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Review
. 2022 Jan 12;11(1):88.
doi: 10.3390/antibiotics11010088.

Antimicrobial Bacillus: Metabolites and Their Mode of Action

Charlie Tran  1 , Ian E Cock  2 , Xiaojing Chen  3 , Yunjiang Feng  1
Affiliations
Review

Antimicrobial Bacillus: Metabolites and Their Mode of Action

Charlie Tran et al. Antibiotics (Basel). .

Abstract

The agricultural industry utilizes antibiotic growth promoters to promote livestock growth and health. However, the World Health Organization has raised concerns over the ongoing spread of antibiotic resistance transmission in the populace, leading to its subsequent ban in several countries, especially in the European Union. These restrictions have translated into an increase in pathogenic outbreaks in the agricultural industry, highlighting the need for an economically viable, non-toxic, and renewable alternative to antibiotics in livestock. Probiotics inhibit pathogen growth, promote a beneficial microbiota, regulate the immune response of its host, enhance feed conversion to nutrients, and form biofilms that block further infection. Commonly used lactic acid bacteria probiotics are vulnerable to the harsh conditions of the upper gastrointestinal system, leading to novel research using spore-forming bacteria from the genus Bacillus. However, the exact mechanisms behind Bacillus probiotics remain unexplored. This review tackles this issue, by reporting antimicrobial compounds produced from Bacillus strains, their proposed mechanisms of action, and any gaps in the mechanism studies of these compounds. Lastly, this paper explores omics approaches to clarify the mechanisms behind Bacillus probiotics.

Keywords: Bacillus; animal feed; antimicrobials; omics; probiotic.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
The number of Bacillus strains reported for each species.
Figure 2
Figure 2
Metabolites targeting (a) cell wall and (b) plasma membrane.
Figure 3
Figure 3
Chemical structures of bacitracin A (1), bacilysin (2), chlorotetaine (3), and kanosamine (4).
Figure 4
Figure 4
Chemical structures of subtilin (5), clausin (6), mersacidin (7), amylolysin A (8), and haloduracin (9).
Figure 5
Figure 5
Chemical structures of ε-poly-L-Lysine (10), plantazolicin (11), octapeptin B (12), aurantinin B (13), aurantinin C (14), aurantinin (D) (15), myriocin (16), gramicidin A (17), and gramicidin S (18).
Figure 6
Figure 6
Chemical structures of surfactin A–C (19–21), lichenysin (22), and fengycin A–D (23–26).
Figure 7
Figure 7
Chemical structures of iturin A (27), bacillomycin D (28), bacillomycin L (29), and mycosubtilin (30).
Figure 8
Figure 8
Chemical structures of mycobacillin (31) and subtilosin A (32).
Figure 9
Figure 9
Chemical structures of zwittermicin A (33), difficidin (34), and sublancin (35).
Figure 10
Figure 10
Chemical structures of amicoumacin A (36), prumycin (37), thiocillin (38), hetiamacin E (39), hetiamacin F (40), rhizocticin A (41), macrolactin N (42), and azoxybacilin (43).
Figure 11
Figure 11
Chemical structures of stigmatellin Y (44), bacillaene (45), bacillibactin (46), and schizokinen (47).
Figure 12
Figure 12
The analysis of (a) the number of strains in each species and the (b) mechanism of action targeted by each strain.
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