Nisin E Is a Novel Nisin Variant Produced by Multiple Streptococcus equinus Strains

Sugrue, Ivan; Hill, Daragh; O’Connor, Paula M.; Day, Linda; Stanton, Catherine; Hill, Colin; Ross, R. Paul

doi:10.3390/microorganisms11020427

Cited by 7 publications

(6 citation statements)

References 63 publications

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“…The amino acid substitution T25S in nisin S involves the formation of a lanthionine bridge that stabilizes the E ring, instead of a 3-methyllanthionine bridge stabilizing the E ring in nisin A ( Figure 6 ). At position 27 and within the E ring, nisin S (H27G) shows a hydrophobic residue (G) while nisin A has a polar amino acid (H), a substitution also observed in nisin P, nisin O, nisin U, nisin U2, and nisin E [ 18 , 20 , 21 , 23 , 56 ]. This substitution could confer nisin S has a stronger ability to permeate membranes and support, in part, its antimicrobial activity against Gram-negative bacteria such as E. coli , something documented for nisin J which has a hydrophobic residue at position 20 of its molecule [ 8 ].…”

Section: Discussionmentioning

confidence: 99%

Nisin S, a Novel Nisin Variant Produced by Ligilactobacillus salivarius P1CEA3

Sevillano

Peña

Lafuente

et al. 2023

IJMS

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Recently, the food industry and the animal farming field have been working on different strategies to reduce the use of antibiotics in animal production. The use of probiotic producers of antimicrobial peptides (bacteriocins) is considered to be a potential solution to control bacterial infections and to reduce the use of antibiotics in animal production. In this study, Ligilactobacillus salivarius P1CEA3, isolated from the gastrointestinal tract (GIT) of pigs, was selected for its antagonistic activity against Gram-positive pathogens of relevance in swine production. Whole genome sequencing (WGS) of L. salivarius P1ACE3 revealed the existence of two gene clusters involved in bacteriocin production, one with genes encoding the class II bacteriocins salivaricin B (SalB) and Abp118, and a second cluster encoding a putative nisin variant. Colony MALDI-TOF MS determinations and a targeted proteomics combined with massive peptide analysis (LC-MS/MS) of the antimicrobial peptides encoded by L. salivarius P1CEA3 confirmed the production of a 3347 Da novel nisin variant, termed nisin S, but not the production of the bacteriocins SalB and Abp118, in the supernatants of the producer strain. This is the first report of a nisin variant encoded and produced by L. salivarius, a bacterial species specially recognized for its safety and probiotic potential.

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Section: Discussionmentioning

confidence: 99%

Nisin S, a Novel Nisin Variant Produced by Ligilactobacillus salivarius P1CEA3

Sevillano

Peña

Lafuente

et al. 2023

IJMS

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“…A wide variety of bacteriocins, belonging to all four main classes (lantibiotics, nonlantibiotics, Class III, and the unusual cyclic peptides), have been identified and characterized from nearly every Streptococcus species, isolated from different environments (GARCIA-GUTIERREZ et al, 2020;WATANABE et al, 2021;CHRISTOPHERS et al, 2023). Recently, Sugrue et al (2023) isolated two strains of Streptococcus equinus that produce a nisin variant, named nisin E. Specifically for Streptococcus equinus C6I9, used in our study, post-translational modification genes of the lantibiotic class of bacteriocins (lanB, lanC, lanM) were not detected, which may indicate that other lantibiotic post-translational modification genes are present or that the produced bioactive compound(s) belong(s) to other classes of peptides (SABINO et al, 2019).…”

Section: Discussionmentioning

confidence: 99%

Partial characterization of a bacteriocin-like inhibitory substance produced by Streptococcus equinus C6I9, a bovine rumen isolate.

