Design and Characterization of a Novel Hybrid Antimicrobial Peptide OM19R Based on Oncocin and MDAP-2

Liu, Lei; Liu, Jie; Cui, Qi; Jia, Boyin; Pei, Zhihua; Odah, Kokou Ayefounin; Wang, Yiming; Dong, Wenlong; Kong, Lingcong; Ma, Huiqin

doi:10.1007/s10989-019-09984-3

Cited by 8 publications

(7 citation statements)

References 33 publications

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“…The conjugation of two different peptides constitutes an efficient approach to obtain novel compounds with improved antimicrobial activity compared to the individual sequences [ 27 , 28 , 29 ]. In fact, the conjugation of sequences with antimicrobial activity has been extensively reported [ 30 , 31 , 32 , 33 , 34 , 35 ]. In this context, we conjugated the antimicrobial peptide BP100 with fragments of natural antimicrobial peptides to obtain peptide conjugates with improved biological activity against plant pathogens than their corresponding monomers [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

A Bifunctional Peptide Conjugate That Controls Infections of Erwinia amylovora in Pear Plants

et al. 2021

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In this paper, peptide conjugates were designed and synthesized by incorporating the antimicrobial undecapeptide BP16 at the C- or N-terminus of the plant defense elicitor peptide flg15, leading to BP358 and BP359, respectively. The evaluation of their in vitro activity against six plant pathogenic bacteria revealed that BP358 displayed MIC values between 1.6 and 12.5 μM, being more active than flg15, BP16, BP359, and an equimolar mixture of BP16 and flg15. Moreover, BP358 was neither hemolytic nor toxic to tobacco leaves. BP358 triggered the overexpression of 6 out of the 11 plant defense-related genes tested. Interestingly, BP358 inhibited Erwinia amylovora infections in pear plants, showing slightly higher efficacy than the mixture of BP16 and flg15, and both treatments were as effective as the antibiotic kasugamycin. Thus, the bifunctional peptide conjugate BP358 is a promising agent to control fire blight and possibly other plant bacterial diseases.

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Section: Introductionmentioning

confidence: 99%

A Bifunctional Peptide Conjugate That Controls Infections of Erwinia amylovora in Pear Plants

et al. 2021

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“…In previous studies, Oncocin was shown to enter the cell by the SbmA transporter. OM19r is an antimicrobial peptide heterozygous by Oncocin with the MDAP-2 fragment (Liu L. et al, 2020). So, the For non-membrane targeted antimicrobial peptides, current research on the mechanism has mainly focused on the effect of antimicrobial peptides on bacterial DNA (Bai et al, 2021) and protein levels (Roy et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

“…Proline-rich antimicrobial peptide OM19r (VDKPPYLPRPRPIRrPGGr-NH 2 ) is a sequence-derived peptide from the existing AMP sequences. The new peptide OM19r of this study was designed by substitution of D-type amino acid at positions 15 and 19 of OM19R ( Cui et al, 2021 ), while OM19R(VDKPPYLPRPRPIRRPGGR-NH 2 ) was a hybrid obtained from Oncocin and MDAP-2 fragments ( Liu L. et al, 2020 ). OM19r shown the effective restoration the gentamicin (GEN) sensitivity of multidrug resistant E. coli .…”

Section: Introductionmentioning

confidence: 99%

Antibiotic synergist OM19r reverses aminoglycoside resistance in multidrug-resistant Escherichia coli

Cui

Liu

et al. 2023

Front. Microbiol.

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IntroductionThe continued emergence and spread of multidrug-resistant (MDR) bacterial pathogens require a new strategy to improve the efficacy of existing antibiotics. Proline-rich antimicrobial peptides (PrAMPs) could also be used as antibacterial synergists due to their unique mechanism of action.MethodsUtilizing a series of experiments on membrane permeability, In vitro protein synthesis, In vitro transcription and mRNA translation, to further elucidate the synergistic mechanism of OM19r combined with gentamicin.ResultsA proline-rich antimicrobial peptide OM19r was identified in this study and its efficacy against Escherichia coli B2 (E. coli B2) was evaluated on multiple aspects. OM19r increased antibacterial activity of gentamicin against multidrug-resistance E. coli B2 by 64 folds, when used in combination with aminoglycoside antibiotics. Mechanistically, OM19r induced change of inner membrane permeability and inhibited translational elongation of protein synthesis by entering to E. coli B2 via intimal transporter SbmA. OM19r also facilitated the accumulation of intracellular reactive oxygen species (ROS). In animal models, OM19r significantly improved the efficacy of gentamicin against E. coli B2.DiscussionOur study reveals that OM19r combined with GEN had a strong synergistic inhibitory effect against multi-drug resistant E. coli B2. OM19r and GEN inhibited translation elongation and initiation, respectively, and ultimately affected the normal protein synthesis of bacteria. These findings provide a potential therapeutic option against multidrug-resistant E. coli.

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“…In this study, we focused on trypsin and focused on overcoming its degradation of antibacterial peptides. According to our previous reports, OM19R has high activity against some intestinal pathogenic bacteria such as Escherichia coli and Salmonella [ 29 ]. Therefore, it is likely to be used as an intestinal microbicide in the future.…”

Section: Discussionmentioning

confidence: 99%

“…It has high antibacterial activity against some gram-negative bacteria and low toxicity in vitro. It has high stability against some environmental factors such as physiological salt and serum, but its resistance to trypsin needs to be improved [ 29 ]. We replaced all l -Arginine and l -Lysine in OM19R with d -Arginine and d -Lysine to obtain a new peptide OM19D.…”

Section: Introductionmentioning

confidence: 99%

An Antibacterial Peptide with High Resistance to Trypsin Obtained by Substituting d-Amino Acids for Trypsin Cleavage Sites

et al. 2021

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The poor stability of antibacterial peptide to protease limits its clinical application. Among these limitations, trypsin mainly exists in digestive tract, which is an insurmountable obstacle to orally delivered peptides. OM19R is a random curly polyproline cationic antimicrobial peptide, which has high antibacterial activity against some gram-negative bacteria, but its stability against pancreatin is poor. According to the structure-activity relationship of OM19R, all cationic amino acid residues (l-arginine and l-lysine) at the trypsin cleavage sites were replaced with corresponding d-amino acid residues to obtain the designed peptide OM19D, which not only maintained its antibacterial activity but also enhanced the stability of trypsin. Proceeding high concentrations of trypsin and long-time (such as 10 mg/mL, 8 h) treatment, it still had high antibacterial activity (MIC = 16–32 µg/mL). In addition, OM19D also showed high stability to serum, plasma and other environmental factors. It is similar to its parent peptide in secondary structure and mechanism of action. Therefore, this strategy is beneficial to improve the protease stability of antibacterial peptides.

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Design and Characterization of a Novel Hybrid Antimicrobial Peptide OM19R Based on Oncocin and MDAP-2

Cited by 8 publications

References 33 publications

A Bifunctional Peptide Conjugate That Controls Infections of Erwinia amylovora in Pear Plants

A Bifunctional Peptide Conjugate That Controls Infections of Erwinia amylovora in Pear Plants

Antibiotic synergist OM19r reverses aminoglycoside resistance in multidrug-resistant Escherichia coli

An Antibacterial Peptide with High Resistance to Trypsin Obtained by Substituting d-Amino Acids for Trypsin Cleavage Sites

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