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소 장관 유래 Enterococcus faecium의 Enterobacter sakazakii에 대한 생육저해활성
박주희,윤성식,박영서,Park, Ju-Hui,Yoon, Sung-Sik,Park, Young-Seo 한국축산식품학회 2008 한국축산식품학회지 Vol.28 No.1
A lactic acid bacterium showing growth inhibitory activity against Enterobacter sakazakii was isolated from bovine intestinal tracts. From biochemical and molecular biological studies, the isolate was identified and named as Enterococcus faecium JH95. This strain was resistant to kanamycin and streptomycin at a concentration of $100{\mu}g/mL$. E. faecium JH95 had high antimicrobial activity against food-borne pathogens such as Escherichia coli O157:H7, Listeria monocytogenes, Salmonella typhimurium, Staphylococcus aureus, and Clostridium perfrigens. The culture supernatant of this strain did not have antimicrobial activity. The culture broth of this strain failed to show the antimicrobial activity by heat treatment at $100^{\circ}C$ for 5 min or by pretense treatments for 2 hr. This result suggested that the putative antimicrobial substance produced by E. faecium JH95 is likely a protein which is not secreted into culture medium.
원형질막에서 약한 막결합부위와 PI(4,5)P₂결합에 의한 Membrane Blebbing 형성
박주희(Ju-Hui Park),박상원(Sang-Won Park),이진아(Jin-A Lee),장덕진(Deok-Jin Jang) 한국생물공학회 2019 KSBB Journal Vol.34 No.4
Plasma membrane blebs are dynamic cellular cytoskeleton remodeling events involved in apoptosis and cell movement. Phosphoinositide (PI) is one of the phospholipid components within inner leaflet of the plasma membrane, but the contribution of PI on membrane blebbing remains elusive. Here, we found that if the phosphatidylinositol-4-phosphate (PI4P)-specific binding pleckstrin homology (PH) domain of various proteins including OSBP, OSH1, or OSH2 was combined with the N-terminal hydrophobic domain of Aplysia phosphodiesterase 4 short-form (S(N30)), membrane blebbing occurred on the plasma membrane. However, unexpectedly, this membrane blebbing was mediated by phosphatidylinositol 4,5-bisphosphate (PI(4,5)P₂) binding rather than PI4P binding. To further elucidate this, we combined S(N30) with selective PI(4,5)P₂ binding PLCδ1 PH domain (S(N30)-GFP-PH(PLCδ1)), selective phosphatidylinositol 3,4,5-bisphosphate (PI(3,4,5)P₃) binding AKT1 PH domain (S(N30)-GFP-PH(AKT1)), or selective PS binding Lact-C2 domain (S(N30)-GFP-Lact-C2). Interestingly, overexpression of S(N30)-GFP-PH(PLCδ1) but not S(N30)-GFP-PH(AKT1) or S(N30)-GFP-Lact-C2 could strongly induce membrane blebbing. Our results clearly indicate that impairment of PI(4,5)P₂ binding in the plasma membrane is associated with cellular process of the plasma membrane blebbing.