Lipopolysaccharide （LPS）, also termed endotoxin, is a main component of the external leaflet of the outer membrane （OM） in Gram-negative bacteria. It serves as a natural bar- rier against harsh environments and to...Lipopolysaccharide （LPS）, also termed endotoxin, is a main component of the external leaflet of the outer membrane （OM） in Gram-negative bacteria. It serves as a natural bar- rier against harsh environments and toxic compounds, in- cluding antibiotics, and partially confers drug-resistance in bacteria [1]. LPS is also a powerful activator of inflamma- tion and innate immune responses in mammalian cells. For the discovery of LPS receptor, Toll-like receptor 4 （TLR4）, Bruce A. Beutler won the Nobel Prize in Physiology or Medicine in 2011. As LPS is essential to most Gram- negative bacteria, intervening in LPS biogenesis offers great opportunities for developing novel antibiotics against path- ogens. However, for a long time, it is unclear how LPS is transported across the periplasm （the space between the inner and outer membranes） and assembled in the external leaflet of the OM in Gram-negative bacteria. With the funding support from the Ministry of Science and Technol- ogy of China, National Natural Science Foundation of Chi- na and the Strategic Priority Research Program of the Chi- nese Academy of Sciences, structural biologist Yihua Huang and his colleagues at the Institute of Biophysics, Chinese Academy of Sciences, recently determined the crystal structure of the LptD/E complex from the pathogen Shigella flexneri [2]. This new membrane protein complex structure provides crucial insights into an essential step of LPS biogenesis and also provides us a novel target for de- veloping new antibiotics against Gram-negative pathogens.展开更多
文摘Lipopolysaccharide （LPS）, also termed endotoxin, is a main component of the external leaflet of the outer membrane （OM） in Gram-negative bacteria. It serves as a natural bar- rier against harsh environments and toxic compounds, in- cluding antibiotics, and partially confers drug-resistance in bacteria [1]. LPS is also a powerful activator of inflamma- tion and innate immune responses in mammalian cells. For the discovery of LPS receptor, Toll-like receptor 4 （TLR4）, Bruce A. Beutler won the Nobel Prize in Physiology or Medicine in 2011. As LPS is essential to most Gram- negative bacteria, intervening in LPS biogenesis offers great opportunities for developing novel antibiotics against path- ogens. However, for a long time, it is unclear how LPS is transported across the periplasm （the space between the inner and outer membranes） and assembled in the external leaflet of the OM in Gram-negative bacteria. With the funding support from the Ministry of Science and Technol- ogy of China, National Natural Science Foundation of Chi- na and the Strategic Priority Research Program of the Chi- nese Academy of Sciences, structural biologist Yihua Huang and his colleagues at the Institute of Biophysics, Chinese Academy of Sciences, recently determined the crystal structure of the LptD/E complex from the pathogen Shigella flexneri [2]. This new membrane protein complex structure provides crucial insights into an essential step of LPS biogenesis and also provides us a novel target for de- veloping new antibiotics against Gram-negative pathogens.
