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Characterization of a Potent New-Generation Antimicrobial Peptide of Bacillus.

ABSTRACT: An antimicrobial peptide [Bacillus antimicrobial peptide (BAMP)] produced by Bacillus paralicheniformis was isolated from the Indian traditional fermented food and characterized. The antimicrobial peptide BAMP showed many unique features such as thermostability (4.0-125°C), pH tolerance (pH 2.0-9.0), and resistance to physiological enzymes (trypsin, chymotrypsin, pepsin, proteinase K, protease, and catalase), and food-grade metal salts do not inhibit the activity. The broad spectrum of BAMP (antimicrobial activity) makes it a suitable candidate for food preservation as well as antimicrobial therapy. BAMP was found to exhibit a bacteriostatic effect on Salmonella typhi and controls the viability of Listeria monocytogenes in chicken meat efficiently. BAMP was found to establish eubiosis, as it is not antagonistic to Lactobacillus. Its non-hemolytic nature makes it suitable for therapy. Various genome prediction tools were adopted and applied to understand their localization, gene arrangement, and type of antimicrobials. Founded on its superior functional attributes, BAMP is a potent new-generation antimicrobial peptide.

SUBMITTER: Choyam S

PROVIDER: S-EPMC8421597 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature

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Characterization of a Potent New-Generation Antimicrobial Peptide of Bacillus.

Choyam Shilja S Jain Priyanshi M PM Kammara Rajagopal R

Frontiers in microbiology 20210824

An antimicrobial peptide [Bacillus antimicrobial peptide (BAMP)] produced by Bacillus paralicheniformis was isolated from the Indian traditional fermented food and characterized. The antimicrobial peptide BAMP showed many unique features such as thermostability (4.0-125°C), pH tolerance (pH 2.0-9.0), and resistance to physiological enzymes (trypsin, chymotrypsin, pepsin, proteinase K, protease, and catalase), and food-grade metal salts do not inhibit the activity. The broad spectru ...[more]

PMID: 34504482

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Project description:Due to the emergence of multiple antibiotic resistance in many pathogens, the studies on new antimicrobial peptides (AMPs) have become a priority scientific direction in fundamental and applied biology. Diverse mechanisms underlie the antibacterial action of AMPs. Among them are the effects that AMPs cause on bacterial cell membranes. In this work, we studied the antibacterial activity of a peptide named P4 with the following sequence RTKLWEMLVELGNMDKAVKLWRKLKR that was constructed from two alpha-helical fragments of the influenza virus protein M1 and containing two cholesterol-recognizing amino-acid consensus (CRAC) motifs. Previously we have shown that 50 μM of peptide P4 is toxic to cultured mouse macrophages. In the present work, we have found that peptide P4 inhibits the growth of E. coli and B. subtilis strains at concentrations that are significantly lower than the cytotoxic concentration that was found for macrophages. The half-maximal inhibitory concentration (IC50) for B. subtilis and E. coli cells were 0.07 ± 0.01 μM and 1.9 ± 0.4 μM, respectively. Scramble peptide without CRAC motifs did not inhibit the growth of E. coli cells and was not cytotoxic for macrophages but had an inhibitory effect on the growth of B. subtilis cells (IC50 0.4 ± 0.2 μM). A possible involvement of CRAC motifs and membrane sterols in the mechanism of the antimicrobial action of the P4 peptide is discussed. We assume that in the case of the Gram-negative bacterium E. coli, the mechanism of the toxic action of peptide P4 is related to the interaction of CRAC motifs with sterols that are present in the bacterial membrane, whereas in the case of the Gram-positive bacterium B. subtilis, which lacks sterols, the toxic action of peptide P4 is based on membrane permeabilization through the interaction of the peptide cationic domain and anionic lipids of the bacterial membrane. Whatever the mechanism can be, we report antimicrobial activity of the peptide P4 against the representatives of Gram-positive (B. subtilis) and Gram-negative (E. coli) bacteria.

Project description:In Rhizobium-legume symbiosis, the bacteria are converted into nitrogen-fixing bacteroids. In many legume species, differentiation of the endosymbiotic bacteria is irreversible, culminating in definitive loss of their cell division ability. This terminal differentiation is mediated by plant peptides produced in the symbiotic cells. In Medicago truncatula more than ∼700 nodule-specific cysteine-rich (NCR) peptides are involved in this process. We have shown previously that NCR247 and NCR335 have strong antimicrobial activity on various pathogenic bacteria and identified interaction of NCR247 with many bacterial proteins, including FtsZ and several ribosomal proteins, which prevent bacterial cell division and protein synthesis. In this study we designed and synthetized various derivatives of NCR247, including shorter fragments and various chimeric derivatives. The antimicrobial activity of these peptides was tested on the ESKAPE bacteria; Enterococcus faecalis, Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa, and Escherichia coli as a member of Enterobacteriaceae and in addition Listeria monocytogenes and Salmonella enterica. The 12 amino acid long C-terminal half of NCR247, NCR247C partially retained the antimicrobial activity and preserved the multitarget interactions with partners of NCR247. Nevertheless NCR247C became ineffective on S. aureus, P. aeruginosa, and L. monocytogenes. The chimeric derivatives obtained by fusion of NCR247C with other peptide fragments and particularly with a truncated mastoparan sequence significantly increased bactericidal activity and altered the antimicrobial spectrum. The minimal bactericidal concentration of the most potent derivatives was 1.6 μM, which is remarkably lower than that of most classical antibiotics. The killing activity of the NCR247-based chimeric peptides was practically instant. Importantly, these peptides had no hemolytic activity or cytotoxicity on human cells. The properties of these NCR derivatives make them promising antimicrobials for clinical use.

Dataset Information

Characterization of a Potent New-Generation Antimicrobial Peptide of Bacillus.

Publications

Characterization of a Potent New-Generation Antimicrobial Peptide of <i>Bacillus</i>.

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