Author/Editor | Manček, Mateja; Pristovšek, Primož; Jerala, Roman | |
Title | Identification of LPS-binding peptide fragment of MD-2, a toll-receptor accessory protein | |
Type | članek | |
Source | Biochem Biophys Res Commun | |
Vol. and No. | Letnik 292, št. 4 | |
Publication year | 2002 | |
Volume | str. 880-5 | |
Language | eng | |
Abstract | Members of the toll-like receptor family are crucial in recognition of microbial pathogens as part of innate immune response. MD-2, an accessory protein to TLR4, present on the extracellular side of the membrane is needed to initiate the signal transduction. We have identified a 15 amino acid region of human MD-2 that contains several features of other lipopolysaccharide (LPS) binding proteins and peptides. In vitro LPS neutralization by this peptide was observed and confirmed by 2D transferred NOESY NMR experiments. NMR experiments have also shown binding of the MD-2 peptide to lipoteichoic acid (LTA) but not to peptidoglycan. Furthermore this peptide inhibited growth of gram-negative and to a lower extent of some gram-positive bacteria. Our results indicate that this region of MD-2 might be responsible for binding of LPS and confirms the role of MD-2 as an accessory protein in LPS signaling bestowing the Toll receptors their specificity. | |
Descriptors | PEPTIDE FRAGMENTS LIPOPOLYSACCHARIDES ANTIGENS, SURFACE TEICHOIC ACIDS SIGNAL TRANSDUCTION RECEPTORS, CELL SURFACE PROTEIN BINDING PEPTIDOGLYCAN MICROBIAL SENSITIVITY TESTS MEMBRANE GLYCOPROTEINS NUCLEAR MAGNETIC RESONANCE IMMUNITY, NATURAL BINDING SITES GRAM-NEGATIVE BACTERIA GRAM-POSITIVE BACTERIA |