Title Proteomic characterization of the outer membrane vesicle of the halophilic marine bacterium Novosphingobium pentaromativorans US6-1
Author Sung Ho Yun1, Sang-Yeop Lee1, Chi-Won Choi2, Hayoung Lee3, Hyun-Joo Ro1, Sangmi Jun1, Yong Min Kwon4, Kae Kyoung Kwon5, Sang-Jin Kim4,5, Gun-Hwa Kim1, and Seung Il Kim1,6
Address 1Drug and Disease Target Team, Korea Basic Science Institute, Daejeon 34133, Republic of Korea, 2Tunneling Nanotube Research Center, Division of Life Science, Korea University, Seoul 02841, Republic of Korea, 3Department of Bio-Analytical Science, University of Science and Technology (UST), Daejeon 34113, Republic of Korea, 4National Marine Biodiversity Institute of Korea, Seocheon 33662, Republic of Korea, 5Korea Institute of Ocean Science and Technology, Ansan 15627, Republic of Korea, 6National Marine Biodiversity Institute of Korea, Seocheon 33662, Republic of Korea, 5Korea Institute of Ocean Science and Technology, Ansan 15627, Republic of Korea
Bibliography Journal of Microbiology, 55(1),56-62, 2017,
DOI 10.1007/s12275-017-6581-6
Key Words Novosphingobium pentaromativorans, outer membrane vesicle, proteomics
Abstract Novosphingobium pentaromativorans US6-1 is a Gram-negative halophilic marine bacterium able to utilize several polycyclic aromatic hydrocarbons such as phenanthrene, pyrene, and benzo[a]pyrene. In this study, using transmission electron microscopy, we confirmed that N. pentaromativorans US6-1 produces outer membrane vesicles (OMVs). N. pentaromativorans OMVs (hereafter OMVNovo) are spherical in shape, and the average diameter of OMVNovo is 25–70 nm. Proteomic analysis revealed that outer membrane proteins and periplasmic proteins of N. pentaromativorans are the major protein components of OMVNovo. Comparative proteomic analysis with the membrane-associated protein fraction and correlation analysis demonstrated that the outer membrane proteins of OMVNovo originated from the membrane- associated protein fraction. To the best of our knowledge, this study is the first to characterize OMV purified from halophilic marine bacteria.