The diversification of the antimicrobial peptides from marine worms is driven by environmental conditions

Bruno, Rosa‐Maria; Boidin-Wichlacz, Céline; Melnyk, Oleg; Zeppilli, Daniela; Landon, C.; Thomas, Fréderic; Cambon, Marie-Anne; Lafond, Mickaël; Mabrouk, Kamel; Massol, François; Hourdez, Stéphane; Maresca, Marc; Jollivet, Didier; Tasiemski, Aurélie

doi:10.1016/j.scitotenv.2023.162875

Cited by 9 publications

(10 citation statements)

References 71 publications

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“…Our recent results [9] and the data obtained by Bruno et al [10] have demonstrated that, in polychaetes, the BRICHOS domain might be involved in the biosynthesis of AMPs of different structural classes and not only of β-hairpin molecules. Interestingly, a detailed analysis of the A. marina transcriptome revealed two novel types of Cys-rich BRICHOSrelated peptides designated as AmIMP1 and AmIMP2 (Integral Membrane Proteins) [11].…”

Section: Introductionsupporting

confidence: 64%

“…After digestion, we did not observe two terminal parts of HfBRI-25 that pointed at the absence of C1-C2/C3-C4 pairing type. Expectedly, the major product peaks appearing in the HPLC chromatogram (peaks 2 and 3, Figure S2) corresponded to two linear fragments (4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16) and (19/20-25) connected by two disulfide bonds. Therefore, the β-hairpin structure with the pairing type C1-C4/C2-C3 is the most probable, which agrees well with the AlphaFold prediction data (Figure 2B and Figure S3).…”

Section: Production and Structural Analysis Of Novel Peptides Hfbri-2...mentioning

confidence: 99%

“…Interestingly, a single structural family of such peptides have been described for each species: β-hairpin arenicins from A. marina [2,4], β-hairpin abarenicins from Abarenicola pacifica [5], β-hairpin alvinellacins from sister species Alvinella pompejana [6] and A. caudata [7], β-hairpin capitellacin from Capitella teleta [8], α-helical nicomicins bearing a Cterminal loop stabilized by a disulfide bridge from Nicomache minor [9], α-helical (or dimeric β-sheet, exact structure is unknown) polaricin from Amphitritides sp. [10]. First described BRICHOS-related AMPs arenicins and alvinellacin have been directly isolated from the coelomocytes or coelomic liquid of animals [2,6].…”

Section: Introductionmentioning

confidence: 99%

“…Direct peptide isolation is a challenge due to the labor-consuming process of catching small solitary animals followed by the fine purification of peptides from immune cells and body fluids. Therefore, the in silico blasting of known sequences of various AMPs and their preprosequences in genome/transcriptome databases [5,6,8,10] or the RACE-based approach [9] were used to identify novel BRICHOSrelated AMPs in further studies.…”

Section: Introductionmentioning

confidence: 99%

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Novel BRICHOS-Related Antimicrobial Peptides from the Marine Worm Heteromastus filiformis: Transcriptome Mining, Synthesis, Biological Activities, and Therapeutic Potential

Panteleev,

Safronova,

Duan

et al. 2023

Marine Drugs

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Marine polychaetes represent an extremely rich and underexplored source of novel families of antimicrobial peptides (AMPs). The rapid development of next generation sequencing technologies and modern bioinformatics approaches allows us to apply them for characterization of AMP-derived genes and the identification of encoded immune-related peptides with the aid of genome and transcriptome mining. Here, we describe a universal bioinformatic approach based on the conserved BRICHOS domain as a search query for the identification of novel structurally unique AMP families in annelids. In this paper, we report the discovery of 13 novel BRICHOS-related peptides, ranging from 18 to 91 amino acid residues in length, in the cosmopolitan marine worm Heteromastus filiformis with the assistance of transcriptome mining. Two characteristic peptides with a low homology in relation to known AMPs—the α-helical amphiphilic linear peptide, consisting of 28 amino acid residues and designated as HfBRI-28, and the 25-mer β-hairpin peptide, specified as HfBRI-25 and having a unique structure stabilized by two disulfide bonds—were obtained and analyzed as potential antimicrobials. Interestingly, both peptides showed the ability to kill bacteria via membrane damage, but mechanisms of their action and spectra of their activity differed significantly. Being non-cytotoxic towards mammalian cells and stable to proteolysis in the blood serum, HfBRI-25 was selected for further in vivo studies in a lethal murine model of the Escherichia coli infection, where the peptide contributed to the 100% survival rate in animals. A high activity against uropathogenic strains of E. coli (UPEC) as well as a strong ability to kill bacteria within biofilms allow us to consider the novel peptide HfBRI-25 as a promising candidate for the clinical therapy of urinary tract infections (UTI) associated with UPEC.

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Section: Introductionsupporting

confidence: 64%

Section: Production and Structural Analysis Of Novel Peptides Hfbri-2...mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Novel BRICHOS-Related Antimicrobial Peptides from the Marine Worm Heteromastus filiformis: Transcriptome Mining, Synthesis, Biological Activities, and Therapeutic Potential

Panteleev,

Safronova,

Duan

et al. 2023

Marine Drugs

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“…The identified AMPs are alvinellacin (ALV), arenicin (ARE), and polaricin (POL—the novel AMP). All three of the AMPs show bactericidal activity against the bacteria typical of the habitat [ 58 ].…”

Section: Amps From Animalsmentioning

confidence: 99%

Diversity and Mechanisms of Action of Plant, Animal, and Human Antimicrobial Peptides

Satchanska,

Davidova,

Gergova

2024

Antibiotics

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Antimicrobial peptides (AMPs) are usually made up of fewer than 100 amino acid residues. They are found in many living organisms and are an important factor in those organisms’ innate immune systems. AMPs can be extracted from various living sources, including bacteria, plants, animals, and even humans. They are usually cationic peptides with an amphiphilic structure, which allows them to easily bind and interact with the cellular membranes of viruses, bacteria, fungi, and other pathogens. They can act against both Gram-negative and Gram-positive pathogens and have various modes of action against them. Some attack the pathogens’ membranes, while others target their intracellular organelles, as well as their nucleic acids, proteins, and metabolic pathways. A crucial area of AMP use is related to their ability to help with emerging antibiotic resistance: some AMPs are active against resistant strains and are susceptible to peptide engineering. This review considers AMPs from three key sources—plants, animals, and humans—as well as their modes of action and some AMP sequences.

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A 14-amino acid cationic peptide Bolespleenin334-347 from the marine fish mudskipper Boleophthalmus pectinirostris exhibiting potent antimicrobial activity and therapeutic potential

Bai,

Zhang,

Zheng

et al. 2024

Biochemical Pharmacology

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The diversification of the antimicrobial peptides from marine worms is driven by environmental conditions

Cited by 9 publications

References 71 publications

Novel BRICHOS-Related Antimicrobial Peptides from the Marine Worm Heteromastus filiformis: Transcriptome Mining, Synthesis, Biological Activities, and Therapeutic Potential

Novel BRICHOS-Related Antimicrobial Peptides from the Marine Worm Heteromastus filiformis: Transcriptome Mining, Synthesis, Biological Activities, and Therapeutic Potential

Diversity and Mechanisms of Action of Plant, Animal, and Human Antimicrobial Peptides

A 14-amino acid cationic peptide Bolespleenin334-347 from the marine fish mudskipper Boleophthalmus pectinirostris exhibiting potent antimicrobial activity and therapeutic potential

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