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