Recognition of lipopolysaccharide pattern by TLR4 complexes

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Lipopolysaccharide (LPS) is a major component of the outer membrane of Gram-negative bacteria. Minute amounts of LPS released from infecting pathogens can initiate potent innate immune responses that prime the immune system against further infection. However, when the LPS response is not properly controlled it can lead to fatal septic shock syndrome. The common structural pattern of LPS in diverse bacterial species is recognized by a cascade of LPS receptors and accessory proteins, LPS binding protein (LBP), CD14 and the Toll-like receptor4 (TLR4)-MD-2 complex. The structures of these proteins account for how our immune system differentiates LPS molecules from structurally similar host molecules. They also provide insights useful for discovery of anti-sepsis drugs. In this review, we summarize these structures and describe the structural basis of LPS recognition by LPS receptors and accessory proteins.
Publisher
NATURE PUBLISHING GROUP
Issue Date
2013-12
Language
English
Article Type
Review
Keywords

TOLL-LIKE RECEPTOR-3; INNATE IMMUNE RECOGNITION; MONOPHOSPHORYL-LIPID-A; GRAM-NEGATIVE BACTERIA; DOUBLE-STRANDED-RNA; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; SIGNAL-TRANSDUCTION; TIR-DOMAIN; ANTAGONIST ERITORAN

Citation

EXPERIMENTAL AND MOLECULAR MEDICINE, v.45, no.12, pp.1 - 8

ISSN
1226-3613
DOI
10.1038/emm.2013.97
URI
http://hdl.handle.net/10203/187434
Appears in Collection
CH-Journal Papers(저널논문)
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