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Report: Antibacterial activity of a peptide derived from HIV-1 MN strain gp41 envelope glycoprotein against
Sin-Yeang Teow1, Syed Atif Ali1
1Oncological and Radiological Sciences, Advanced Medical and Dental Institute (AMDI), Universiti Sains Malaysia (USM), Bertam, Kepala Batas, Pulau Pinang, Malaysia.
Abstract:
Peptides derived from HIV-1 transmembrane proteins have been extensively studied for antimicrobial activities, and they are known as antimicrobial peptides (AMPs). These AMPs have also been reported to potently combat the drug-resistant microbes. In this study, we demonstrated that peptide #6383 originated from HIV-1 MN strain membrane-spanning domain of gp41 was active (2-log reductions) at 100βg/mL (56.5βM) against methicillin-resistant Staphylococcus aureus (MRSA) in 10% and 50% human plasma-supplemented phosphate buffered saline (PBS). The activity was further enhanced (3-log reductions) in the presence of 5% human serum albumin (HSA) alone. All bactericidal activities were achieved within 6 hours. At 100μg/mL, the peptide showed only 13% toxicity against human erythrocytes. This peptide can serve as an attractive template for a design of a novel peptide antibiotic against drug-resistant bacteria. By sequence-specific engineering or modifications, we anticipated that the bactericidal activity and the reduced toxicity against human erythrocytes will be improved.
Insights
A novel antimicrobial peptide (AMP) derived from HIV-1 gp41 shows potent activity against drug-resistant MRSA. This peptide demonstrates low toxicity to human red blood cells, offering a promising template for new antibiotic development.
Area of Science:
- Microbiology
- Biochemistry
- Drug Discovery
Background:
- Antimicrobial peptides (AMPs) derived from HIV-1 transmembrane proteins exhibit significant antimicrobial properties.
- These AMPs are recognized for their potential to combat drug-resistant microbial strains.
Purpose of the Study:
- To evaluate the antimicrobial activity of peptide #6383, derived from the HIV-1 MN strain gp41.
- To assess the peptide's efficacy against methicillin-resistant Staphylococcus aureus (MRSA) in various human plasma concentrations.
- To determine the peptide's toxicity profile against human erythrocytes.
Main Methods:
- Peptide #6383 was tested against MRSA in phosphate-buffered saline (PBS) supplemented with 10% and 50% human plasma.
- The impact of human serum albumin (HSA) on peptide activity was investigated.
- Bactericidal activity was quantified by log reductions, and cytotoxicity was assessed using human erythrocytes.
Main Results:
- Peptide #6383 demonstrated a 2-log reduction in MRSA at 100 μg/mL in 10% and 50% human plasma.
- Activity increased to a 3-log reduction in the presence of 5% HSA.
- The peptide exhibited low toxicity, with only 13% erythrocyte lysis at 100 μg/mL.
Conclusions:
- Peptide #6383, derived from HIV-1 gp41, is a potent antimicrobial agent against MRSA.
- The peptide shows promising low toxicity to human erythrocytes.
- This peptide serves as a valuable template for developing novel peptide antibiotics against resistant bacteria.