Growth Suppression of a Gingivitis and Skin Pathogen Cutibacterium (Propionibacterium) acnes by Medicinal Plant Extracts.

Propionibacterium acnes, newly reclassified as Cutibacterium acnes, is an anaerobic Gram-positive bacterium causing acne, found mainly on the skin. In addition, P. acnes is responsible for inflammation of the gums (gingivitis) and blood vessels, consequently leading to various diseases in the human body. In recent years, the evolution of microorganisms, such as P. acnes, that have become resistant to many commercial antibiotics due to the widespread use of antimicrobial drugs in the treatment of infectious diseases has emerged as a major clinical problem. We here analyzed the potential use of 37 medicinal plant extracts as plausible candidates for treating P. acnes, in terms of total phenolic and flavonoid contents, antioxidants scavenging and antimicrobial activity. Consequently, methanol extracts from 14 medicinal plants showed promising antimicrobial activities against P. acnes. In particular, as the extracts from Chrysosplenium flagelliferum F. and Thuja orientalis L. exhibited distinct antimicrobial activities in both the broth dilution and disc diffusion assay, they could be effectively used as active ingredients for preventing or treating inflammatory periodontal diseases, such as periodontitis.

Soluble Expression and Efficient Purification of Recombinant Class I Hydrophobin DewA.

Hydrophobins are small proteins (<20 kDa) with an amphipathic tertiary structure that are secreted by various filamentous fungi. Their amphipathic properties provide surfactant-like activity, leading to the formation of robust amphipathic layers at hydrophilic-hydrophobic interfaces, which make them useful for a wide variety of industrial fields spanning protein immobilization to surface functionalization. However, the industrial use of recombinant hydrophobins has been hampered due to low yield from inclusion bodies owing to the complicated process, including an auxiliary refolding step. Herein, we report the soluble expression of a recombinant class I hydrophobin DewA originating from Aspergillus nidulans, and its efficient purification from recombinant Escherichia coli. Soluble expression of the recombinant hydrophobin DewA was achieved by a tagging strategy using a systematically designed expression tag (ramp tag) that was fused to the N-terminus of DewA lacking the innate signal sequence. Highly expressed recombinant hydrophobin DewA in a soluble form was efficiently purified by a modified aqueous two-phase separation technique using isopropyl alcohol. Our approach for expression and purification of the recombinant hydrophobin DewA in E. coli shed light on the industrial production of hydrophobins from prokaryotic hosts.