Development of chimeric peptides to facilitate the neutralisation of lipopolysaccharides during bactericidal targeting of multidrug-resistant Escherichia coli

Wang, Zhenlong; Li, Xuehui; Teng, Da; Mao, Ruoyu; Hao, Ya; Yang, Na; Wang, Xiao; Li, Zhanzhan; Wang, Xiumin; Wang, Jianhua

doi:10.1038/s42003-020-0761-3

Cited by 45 publications

(35 citation statements)

References 69 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To evaluate the effect of preparations, the samples (0.1 mL) were collected after 0, 15, 30, 45, 60, 120 and 240 min and were sown on LB agar to determine number of colonies after 16–18 h of incubation at 37 °C according to [ 26 ].…”

Section: Methodsmentioning

confidence: 99%

Changes in the Ultrastructure of Staphylococcus aureus Treated with Cationic Peptides and Chlorhexidine

et al. 2020

View full text Add to dashboard Cite

Antimicrobial peptides, including synthetic ones, are becoming increasingly important as a promising tool to fight multidrug-resistant bacteria. We examined the effect of cationic peptides H2N-Arg9-Phe2-C(O)NH2 and H2N-(Lys-Phe-Phe)3-Lys-C(O)NH2 on Staphylococcus aureus, which remains one of the most harmful pathogens. Antiseptic chlorhexidine served as reference preparation. We studied viability of S. aureus and examined its ultrastructure under treatment with 100 µM of R9F2 or (KFF)3K peptides or chlorhexidine using transmission electron microscopy of ultrathin sections. Bacterial cells were sampled as kinetic series starting from 1 min up to 4 h of treatment with preparations. Both peptides caused clearly visible damage of bacteria cell membrane within 1 min. Incubation of S. aureus with R9F2 or (KFF)3K peptides led to cell wall thinning, loss of cytoplasm structure, formation of mesosome-derived multimembrane structures and “decorated fibers” derived from DNA chains. The effect of R9F2 peptides on S. aureus was more severe than the effect of (KFF)3K peptides. Chlorhexidine heavily damaged the bacteria cell wall, in particular in areas of septa formation, while cytoplasm kept its structure within the observation time. Our study showed that cell membrane damage is critical for S. aureus viability; however, we believe that cell wall disorders should also be taken into account when analyzing the effects of the mechanisms of action of antimicrobial peptides (AMPs).

show abstract

Section: Methodsmentioning

confidence: 99%

Changes in the Ultrastructure of Staphylococcus aureus Treated with Cationic Peptides and Chlorhexidine

et al. 2020

View full text Add to dashboard Cite

show abstract

“…However, we find it reasonable to assume that the previous fruitful findings and constructive theories from antibacterial studies with AMPs in vivo and in vitro, such as those concerning the mechanism of entry into the host cell and bactericidal details, might be shared and referenced during antiviral studies; it is confirmed from previous works that AMPs enter the blood circulation through different drug delivery routes, reach various organs, and further internalize into the cells through endocytosis and micropinocytosis [ 116 , 117 , 118 , 119 ]. Undoubtedly, wider and deeper new findings are highly deserving of anticipation and will attract great interest due to the unique advantages of AMPs, including their high penetration into the host cell owing to their intracellular origin, their close compatibility with the host, their hypersensitive early-warning/protection response to infection, and their low drug resistance rate owing to strong penetration and multitargeting of pathogens [ 30 , 120 , 121 , 122 , 123 , 124 , 125 ]. We strongly believe and optimistically expect that with the further elucidation of the structure, expression regulation, and mechanism of action of AMPs as a whole, the factors that limit the development of AMPs will be disclosed and overcome one by one, and more new functions of AMPs will be discovered.…”

Section: Discussionmentioning

confidence: 99%

A Review on the Use of Antimicrobial Peptides to Combat Porcine Viruses

et al. 2020

Self Cite

View full text Add to dashboard Cite

Viral infectious diseases pose a serious threat to animal husbandry, especially in the pig industry. With the rapid, continuous variation of viruses, a series of therapeutic measures, including vaccines, have quickly lost their efficacy, leading to great losses for animal husbandry. Therefore, it is urgent to find new drugs with more stable and effective antiviral activity. Recently, it has been reported that antimicrobial peptides (AMPs) have great potential for development and application in animal husbandry because of their significant antibacterial and antiviral activity, and the antiviral ability of AMPs has become a research hotspot. This article aims to review the research situation of AMPs used to combat viruses in swine production of animal husbandry, clarify the mechanism of action of AMPs on viruses and raise some questions, and explore the future potential of AMPs in animal husbandry.

show abstract

“…The BC probe was used to determine the ability of peptides to bind to LPS [ 54 ]. A total of 0.5 µM LPS was incubated with 5 μM BC in 50 µM Tris buffer (pH 7.4) for 4 h at 37 °C.…”

Section: Methodsmentioning

confidence: 99%

Improved Stability and Activity of a Marine Peptide-N6NH2 against Edwardsiella tarda and Its Preliminary Application in Fish

Han

Wang

et al. 2020

Marine Drugs

Self Cite

View full text Add to dashboard Cite

Edwardsiella tarda can cause fatal gastro-/extraintestinal diseases in fish and humans. Overuse of antibiotics has led to antibiotic resistance and contamination in the environment, which highlights the need to find new antimicrobial agents. In this study, the marine peptide-N6 was amidated at its C-terminus to generate N6NH2. The antibacterial activity of N6 and N6NH2 against E. tarda was evaluated in vitro and in vivo; their stability, toxicity and mode of action were also determined. Minimal inhibitory concentrations (MICs) of N6 and N6NH2 against E. tarda were 1.29–3.2 μM. Both N6 and N6NH2 killed bacteria by destroying the cell membrane of E. tarda and binding to lipopolysaccharide (LPS) and genomic DNA. In contrast with N6, N6NH2 improved the stability toward trypsin, reduced hemolysis (by 0.19% at a concentration of 256 μg/mL) and enhanced the ability to penetrate the bacterial outer and inner membrane. In the model of fish peritonitis caused by E. tarda, superior to norfloxacin, N6NH2 improved the survival rate of fish, reduced the bacterial load on the organs, alleviated the organ injury and regulated the immunity of the liver and kidney. These data suggest that the marine peptide N6NH2 may be a candidate for novel antimicrobial agents against E. tarda infections.

show abstract

Development of chimeric peptides to facilitate the neutralisation of lipopolysaccharides during bactericidal targeting of multidrug-resistant Escherichia coli

Cited by 45 publications

References 69 publications

Changes in the Ultrastructure of Staphylococcus aureus Treated with Cationic Peptides and Chlorhexidine

Changes in the Ultrastructure of Staphylococcus aureus Treated with Cationic Peptides and Chlorhexidine

A Review on the Use of Antimicrobial Peptides to Combat Porcine Viruses

Improved Stability and Activity of a Marine Peptide-N6NH2 against Edwardsiella tarda and Its Preliminary Application in Fish

Contact Info

Product

Resources

About