ArticleMicrobiology spectrum2022
LcCCL28-25, Derived from Piscine Chemokine, Exhibits Antimicrobial Activity against Gram-Negative and Gram-Positive Bacteria
Article in Microbiology spectrum, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Chemokines kill bacteria without triggering antimicrobial resistance by binding anionic phospholipids.Science advances · 2025Article
- Marine-derived new peptaibols with antibacterial activities by targeting bacterial membrane phospholipids.Acta pharmaceutica Sinica. B · 2025Article
- Therapeutic potential of isoallolithocholic acid in methicillin-resistant Staphylococcus Aureus peritoneal infection.The Journal of antibiotics · 2025Article
- Article
- Inhibition of the Growth ofMicroorganisms · 2024Article
- Identification and Functional Analysis ofGenes · 2023Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antimicrobial peptides (AMPs) are currently recognized as potentially promising antibiotic substitutes. Fish are an important seawater/freshwater medicinal biological resource, and the antimicrobial peptides and proteins that are key components of their innate immune systems are potential candidates for the development of novel antibacterial agents. The rainbow trout Oncorhynchus mykiss chemokine CK11 (omCK11), classified in the C-C motif chemokine ligand 27/28 (CCL27/28) family, is the only CC-type chemokine reported to play a direct antibacterial role in the immune response; however, its antibacterial domain remains unknown. In this study, we analyzed the structure-activity relationship of omCK11 and identified the antibacterial C-terminal domain. Additionally, we performed structure-function analyses of CCL27/28 proteins from different, representative freshwater and seawater fishes, revealing their shared C-terminal antibacterial domains. Surprisingly, a synthesized cationic peptide (named lcCCL28-25), derived from the large yellow croaker Larimichthys crocea CCL28, exhibited broad-spectrum and the most acceptable bactericidal activity, as well as antibiofilm activity and negligible hemolytic and cytotoxic activity
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Registered trials
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