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Development of novel antimicrobial peptides derived from anti-lipopolysaccharide factor of the swimming crab, Portunus trituberculatus
- Source :
- Fish & Shellfish Immunology. 84:664-672
- Publication Year :
- 2019
- Publisher :
- Elsevier BV, 2019.
-
Abstract
- Anti-lipopolysaccharide factors (ALFs) are a representative host defense protein in crustaceans. In this study, we successfully developed two novel antimicrobial peptides (AMPs), named crab-ALF2A and crab-ALF6A, which contain changes to the amino acid sequences of the lipopolysaccharide binding domain and signal peptide, respectively, of the ALF of the swimming crab Portunus trituberculatus. The crab-ALF2A peptide showed potent antimicrobial activity against the Gram-positive bacteria Bacillus cereus, Staphylococcus aureus, and Streptococcus iniae (minimal effective concentration [MEC] 1.51–1.93 μg/mL) and the Gram-negative bacteria Pseudomonas aeruginosa and Escherichia coli (MEC 1.87–1.98 μg/mL), with maximal bactericidal activity at a peptide concentration of 5 μg/mL. The crab-ALF6A peptide also showed potent antimicrobial activity against B. cereus, S. aureus, and S. iniae (MEC 1.49–2.3 μg/mL) and P. aeruginosa and E. coli (MEC 1.72–1.19 μg/mL) at a peptide concentration of 5 μg/mL. Notably, the crab-ALF2A and crab-ALF6A peptides exhibited strong activity against Candida albicans (MECs of 2.11 and 1.95 μg/mL, respectively). These activities were stable following heat treatment. Moreover, the effect of crab-ALF2A and crab-ALF6A peptide treatment on microbe cell morphology was confirmed by scanning electron microscopy. Membrane disruption and damage, and the leakage of cytoplasmic content were clearly observed. A downsizing peptide approach illustrated that the hexapeptide ALF6A8 (RVLLRL) was the shortest peptide showing significant antimicrobial activity. Our approach allows for the generation of novel antimicrobial peptides in a cost effective manner as potential next-generation antibiotics.
- Subjects :
- 0301 basic medicine
Signal peptide
animal structures
Brachyura
Antimicrobial peptides
Bacillus cereus
Peptide
Aquatic Science
Gram-Positive Bacteria
Cell morphology
Arthropod Proteins
Microbiology
03 medical and health sciences
Anti-Infective Agents
Gram-Negative Bacteria
Animals
Environmental Chemistry
Amino Acid Sequence
chemistry.chemical_classification
biology
04 agricultural and veterinary sciences
General Medicine
Portunus trituberculatus
Antimicrobial
biology.organism_classification
Lipopolysaccharide binding
body regions
030104 developmental biology
chemistry
040102 fisheries
0401 agriculture, forestry, and fisheries
Antimicrobial Cationic Peptides
Subjects
Details
- ISSN :
- 10504648
- Volume :
- 84
- Database :
- OpenAIRE
- Journal :
- Fish & Shellfish Immunology
- Accession number :
- edsair.doi.dedup.....30fa5151c0e81c83a3c429369bc0c5dc