A designed antimicrobial peptide with potential ability against methicillin resistant Staphylococcus aureus.

Staphylococcus aureus (S. aureus) is a Gram-positive pathogenic bacterium, which persistently colonizes the anterior nares of approximately 20-30% of the healthy adult population, and up to 60% is intermittently colonized. With the misuse and overuse of antibiotics, large-scale drug-resistant bacteria, including methicillin-resistant S. aureus (MRSA), have been appeared. MRSA is among the most prevalent pathogens causing community-associated infections. Once out of control, the number of deaths caused by antimicrobial resistance may exceed 10 million annually by 2050. Antimicrobial peptides (AMPs) are regarded as the best solution, for they are not easy to develop drug resistance. Based on our previous research, here we designed a new antimicrobial peptide named GW18, which showed excellent antimicrobial activity against S. aureus, even MRSA, with the hemolysis less than 5%, no cytotoxicity, and no acute toxicity. Notably, administration of GW18 significantly decreased S. aureus infection in mouse model. These findings identify GW18 as the ideal candidate against S. aureus infection.

Peptide OPTX-1 From Ornithodoros papillipes Tick Inhibits the pS273R Protease of African Swine Fever Virus.

African swine fever virus (ASFV) is a large double-stranded DNA virus and causes high mortality in swine. ASFV can be transmitted by biological vectors, including soft ticks in genus Ornithodoros but not hard ticks. However, the underlying mechanisms evolved in the vectorial capacity of soft ticks are not well-understood. Here, we found that a defensin-like peptide toxin OPTX-1 identified from Ornithodoros papillipes inhibits the enzyme activity of the ASFV pS273R protease with a Ki =0.821±0.526µM and shows inhibitory activity on the replication of ASFV. The analogs of OPTX-1 from hard ticks show more inhibitory efficient on pS273R protease. Considering that ticks are blood-sucking animals, we tested the effects of OPTX-1 and its analogs on the coagulation system. At last, top 3D structures represented surface analyses of the binding sites of pS273R with different inhibitors that were obtained by molecular docking based on known structural information. In summary, our study provides evidence that different inhibitory efficiencies between soft tick-derived OPTX-1 and hard tick-derived defensin-like peptides may determine the vector and reservoir competence of ticks.