Magalhães Júnior,

Fochat,

Húngaro

et al. 2023

CLIUM

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The present study aimed to evaluate the production and the factors that influence the antimicrobial activity of a bacteriocin-like inhibitory substance (BLIS) produced by Streptococcus equinus C6I9, a bovine rumen isolate. The antagonist activity was evaluated by the spot-on-lawn assay. Antimicrobial activity of the crude extracts obtained using NaCl acidic solution (pH 2, 100 mM) was evaluated along the bacterial growth and in growth medium containing different carbon and nitrogen sources, by agar diffusion method. Crude extract was evaluated regarding temperature stability, storage conditions, and pH sensitivity. S. equinus C619 inhibited both Gram-positive and Gram-negative strains. The crude extract was sensitive to proteinase K, and showed great stability to different temperatures and pH (2 to 12). The presence of meat extract (1.5 g/L) and sucrose (8 g/L) resulted in higher production of BLIS by S. equinus C6I9. The BLIS molecular mass was determined as approximately 3.5 kDa. The results obtained in this study evidenced the production of a broad spectrum activity, thermo- and pH stable BLIS by the ruminal isolate S. equinus C6I9, important features for its biotechnological application.

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“…Nisin belongs to class I bacteriocins (lantibiotics), and its main structure is linear with five‐ring structural domains (Figure 1a) (Gharsallaoui et al., 2016). There are 12 natural variants of nisin reported so far, namely nisin A, Z, F, Q, H, O, U, P, J, S, E, and G (Aldarhami et al., 2020; Lawrence et al., 2022; O'Sullivan et al., 2020; Sugrue et al., 2023; Wirawan et al., 2006; Zendo et al., 2003), among which nisin A and Z are the two most widely studied variants. By analyzing the characteristics, nisin A and Z have little difference in terms of thermal stability, resistance to pH changes, sensitivity to proteolytic enzymes, and antimicrobial spectrum, but nisin Z is more soluble than nisin A when the pH is close to neutral (Gharsallaoui et al., 2016).…”

Section: Species and Biosynthesis Of Nisinmentioning

confidence: 99%

Bacteriostasis of nisin against planktonic and biofilm bacteria: Its mechanism and application

Shi,

Wen,

Zhao

et al. 2024

Journal of Food Science

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Food safety incidents caused by bacterial contamination have always been one of the public safety issues of social concern. Planktonic cells, viable but non‐culturable (VBNC) cells, and biofilm cells of bacteria can coexist in food or food processing, posing more serious challenges to public health and safety by increasing bacterial survival and difficulty in detection. As a non‐toxic, no side effect, and highly effective bacteriostatic substance, nisin has received wide attention from researchers. In this review, we summarized the species and biosynthesis of nisin, the effects of nisin alone or in combination with other treatments on planktonic and biofilm cells, and its applications in the fields of food, feed, and medicine by consulting numerous studies. Meanwhile, the mechanism of nisin on planktonic and biofilm cells was proposed based on existing researches. Nisin not only has antibacterial activity against most G+ bacteria but also exhibits a bacteriostatic effect on G− bacteria when combined with other antibacterial treatments. In addition to planktonic cells, nisin also has significant effects on bacterial cells in biofilms by changing the thickness, density, and composition of biofilms. Based on the three action processes of nisin on biofilms, we summarized the changes of bacteria in biofilms, including the causes of bacterial death and the formation of the VBNC state. We consider that research on the relationship between nisin and VBNC state should be strengthened.

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Nisin E Is a Novel Nisin Variant Produced by Multiple Streptococcus equinus Strains

Cited by 7 publications

References 63 publications

Nisin S, a Novel Nisin Variant Produced by Ligilactobacillus salivarius P1CEA3

Nisin S, a Novel Nisin Variant Produced by Ligilactobacillus salivarius P1CEA3

Partial characterization of a bacteriocin-like inhibitory substance produced by Streptococcus equinus C6I9, a bovine rumen isolate.

Bacteriostasis of nisin against planktonic and biofilm bacteria: Its mechanism and application

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