Assessing the potential of the two-peptide lantibiotic lichenicidin as a new generation antimicrobial

Barbosa, Joana; Silva, Ítala C.; Caetano, Tânia; Mösker, Eva; Seidel, Maria; Lourenço, Joana; Süssmuth, Roderich D.; Santos, Nuno C.; Gonçalves, Sónia; Mendo, Sónia

doi:10.1007/s11274-021-03196-y

Cited by 7 publications

(4 citation statements)

References 54 publications

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“…Interesting, B. licheniformis CG1, the only strain that inhibited the growth of the mycobacterial strain (see Figure 2 ), contained (in addition to the sequences with 100% similarity to lichenysin) another sequence with 100 % similarity to lichenicidin (see Figure 4 ). Lichenicidin is a lantibiotic compound with antimicrobial activity against a wide range of Gram-positive bacteria [ 35 ], which has been previously shown to be produced by another B. licheniformis strain, i.e., DSM13 [ 36 ]. This antibiotic might account for the antimicrobial activity against M. smegmatis observed by the CG1 strain; however, this hypothesis would require further testing.…”

Section: Resultsmentioning

confidence: 99%

Characterization of Bacillus Strains from Natural Honeybee Products with High Keratinolytic Activity and Antimicrobial Potential

et al. 2023

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Two efficient feather-degrading bacteria were isolated from honeybee samples and identified as Bacillus sonorensis and Bacillus licheniformis based on 16S rRNA and genome sequencing. The strains were able to grow on chicken feathers as the sole carbon and nitrogen sources and degraded the feathers in a few days. The highest keratinase activity was detected by the B. licheniformis CG1 strain (3800 U × mL−1), followed by B. sonorensis AB7 (1450 U × mL−1). Keratinase from B. licheniformis CG1 was shown to be active across a wide range of pH, potentially making this strain advantageous for further industrial applications. All isolates displayed antimicrobial activity against Micrococcus luteus; however, only B. licheniformis CG1 was able to inhibit the growth of Mycobacterium smegmatis. In silico analysis using BAGEL and antiSMASH identified gene clusters associated with the synthesis of non-ribosomal peptide synthetases (NRPS), polyketide synthases (PKSs) and/or ribosomally synthesized and post-translationally modified peptides (RiPPs) in most of the Bacillus isolates. B. licheniformis CG1, the only strain that inhibited the growth of the mycobacterial strain, contained sequences with 100% similarity to lichenysin (also present in the other isolates) and lichenicidin (only present in the CG1 strain). Both compounds have been described to display antimicrobial activity against distinct bacteria. In summary, in this work, we have isolated a strain (B. licheniformis CG1) with promising potential for use in different industrial applications, including animal nutrition, leather processing, detergent formulation and feather degradation.

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Section: Resultsmentioning

confidence: 99%

Characterization of Bacillus Strains from Natural Honeybee Products with High Keratinolytic Activity and Antimicrobial Potential

et al. 2023

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“…Despite the identity of the amino acid sequences of the precursor and the same dehydration sites, the N -terminal domain of Licα contains the Dha5–Cys7 lanthionine bridge and two Dhb residues (in positions 3 and 6). Surprisingly, the β-components of the two lantibiotics (Lchβ and Licβ) are identical and exhibit synergistic effects with both α-peptide variants [ 19 , 37 , 45 , 46 ].…”

Section: Discussionmentioning

confidence: 99%

Specific Binding of the α-Component of the Lantibiotic Lichenicidin to the Peptidoglycan Precursor Lipid II Predetermines Its Antimicrobial Activity

Panina

Balandin

Tsarev

et al. 2023

IJMS

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To date, a number of lantibiotics have been shown to use lipid II—a highly conserved peptidoglycan precursor in the cytoplasmic membrane of bacteria—as their molecular target. The α-component (Lchα) of the two-component lantibiotic lichenicidin, previously isolated from the Bacillus licheniformis VK21 strain, seems to contain two putative lipid II binding sites in its N-terminal and C-terminal domains. Using NMR spectroscopy in DPC micelles, we obtained convincing evidence that the C-terminal mersacidin-like site is involved in the interaction with lipid II. These data were confirmed by the MD simulations. The contact area of lipid II includes pyrophosphate and disaccharide residues along with the first isoprene units of bactoprenol. MD also showed the potential for the formation of a stable N-terminal nisin-like complex; however, the conditions necessary for its implementation in vitro remain unknown. Overall, our results clarify the picture of two component lantibiotics mechanism of antimicrobial action.

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“…Lichenicidin is a class II dipeptide lantibiotic that was first described in B. licheniformis DSM 13 [ 56 ]. Moreover, it has been shown that lichenicidin can be produced by other strains of B. licheniformis , and the structure of its peptides may differ depending on the producing strain [ 57 ]. Furthermore, the production of several bacteriocin-like substances with different characteristics and a wide spectrum of activity against pathogenic bacteria, such as lichenin, bacillocin 490 and P40, was also recorded in B. licheniformis strains [ 58 , 59 ].…”

Section: Discussionmentioning

confidence: 99%

Inhibitory Effect of Bacillus licheniformis Strains Isolated from Canine Oral Cavity

Hudáková

Kačírová

Sondorová

et al. 2022

Life

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Bacillus licheniformis is used in a broad spectrum of areas, including some probiotic preparations for human and veterinary health. Moreover, B. licheniformis strains are known producers of various bioactive substances with antimicrobial and antibiofilm effects. In searching for new potentially beneficial bacteria for oral health, the inhibitory effect of B. licheniformis strains isolated from canine dental biofilm against pathogenic oral bacteria was evaluated. The antimicrobial effect of neutralized cell-free supernatants (nCFS) was assessed in vitro on polystyrene microtiter plates. Furthermore, molecular and morphological analyses were executed to evaluate the production of bioactive substances. To determine the nature of antimicrobial substance present in nCFS of B. licheniformis A-1-5B-AP, nCFS was exposed to the activity of various enzymes. The nCFS of B. licheniformis A-1-5B-AP significantly (p < 0.0001) reduced the growth of Porphyromonas gulae 3/H, Prevotella intermedia 1/P and Streptococcus mutans ATCC 35668. On the other hand, B. licheniformis A-2-11B-AP only significantly (p < 0.0001) inhibited the growth of P. intermedia 1/P and S. mutans ATCC 35668. However, enzyme-treated nCFS of B. licheniformis A-1-5B-AP did not lose its antimicrobial effect and significantly (p < 0.0001) inhibited the growth of Micrococcus luteus DSM 1790. Further studies are needed for the identification of antimicrobial substances.

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Assessing the potential of the two-peptide lantibiotic lichenicidin as a new generation antimicrobial

Cited by 7 publications

References 54 publications

Characterization of Bacillus Strains from Natural Honeybee Products with High Keratinolytic Activity and Antimicrobial Potential

Characterization of Bacillus Strains from Natural Honeybee Products with High Keratinolytic Activity and Antimicrobial Potential

Specific Binding of the α-Component of the Lantibiotic Lichenicidin to the Peptidoglycan Precursor Lipid II Predetermines Its Antimicrobial Activity

Inhibitory Effect of Bacillus licheniformis Strains Isolated from Canine Oral Cavity

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