Discovery of antimicrobial peptides clostrisin and cellulosin from Clostridium: insights into their structures, co-localized biosynthetic gene clusters, and antibiotic activity

• Moisés Alejandro Alejo Hernandez,
• Katia Pamela Villavicencio Sánchez,
• Rosendo Sánchez Morales,
• Karla Georgina Hernández-Magro Gil,
• David Silverio Moreno-Gutiérrez,
• Eddie Guillermo Sanchez-Rueda,
• Yanet Teresa-Cruz,
• Brian Choi,
• Armando Hernández Garcia,
• Alba Romero-Rodríguez,
• Oscar Juárez,
• Siseth Martínez-Caballero,
• Mario Figueroa and
• Corina-Diana Ceapă

Beilstein J. Org. Chem. 2024, 20, 1800–1816, doi:10.3762/bjoc.20.159

• associated bioactive peptides. Keywords: antimicrobials; genome mining; lantibiotics; lanthipeptides; multi-drug resistant bacteria; natural products; Introduction Antimicrobial resistance (AMR) is a significant public health challenge. Only in 2019, there were 4.95 million deaths associated with AMR [1

• Mycobacterium tuberculosis. The effects of some of these peptides are attributed to their affinity for the lipid II component of Gram-positive bacterial cell walls [25]. Additionally, there have been reports of lantibiotics such as CMB001 displaying activity against resistant Gram-negative bacteria, including

• antibiotics against drug-resistant pathogens. Although certain RiPPs with activity against Clostridia have been described [31], the characterization of complete gene clusters encoding for lantibiotics, using their native biosynthetic machinery and not that of nisin or of other non-native peptides, as well as

Cyclisation mechanisms in the biosynthesis of ribosomally synthesised and post-translationally modified peptides

• Andrew W. Truman

Beilstein J. Org. Chem. 2016, 12, 1250–1268, doi:10.3762/bjoc.12.120

• (alternatively named lantipeptides [44]) are large bacterial RiPPs, and the first member to be reported was nisin (Figure 4A) from Lactococcus lactis in 1928 [45]. Many members of this family have antibacterial activity and these are termed lantibiotics [46]; nisin itself is used as a food preservative as it

Natural product biosyntheses in cyanobacteria: A treasure trove of unique enzymes

• Jan-Christoph Kehr,
• Douglas Gatte Picchi and
• Elke Dittmann

Beilstein J. Org. Chem. 2011, 7, 1622–1635, doi:10.3762/bjoc.7.191

• antimicrobial activities (lantibiotics) [68]. Cyanobacteria were shown to frequently encode LanM type enzymes, i.e., bifunctional enzymes catalyzing both dehydration and cyclization reactions [68]. An interesting phenomenon was observed for the strain Prochlorococcus MIT9313, which is a single-celled planktonic