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SMAP-29: a potent antibacterial and antifungal peptide from sheep leukocytes
B Skerlavaj1, M Benincasa, A Risso
1Dipartimento di Scienze e Tecnologie Biomediche, Università di Udine, 33100, Udine, Italy.
Abstract:
SMAP-29 is a cathelicidin-derived peptide deduced from sheep myeloid mRNA. The C-terminally amidated form of this peptide was chemically synthesized and shown to exert a potent antimicrobial activity. Antibiotic-resistant clinical isolates highly susceptible to this peptide include MRSA and VREF isolates, that are a major worldwide problem, and mucoid Pseudomonas aeruginosa associated with chronic respiratory inflammation in CF patients. In addition, SMAP-29 is also active against fungi, including Cryptococcus neoformans isolated from immunocompromised patients. SMAP-29 causes significant morphological alterations of the bacterial surfaces, as shown by scanning electron microscopy, and is also hemolytic against human, but not sheep erythrocytes. Its potent antimicrobial activity suggests that this peptide is an excellent candidate as a lead compound for the development of novel antiinfective agents.
Insights
Sheep cathelicidin-derived peptide SMAP-29 shows potent antimicrobial activity against antibiotic-resistant bacteria like MRSA and fungi. This peptide is a promising lead for developing new anti-infective agents.
Area of Science:
- Biochemistry
- Microbiology
- Pharmacology
Background:
- Cathelicidins are antimicrobial peptides with diverse biological activities.
- Antibiotic resistance is a growing global health concern, necessitating novel therapeutic strategies.
- Sheep myeloid antimicrobial peptide-29 (SMAP-29) is a synthetic peptide derived from sheep cathelicidin.
Purpose of the Study:
- To synthesize and characterize the antimicrobial and hemolytic activities of SMAP-29.
- To evaluate the efficacy of SMAP-29 against clinically relevant antibiotic-resistant pathogens and fungi.
- To investigate the mechanism of action of SMAP-29 on bacterial surfaces.
Main Methods:
- Chemical synthesis of C-terminally amidated SMAP-29.
- Antimicrobial susceptibility testing against various bacterial and fungal isolates, including MRSA, VREF, Pseudomonas aeruginosa, and Cryptococcus neoformans.
- Scanning electron microscopy (SEM) to visualize morphological changes on bacterial surfaces.
- Hemolytic assays using human and sheep erythrocytes.
Main Results:
- SMAP-29 demonstrated potent antimicrobial activity against methicillin-resistant Staphylococcus aureus (MRSA), vancomycin-resistant Enterococcus faecium (VREF), and mucoid Pseudomonas aeruginosa.
- The peptide was also effective against Cryptococcus neoformans, a fungal pathogen.
- SEM revealed significant alterations in bacterial surface morphology upon SMAP-29 treatment.
- SMAP-29 exhibited hemolytic activity against human erythrocytes but not sheep erythrocytes.
Conclusions:
- SMAP-29 possesses broad-spectrum antimicrobial activity against challenging pathogens.
- The peptide's ability to disrupt bacterial surfaces suggests a unique mechanism of action.
- SMAP-29 represents a promising lead compound for the development of novel anti-infective therapies.