原创力文档vibrio cholerae proteome-wide screen for immunostimulatory proteins identifies phosphatidylserine decarboxylase as a novel toll-like receptor 4 agonist霍乱弧菌proteome-wide屏幕免疫刺激性蛋白质识别磷脂酰丝氨酸脱羧酶作为一种新颖的toll样受体4受体激动剂.pdfVIP
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vibrio cholerae proteome-wide screen for immunostimulatory proteins identifies phosphatidylserine decarboxylase as a novel toll-like receptor 4 agonist霍乱弧菌proteome-wide屏幕免疫刺激性蛋白质识别磷脂酰丝氨酸脱羧酶作为一种新颖的toll样受体4受体激动剂
Vibrio cholerae Proteome-Wide Screen for
Immunostimulatory Proteins Identifies
Phosphatidylserine Decarboxylase as a Novel Toll-Like
Receptor 4 Agonist
1 2 2 1 1,3,4
Ann Thanawastien , Wagner R. Montor , Joshua LaBaer , John J. Mekalanos , Sang Sun Yoon *
1 Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts, United States of America, 2 Harvard Institute of Proteomics,
Harvard Medical School, Cambridge, Massachusetts, United States of America, 3 Department of Microbiology and Immunology, University of Otago, Dunedin, New
Zealand, 4 Department of Microbiology, College of Medicine, Yonsei University, Seodaemun-gu, Seoul, Korea
Abstract
Recognition of conserved bacterial components provides immediate and efficient immune responses and plays a critical
role in triggering antigen-specific adaptive immunity. To date, most microbial components that are detected by host innate
immune system are non-proteinaceous structural components. In order to identify novel bacterial immunostimulatory
proteins, we developed a new high-throughput approach called ‘‘EPSIA’’, Expressed Protein Screen for Immune Activators.
Out of 3,882 Vibrio cholerae proteins, we identified phosphatidylserine decarboxylase (PSD) as a conserved bacterial protein
capable of activating host innate immunity. PSD in concentrations as low as 100 ng/ml stimulated RAW264.7 murine
macrophage cells and primary peritoneal macrophage cells to secrete TNFa and IL-6, respectively. PSD-induced
proinflammatory response was dependent on the presence of MyD88, a known adaptor molecule for innate i
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